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13-OH-chlorophyll a + H2O
phytol + 13-OH-chlorophyllide a
-
in varieties Hojiblanca and Picual
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
-
?
bacteriochlorophyll + H2O
?
bacteriochlorophyll + H2o
bacteriochlorophyllide + phytol
-
-
-
?
bacteriochlorophyll a + H2O
bacteriochlorophyllide a + phytol
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
bacteriochlorophyll a + Triton X-100 + H2O
bacteriochlorophyllide a tritonyl ester
-
-
-
?
chlorobium chlorophyll + H2O
?
-
-
-
-
ir
chlorophyll + H2O
chlorophyllide + ?
chlorophyll + H2O
chlorophyllide + phytol
chlorophyll + H2O
phytol + chlorophyllide
chlorophyll a + CH3OH + phytol
methylchlorophyllide + ?
-
-
-
?
chlorophyll a + H2O
?
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
chlorophyll a + H2O
phytol + chlorophyllide
chlorophyll a + H2O
phytol + chlorophyllide a
chlorophyll a + Triton X-100 + H2O
chlorophyllide a tritonyl ester
-
-
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
chlorophyll aXXX ester + alcohol
chlorophyllide a(alcohol) + phytol
-
-
-
?
chlorophyll b + H2O
?
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
chlorophyll b + H2O
phytol + chlorophyllide
-
stereospecific for the substrate, no activity with the C13-epimer
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
chlorophyllide a + phytol
chlorophyll a + H2O
-
-
-
r
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl decanoate + H2O
p-nitrophenol + decanoate
-
-
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + palmitate
-
-
-
-
?
pheophorbide a methyl ester + H2O
?
-
-
-
?
pheophytin + H2O
?
-
-
-
-
?
pheophytin + H2O
pheophorbide + ?
-
-
-
-
?
pheophytin + H2O
phytol + pheophorbide
-
-
-
?
pheophytin a + H2O
?
-
-
-
-
ir
pheophytin a + H2O
pheophorbide a + phytol
-
-
-
?
pheophytin a + H2O
phytol + pheophorbide
pheophytin b + H2O
?
-
-
-
-
ir
pheophytin b + H2O
? + phytol
-
-
-
?
pheophytin b + H2O
phytol + pheophorbide
-
-
-
?
pyrobacteriochlorophyll a + Triton X-100 + H2O
pyrobacteriochlorophyllide a tritonyl ester
-
-
-
?
pyrochlorophyll a + Triton X-100 + H2O
pyrochlorophyllide a tritonyl ester + phytol
-
-
-
?
additional information
?
-
bacteriochlorophyll + H2O
?
-
-
-
-
?
bacteriochlorophyll + H2O
?
-
-
-
-
ir
bacteriochlorophyll + H2O
?
-
hydrolyzes bacteriochlorophyll isolated from Rhodospirillum rubrum, but not the pigment bound to the membrane of chromatophores or spheroplasts from the bacterium. Acetone enables the enzyme to hydrolyze the bound pigment
-
-
?
bacteriochlorophyll + H2O
?
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
preferred substrate
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A1X0M486
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A031JJ58
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0X3WMQ3
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0B6FPX1
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0B6FPX1
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
chlorophyll + H2O
chlorophyllide + ?
-
-
-
-
?
chlorophyll + H2O
chlorophyllide + ?
-
-
-
-
?
chlorophyll + H2O
chlorophyllide + ?
-
-
-
?
chlorophyll + H2O
chlorophyllide + ?
-
-
-
-
?
chlorophyll + H2O
chlorophyllide + ?
-
-
-
-
?
chlorophyll + H2O
chlorophyllide + phytol
-
-
-
-
ir
chlorophyll + H2O
chlorophyllide + phytol
-
-
-
-
ir
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
isozyme AtCLH1 is not essential for chlorophyll breakdown during plant senescence, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
isozyme AtCLH2 is not essential for chlorophyll breakdown during plant senescence, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
the enzyme is involved in the first step of chlorophyll degradation, molecular regulation of in vivo activities, AtCLH2 might play a distinctive role in chlorophyll catabolism in vivo, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
removal of the lipophilic phytol moiety of chlorophyll
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
chlorophyllase is the first enzyme in the degradation pathway of chlorophyll, resulting in postharvest yellowing in broccoli
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
chlorophyllase is the first enzyme in the degradation pathway of chlorophyll, resulting in postharvest yellowing in broccoli, CLH1 is expressed during the course of broccoli postharvest senescence
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
substrate ethanol-dissolved Chl a from Anacystis nidulans algae
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
Chlase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated, it catalyzes the cleavage of the hydrophobic thylakoid-anchoring phytol chain of chlorophyll from the porphyrin ring, resulting in the product chlorophyllide, which retains the typical green color, chlorophyll catabolic pathway, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
chlorophyll from spinach leaves
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
the first enzyme in the chlorophyll degradation pathway in vivo catalyzes the hydrolysis of chlorophylls and pheophytins into their hydrophilic chromophore moieties chlorophyllides and pheophorbides, respectively
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
chlorophyll from Spinacia oleracea
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
no gender-specific changes in chlorophyllase activity is response to low temperature stress, however, male plants show higher chlorophyll a/b ratio than female plants, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
chlorophyllase catalyzes the initial hydrolysis of the phytol moiety from the pigment in the degradation of chlorophyll, overview
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
hydrolyzes the a, i.e.132R form but not the a', i.e.132S form
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
-
r
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
?
chlorophyll a + H2O
chlorophyllide a + phytol
-
-
-
-
ir
chlorophyll a + H2O
phytol + chlorophyllide
-
best substrate, stereospecific for the substrate, no activity with the C13-epimer
-
?
chlorophyll a + H2O
phytol + chlorophyllide
chlorophyll a substrate from Petroselinum sativum leaves
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
preferred substrate
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_010934773
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_008355440
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
chlorophyllide a production occurs only in variety Arbequina
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_008235366
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_010326690
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
-
specific for
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
-
the enzyme is involved in the regulation of chlorophyll a and b content
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
hydrolyzes the a, i.e. 132R form but not the a', i.e.132S form
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
-
-
-
?
chlorophyll b + H2O
chlorophyllide b + phytol
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
chlorophyll b is recognized and degraded with greater efficiency than chlorophyll a
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
pheophytin a + H2O
phytol + pheophorbide
-
-
-
?
pheophytin a + H2O
phytol + pheophorbide
-
in varieties Hojiblanca and Picual
-
?
additional information
?
-
-
no activity with 4-nitrophenyl esters of fatty acids and tributyrin
-
?
additional information
?
-
-
reactions in the off-line format are performed in PCR-type microtubes, micellar electrokinetic chromatography (MEKC) assay, method, detailed overview
-
-
?
additional information
?
-
-
the enzyme participates in the phytyl ester formation in the final step of chlorophyll biosynthesis
-
-
?
additional information
?
-
-
first stage in the enzymic breakdown of chlorophyll in vivo may be the removal of the phytol side chain by chlorophyllase
-
-
?
additional information
?
-
isoform CLH1 preferably hydrolyzes Mg-free chlorophyll
-
-
?
additional information
?
-
isoform CLH1 preferably hydrolyzes Mg-free chlorophyll
-
-
?
additional information
?
-
isoform CLH1 preferably hydrolyzes Mg-free chlorophyll
-
-
?
additional information
?
-
-
isoform CLH1 preferably hydrolyzes Mg-free chlorophyll
-
-
?
additional information
?
-
isoform CLH2 hydrolyzes both chlorophyll and Mg-free chlorophyll at a similar level
-
-
?
additional information
?
-
isoform CLH2 hydrolyzes both chlorophyll and Mg-free chlorophyll at a similar level
-
-
?
additional information
?
-
isoform CLH2 hydrolyzes both chlorophyll and Mg-free chlorophyll at a similar level
-
-
?
additional information
?
-
-
isoform CLH2 hydrolyzes both chlorophyll and Mg-free chlorophyll at a similar level
-
-
?
additional information
?
-
isoform CLH3 shows very low Chlase activity
-
-
?
additional information
?
-
isoform CLH3 shows very low Chlase activity
-
-
?
additional information
?
-
isoform CLH3 shows very low Chlase activity
-
-
?
additional information
?
-
-
isoform CLH3 shows very low Chlase activity
-
-
?
additional information
?
-
key enzyme in chlorophyll degradation
-
-
?
additional information
?
-
-
key enzyme in chlorophyll degradation
-
-
?
additional information
?
-
recombinant CrCLH1 has a higher catalytic efficiency for chlorophyll a than for chlorophyll b and bacteriochlorophyll a. Recombinant CrCLH1 catalyzes the conversion of chlorophyll a to pheophorbide a at pH 5.0
-
-
?
additional information
?
-
-
recombinant CrCLH1 has a higher catalytic efficiency for chlorophyll a than for chlorophyll b and bacteriochlorophyll a. Recombinant CrCLH1 catalyzes the conversion of chlorophyll a to pheophorbide a at pH 5.0
-
-
?
additional information
?
-
-
autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
-
-
?
additional information
?
-
enzyme substrate specificity, overview. Recombinant CyanoCLH prefers hydrolyzing bacteriochlorophyll a to produce bacteriochlorophyllide a (BChlide a), which can be converted to bacteriopheophorbide a by removing magnesium ion
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in CN1927 exhibits a higher substrate preference toward chlorophyll (Chl) b than Chl a
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in CN1927 exhibits a higher substrate preference toward chlorophyll (Chl) b than Chl a
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in CN1927 exhibits a higher substrate preference toward chlorophyll (Chl) b than Chl a
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar CYY8467 exhibits a higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar CYY8467 exhibits a higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar CYY8467 exhibits a higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar TN57 exhibits a slightly higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar TN57 exhibits a slightly higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
substrate specificities of isozymes from different cultivars, overview. Chlorophyllase (Chl) activity in cultivar TN57 exhibits a slightly higher substrate preference toward chlorophyll (Chl) a than Chl b
-
-
?
additional information
?
-
-
the enzyme acts preferentially with compounds having the isocyclic carbomethoxy and C-17 propionic residue facing opposite sides of the pyorphyrin macrocycle
-
-
?
additional information
?
-
-
no activity with chlorophyll b in all variants
-
?
additional information
?
-
-
autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
-
-
?
additional information
?
-
-
immobilized enzyme shows a higher affinity towards chlorophyll than pheophytin as substrate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme acts preferentially with compounds having the isocyclic carbomethoxy and C-17 propionic residue facing opposite sides of the pyorphyrin macrocycle
-
-
?
additional information
?
-
-
since chlorophyll degradation is a defining feature of plant senescence, compounds inhibiting chlorophyllase activity may delay senescence, thereby improving shelf life and appearance of plant products
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
13-OH-chlorophyll a + H2O
phytol + 13-OH-chlorophyllide a
-
in varieties Hojiblanca and Picual
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
chlorophyll + H2O
chlorophyllide + phytol
-
-
-
-
ir
chlorophyll + H2O
phytol + chlorophyllide
chlorophyll a + H2O
phytol + chlorophyllide a
chlorophyll a/b + H2O
phytol + chlorophyllide
chlorophyll b + H2O
phytol + chlorophyllide b
pheophytin a + H2O
phytol + pheophorbide
-
in varieties Hojiblanca and Picual
-
?
additional information
?
-
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
preferred substrate
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A1X0M486
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A031JJ58
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0X3WMQ3
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0B6FPX1
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
A0A0B6FPX1
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
bacteriochlorophyll a + H2O
phytol + bacteriochlorophyllide a
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
isozyme AtCLH1 is not essential for chlorophyll breakdown during plant senescence, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
isozyme AtCLH2 is not essential for chlorophyll breakdown during plant senescence, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
the enzyme is involved in the first step of chlorophyll degradation, molecular regulation of in vivo activities, AtCLH2 might play a distinctive role in chlorophyll catabolism in vivo, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
chlorophyllase is the first enzyme in the degradation pathway of chlorophyll, resulting in postharvest yellowing in broccoli
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
chlorophyllase is the first enzyme in the degradation pathway of chlorophyll, resulting in postharvest yellowing in broccoli, CLH1 is expressed during the course of broccoli postharvest senescence
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
Chlase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated, it catalyzes the cleavage of the hydrophobic thylakoid-anchoring phytol chain of chlorophyll from the porphyrin ring, resulting in the product chlorophyllide, which retains the typical green color, chlorophyll catabolic pathway, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
the first enzyme in the chlorophyll degradation pathway in vivo catalyzes the hydrolysis of chlorophylls and pheophytins into their hydrophilic chromophore moieties chlorophyllides and pheophorbides, respectively
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
no gender-specific changes in chlorophyllase activity is response to low temperature stress, however, male plants show higher chlorophyll a/b ratio than female plants, overview
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll + H2O
phytol + chlorophyllide
-
chlorophyllase catalyzes the initial hydrolysis of the phytol moiety from the pigment in the degradation of chlorophyll, overview
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_010934773
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_008355440
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
chlorophyllide a production occurs only in variety Arbequina
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_008235366
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
XP_010326690
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a + H2O
phytol + chlorophyllide a
-
-
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
-
the enzyme is involved in the regulation of chlorophyll a and b content
-
?
chlorophyll a/b + H2O
phytol + chlorophyllide
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
chlorophyll b is recognized and degraded with greater efficiency than chlorophyll a
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
chlorophyll b + H2O
phytol + chlorophyllide b
-
-
-
-
?
additional information
?
-
-
the enzyme participates in the phytyl ester formation in the final step of chlorophyll biosynthesis
-
-
?
additional information
?
-
-
first stage in the enzymic breakdown of chlorophyll in vivo may be the removal of the phytol side chain by chlorophyllase
-
-
?
additional information
?
-
key enzyme in chlorophyll degradation
-
-
?
additional information
?
-
-
key enzyme in chlorophyll degradation
-
-
?
additional information
?
-
-
autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
-
-
?
additional information
?
-
-
no activity with chlorophyll b in all variants
-
?
additional information
?
-
-
autolysis of chlorophyll appears to be brought about by enzymatic activity of chlorophyllase which upon membrane disruption and solubilization obtains access to its chlorophyll substrate
-
-
?
additional information
?
-
-
since chlorophyll degradation is a defining feature of plant senescence, compounds inhibiting chlorophyllase activity may delay senescence, thereby improving shelf life and appearance of plant products
-
-
?
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metabolism
-
the enzyme is involved in the chlorophyll metabolism. Chlorophyllide is not a first intermediate of chlorophyll breakdown, almost unchanged chlorophyll to chlorophyllide ratio after 24 h of paraquat treatment. Melatonin treatment of seeds enhances the ability of pea seedlings to accelerate chlorophyll breakdown and chlorophyll de novo synthesis before oxidative stress exerted by herbicide paraquat treatment appears and several hours after stressing, respectively, while during prolonged paraquat incubation, melatonin delays chlorophyll degradation
evolution
IbChlase in TN57, CN1927, and CYY8467 shares 95% identity, and an eight-nucleotide sequence of Chlase in CYY8467 is missing due to a frame-shift mutation of the Chlase gene leading to early termination of gene translation. Sequences from cutlivars TN57 and CN1927 are clustered together in a clade as Chlase2. Phylogenetic analysis and tree
evolution
the deduced amino acid sequence of recombinant CyanoCLH comprises a unique lipase-motif GHSLG, which differs from the GHSRG sequence of other plants and lacks a histidine of the typical and conserved catalytic triad Ser-Asp-His
evolution
the enzyme shares th highly conserved lipase motif GXSXG
malfunction
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of MeJA-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
malfunction
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of methyl jasmonate-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
malfunction
exposure to phenanthrene, a model compound for polycyclic aromatic hydrocarbon (PAH) stress, leads to enhancement of both chlorophyll synthesis and degradation, but the degradation rate is faster. Phenanthrene accumulation has significant and positive effects on increase of glutamate, 5-aminolevulinic acid, uroporphyrinogen III, protoporphyrin IX, Mg-protoporphyrin IX and protochlorophyllide concentrations. Over the exposure time, wheat leaf color turns light. With the accumulation of phenanthrene, the concentrations of glutamate, 5-aminolevulinic acid, uroporphyrinogen III, protoporphyrin IX, Mg-protoporphyrin IX and protochlorophyllide increase while the concentrations of porphobilinogen and Chlorophyll b decrease. Also chlorophyll a content rises initially and then declines. Uroporphyrinogen III synthase and chlorophyllase are activated and porphobilinogen deaminase activity declines in the treatments. There is a negative correlation between phenanthrene accumulation and total chlorophyll. Toxicity of PAHs to plants and crop PAH-adaptive mechanism in the environment, overview. With increasing phenanthrene accumulation in wheat leaves, the growth of wheat leaves is inhibited, and mature wheat leaf color turns light
malfunction
the incomplete Chlase2 protein of cultivar CYY8467 lacks for the core domain, suggesting that the incomplete CYY8467 Chlase2 does not function in Chl degradation
malfunction
-
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of MeJA-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
-
malfunction
-
chlorophyll breakdown is indistinguishable between wild-type plants and clh1 and clh1/clh2 mutant plants. By contrast, chlorophyll degradation is significantly delayed in an Arabidopsis thaliana mutant that lacks pheophytinase (PPH), catalyzing the breakdown of phytol and known to be associated with chlorophyll catabolism. These data indicate that PPH, not CLH1, is responsible for the majority of methyl jasmonate-enhanced chlorophyll breakdown, even though CLH1 is highly induced by methyl jasmonate
-
physiological function
-
type II chlorophyllase takes part in chlorophyll degradation in stored broccoli florets
physiological function
-
chlorophyll (Chl) breakdown, Chl degradation into phytol, is a multistep enzymatic process, phytol is the first decomposition product of the porphyrin ring. The breakdown takes place in four successive steps catalyzed by chlorophyllase (Chlase), Mg-dechelatase, PAO and red chlorophyll catabolite reductase. Enzyme chlorophyllase (Chlase) catalyzes the reaction of chlorophyll hydrolysis to chlorophyllide (Chlide) and phytol, and it is the first enzyme of Chl catabolism during fruit ripening and leaf senescence
physiological function
chlorophyllase (Chlase) is a hydrophobic enzyme that catalyzes the hydrolysis of chlorophyll (Chl) to chlorophyllide (Chlide) and phytol. Chlase characteristics of sweet potatoes (Ipomoea batatas) with various leaf colors indifferent varieties: yellow (CN1927), green (TN57), and purple (CYY8467). Large variations in Chl and anthocyanin (Ant) and carotenoid (Car) exist in all plants, and cv. CYY8467 contains significantly higher Chl, Ant, and Car levels compared to cvs. TN57 and CN1927. Various plants exhibit different Chlase activities, and Chl a degradation by Chlase of CYY8467 is higher than those of TN57 and CN1927
physiological function
chlorophyllase 1 (CLH1) is not involved in endogenous chlorophyll catabolism, but CLH1 promotes chlorophyllide formation upon disruption of leaf cells, or when it is artificially mistargeted to the chloroplast. CLH is responsible for chlorophyllide formation after the collapse of cells, suggesting that chlorophyllide formation might be a process of defense against chewing herbivores. Arabidopsis leaves with genetically enhanced CLH1 activity exhibit toxicity when fed to Spodoptera litura larvae, an insect herbivore. Purified chlorophyllide partially suppresses the growth of the larvae. Isozyme CLH1 represents the majority of detectable CLH activity in Arabidopsis thaliana
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
A0A0X3WMQ3
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
A0A0B6FPX1
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
A0A1X0M486
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
A0A031JJ58
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
physiological function
CLH2 represents the minority of detectable CLH activity in Arabidopsis thaliana
physiological function
-
induction and course of autumn leaf senescence in early, intermediate and late phenological forms of beech is analyzed from the contents of chlorophyll a and b, chlorophyll degradation products and the activities of chlorophyllase and Mg-dechelatase. Chlorophyll degradation in senescing leaves (obvious by leaf discoloration) of this form occurs in three stages, which strongly coincides with the dates of sudden temperature drops. These stages are less visible in the intermediate form, wherexadas chlorophyll degradation in the late form is the most stable and occurs in two stages. The fraction of chlorophyllides and phaeophytin in relation to chlorophylls in the early phenological form is significantly higher than that in the late form. Biochemical analyses indicate that pigment dephytylation associated with an increase in chlorophyllase activity is an early reaction of chlorophyll degradation, whereas the Mg-dexadchelating reaction is much less important. The activity of chlorophyllase depends significantly on the phenological form. All chlorophyll degradation parameters are highly corxadrelated with temperature changes during senescence. The early phenological form is characterised by the highest correlation coefficients
physiological function
-
key enzyme in chlorophyll degradation
physiological function
-
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
XP_010934773
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
XP_008355440
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
XP_008235366
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
XP_010326690
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
key enzyme in chlorophyll degradation
physiological function
recombinant chlorophyllase 1, CrCLH1, can perform chlorophyll dephytylation and produce chlorophyllide and phytol
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase 1 (CLH1) is not involved in endogenous chlorophyll catabolism, but CLH1 promotes chlorophyllide formation upon disruption of leaf cells, or when it is artificially mistargeted to the chloroplast. CLH is responsible for chlorophyllide formation after the collapse of cells, suggesting that chlorophyllide formation might be a process of defense against chewing herbivores. Arabidopsis leaves with genetically enhanced CLH1 activity exhibit toxicity when fed to Spodoptera litura larvae, an insect herbivore. Purified chlorophyllide partially suppresses the growth of the larvae. Isozyme CLH1 represents the majority of detectable CLH activity in Arabidopsis thaliana
-
physiological function
-
CLH2 represents the minority of detectable CLH activity in Arabidopsis thaliana
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
physiological function
-
chlorophyllase activity involves degradation of chlorophyll and disintegration of the photosynthetic apparatus. The chlorophyllase enzyme catalyzes the hydrolysis of the ester bond in the chlorophyll molecule leading to production of chlorophyllide and phytol
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
A0A0X3WMQ3
bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
A0A0B6FPX1
bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
A0A1X0M486
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
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bioinformatics evaluation of bacterial chlorophyllases, overview
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A0A031JJ58
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
additional information
-
bioinformatics evaluation of plant chlorophyllases, overview
additional information
-
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
XP_010934773
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
XP_008355440
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
XP_008235366
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
XP_010326690
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
bioinformatics evaluation of plant chlorophyllases, overview
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
additional information
-
bioinformatics evaluation of bacterial chlorophyllases, overview
-
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-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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dimer
-
2 * 65000, SDS-PAGE
tetramer
-
4 * 27000, SDS-PAGE
?
-
x * 32922, sequence calculation
?
x * 33910, sequence calculation
?
x * 33710, sequence calculation
?
x * 32705, sequence calculation
?
-
x * 31747, sequence calculation
?
x * 35355, sequence calculation
?
-
x * 35355, sequence calculation
-
?
x * 33110, sequence calculation
?
x * 33821, sequence calculation
?
-
x * 33355, sequence calculation
?
x * 34840, sequence calculation
?
x * 35000, recombinant AtCLH2, SDS-PAGE
?
x * 34850, sequence calculation
?
-
x * 30416, sequence calculation
?
x * 26218, sequence calculation
?
x * 37200, about, sequence calculation
?
x * 32650, sequence calculation
?
x * 23500, isoform CLH3, calculated from amino acid sequence
?
x * 34700, isoform CLH1, calculated from amino acid sequence
?
x * 35300, isoform CLH2, calculated from amino acid sequence
?
x * 66200, isoform CLH3 as MBP-fusion protein, SDS-PAGE
?
x * 77400, isoform CLH1 as MBP-fusion protein, SDS-PAGE
?
x * 78000, isoform CLH2 as MBP-fusion protein, SDS-PAGE
?
x * 35240, sequence calculation
?
x * 31956, sequence calculation
?
-
x * 35422, sequence calculation
?
-
x * 31662, sequence calculation
?
-
x * 31935, sequence calculation
?
-
x * 38001, sequence calculation
?
-
x * 38001, sequence calculation
-
?
-
x * 31620, sequence calculation
?
-
x * 31620, sequence calculation
-
?
-
x * 32295, sequence calculation
?
x * 37723, sequence calculation
?
-
x * 43000 + x * 46000, SDS-PAGE
?
x * 38710, sequence calculation
?
x * 36500, recombinant T7-tagged enzyme, SDS-PAGE
?
x * 32000, recombinant enzyme, SDS-PAGE
?
x * 35290, sequence calculation
?
x * 35250, sequence calculation
?
x * 35250, sequence calculation
?
x * 30212, sequence calculation
?
-
x * 30212, sequence calculation
-
?
x * 54700, recombinant T7-tagged enzyme, SDS-PAGE
?
x * 33910, sequence calculation
?
x * 33360, sequence calculation
?
-
x * 33360, sequence calculation
-
?
XP_010934773
x * 33230, sequence calculation
?
x * 34364, sequence calculation
?
-
x * 26258, sequence calculation
?
-
x * 36325, sequence calculation
?
-
x * 36325, sequence calculation
-
?
x * 33520, sequence calculation
?
x * 29549, sequence calculation
?
-
x * 29549, sequence calculation
-
?
x * 37180, sequence calculation
?
x * 40511, sequence calculation
?
-
x * 40511, sequence calculation
-
?
x * 33332, sequence calculation
?
x * 34534, sequence calculation
?
x * 33824, sequence calculation
?
x * 34360, sequence calculation
?
x * 33429, sequence calculation
?
-
x * 32767, sequence calculation
?
-
x * 33357, sequence calculation
?
x * 33731, sequence calculation
?
-
x * 33731, sequence calculation
-
?
x * 31554, sequence calculation
?
x * 31549, sequence calculation
?
XP_008355440
x * 34730, sequence calculation
?
-
x * 34124, sequence calculation
?
x * 33910, sequence calculation
?
x * 32799, sequence calculation
?
x * 33011, sequence calculation
?
-
x * 33011, sequence calculation
-
?
x * 33486, sequence calculation
?
x * 33704, sequence calculation
?
-
x * 33704, sequence calculation
-
?
x * 33252, sequence calculation
?
-
x * 33252, sequence calculation
-
?
-
x * 33252, sequence calculation
-
?
-
x * 33252, sequence calculation
-
?
-
x * 33252, sequence calculation
-
?
-
x * 33252, sequence calculation
-
?
-
x * 33252, sequence calculation
-
?
x * 24127, sequence calculation
?
-
x * 24127, sequence calculation
-
?
-
x * 24127, sequence calculation
-
?
-
x * 24127, sequence calculation
-
?
-
x * 24127, sequence calculation
-
?
-
x * 24127, sequence calculation
-
?
-
x * 24127, sequence calculation
-
?
x * 33704, sequence calculation
?
-
x * 33704, sequence calculation
-
?
-
x * 31991, sequence calculation
?
-
x * 33237, sequence calculation
?
-
x * 32255, sequence calculation
?
-
x * 33481, sequence calculation
?
x * 33169, sequence calculation
?
x * 38001, sequence calculation
?
x * 37770, sequence calculation
?
-
x * 34783, sequence calculation
?
x * 33780, sequence calculation
?
-
x * 34148, sequence calculation
?
x * 32798, sequence calculation
?
-
x * 33865, sequence calculation
?
-
x * 43000 + x * 46000, SDS-PAGE
?
-
x * 34540, sequence calculation
?
x * 35720, sequence calculation
?
x * 34560, sequence calculation
?
x * 33010, sequence calculation
?
x * 36060, sequence calculation
?
x * 33434, sequence calculation
?
-
x * 33434, sequence calculation
-
?
-
x * 33434, sequence calculation
-
?
-
x * 100000, isoform Chlase F1, SDS-PAGE
?
-
x * 60000, isoform Chlase F2, SDS-PAGE
?
-
x * 100000, isoform Chlase F1, SDS-PAGE
?
-
x * 35000, isoform Chlase F2, SDS-PAGE
?
XP_008235366
x * 34160, sequence calculation
?
-
x * 40000, isoform Chlase F2, SDS-PAGE
?
-
x * 90000, isoform Chlase F1, SDS-PAGE
?
-
x * 34464, sequence calculation
?
-
x * 34464, sequence calculation
-
?
x * 39343, sequence calculation
?
-
x * 32020, sequence calculation
?
x * 32310, sequence calculation
?
-
x * 33648, sequence calculation
?
A0A1X0M486
x * 33666, sequence calculation
?
-
x * 32079, sequence calculation
?
x * 33394, sequence calculation
?
-
x * 33394, sequence calculation
-
?
-
x * 33352, sequence calculation
?
-
x * 34638, sequence calculation
?
x * 34825, sequence calculation
?
-
x * 34825, sequence calculation
-
?
-
x * 32633, sequence calculation
?
x * 38260, sequence calculation
?
-
x * 36861, sequence calculation
?
-
x * 34060, sequence calculation
?
x * 35380, sequence calculation
?
XP_010326690
x * 34360, sequence calculation
?
x * 34390, sequence calculation
?
x * 34770, sequence calculation
?
x * 34900, sequence calculation
?
A0A031JJ58
x * 32206, sequence calculation
?
-
x * 34636, sequence calculation
?
-
x * 34542, sequence calculation
?
-
x * 33506, sequence calculation
?
-
x * 33759, sequence calculation
?
-
x * 34330, sequence calculation
?
-
x * 33281, sequence calculation
?
x * 33613, sequence calculation
?
-
x * 32672, sequence calculation
?
-
x * 31526, sequence calculation
?
x * 33125, sequence calculation
?
-
x * 33125, sequence calculation
-
?
x * 33303, sequence calculation
?
x * 33743, sequence calculation
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 33743, sequence calculation
-
?
-
x * 30035, sequence calculation
?
-
x * 33538, sequence calculation
?
-
x * 33453, sequence calculation
?
x * 33145, sequence calculation
?
-
x * 33395, sequence calculation
?
x * 33625, sequence calculation
?
-
x * 33625, sequence calculation
-
?
A0A0X3WMQ3
x * 33418, sequence calculation
?
x * 33714, sequence calculation
?
-
x * 33124, sequence calculation
?
x * 33079, sequence calculation
?
-
x * 33079, sequence calculation
-
?
-
x * 33648, sequence calculation
?
x * 31448, sequence calculation
?
x * 34279, sequence calculation
?
x * 33485, sequence calculation
?
x * 33744, sequence calculation
?
-
x * 33744, sequence calculation
-
?
x * 33509, sequence calculation
?
x * 33666, sequence calculation
?
-
x * 31785, sequence calculation
?
x * 33407, sequence calculation
?
-
x * 32935, sequence calculation
?
-
x * 32346, sequence calculation
?
-
x * 34382, sequence calculation
?
x * 82490, sequence calculation
?
-
x * 82490, sequence calculation
-
?
-
x * 82490, sequence calculation
-
?
-
x * 82490, sequence calculation
-
?
x * 37315, sequence calculation
?
-
x * 37315, sequence calculation
-
?
x * 33840, sequence calculation
?
x * 32440, sequence calculation
?
x * 33260, sequence calculation
?
-
x * 53975, sequence calculation
?
-
x * 53975, sequence calculation
-
?
-
x * 31419, sequence calculation
?
A0A0B6FPX1
x * 31368, sequence calculation
?
-
x * 31368, sequence calculation
-
?
x * 37634, sequence calculation
?
x * 31368, sequence calculation
?
-
x * 32081, sequence calculation
?
-
x * 32058, sequence calculation
?
-
x * 32058, sequence calculation
-
?
x * 35990, sequence calculation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
the mature form is N-terminally processed after amino acids 21, 20 or 19
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 11
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 247
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 36
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 201 and 261
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 212
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 198, 213, 257, and 311
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 106
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 131
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 225
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 202
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 116 and 225
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 145 and 319
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 215, 229, 251, and 321
glycoprotein
the enzyme sequence contains 5 glycosylation sites at positions 77, 137, 229, 249, and 264
glycoprotein
the enzyme sequence contains 5 glycosylation sites at positions 77, 137, 229, 249, and 267
glycoprotein
the enzyme sequence contains 5 glycosylation sites at positions 77, 137, 229, 249, and 267
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 109 and 103
glycoprotein
XP_010934773
the enzyme sequence contains 2 glycosylation sites
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 17, 194, and 298
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 211
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 240
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 240
-
glycoprotein
the enzyme sequence contains 3 glycosylation sites at position 153, 217, and 257
glycoprotein
the enzyme sequence contains 6 glycosylation sites at positions 29, 39, 57, 75, 100, and 253
glycoprotein
-
the enzyme sequence contains 6 glycosylation sites at positions 29, 39, 57, 75, 100, and 253
-
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 24, 35, and 103
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 119 and 375
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 119 and 375
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 14
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 56
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 61, 135, and 198
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 61, 135, and 198
-
glycoprotein
XP_008355440
the enzyme sequence contains 2 glycosylation sites at positions 7 and 270
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 115 and 144
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 255
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 287
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 287
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 200
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 200
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 45
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 45
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 5 and 239
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 335
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 189 and 364
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 139
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 34, 156, and 246
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 138
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 197 and 252
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 192 and 289
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 12 and 151
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 4, 16, 125, and 147
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 20, 23, 111, and 173
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 149
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 61, 106, and 144
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 61, 106, and 144
-
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 61, 106, and 144
-
glycoprotein
XP_008235366
the enzyme sequence contains 2 glycosylation sites at positions 191 and 266
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 78, 155, and 224
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 78, 155, and 224
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 249
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 195 and 260
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 248
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 56
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 288
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 133 and 193
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 2, 21, and 131
glycoprotein
XP_010326690
the enzyme sequence contains 4 glycosylation sites at positions 20, 35, 154, and 289
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 290
glycoprotein
the enzyme sequence contains 4 glycosylation sites
glycoprotein
A0A031JJ58
the enzyme sequence contains 1 glycosylation site at position 291
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 195
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 239
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 189, 239,and 289
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 60
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 60
-
glycoprotein
the enzyme sequence contains 6 glycosylation sites at positions 31, 96, 176, 260, 330, and 369
glycoprotein
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 2 glycosylation sites at positions 61 and 198
-
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 169
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 61
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 139
glycoprotein
A0A0X3WMQ3
the enzyme sequence contains 6 glycosylation sites at positions 31, 96, 176, 260, 330, and 369
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 198
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 62
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 64
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 196
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 202
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 12, 245, 319, and 354
glycoprotein
-
the enzyme sequence contains 4 glycosylation sites at positions 12, 245, 319, and 354
-
glycoprotein
-
the enzyme sequence contains 4 glycosylation sites at positions 12, 245, 319, and 354
-
glycoprotein
-
the enzyme sequence contains 4 glycosylation sites at positions 12, 245, 319, and 354
-
glycoprotein
the enzyme sequence contains 3 glycosylation sites at positions 76, 137, and 321
glycoprotein
-
the enzyme sequence contains 3 glycosylation sites at positions 76, 137, and 321
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 11
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 144
glycoprotein
-
the enzyme sequence contains 7 glycosylation sites at positions 76, 108, 334, 371, 379, 385, and 398
glycoprotein
-
the enzyme sequence contains 7 glycosylation sites at positions 76, 108, 334, 371, 379, 385, and 398
-
glycoprotein
the enzyme sequence contains 4 glycosylation sites at positions 31, 90, 91, and 239
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 139
glycoprotein
-
the enzyme sequence contains 1 glycosylation site at position 139
-
glycoprotein
the enzyme sequence contains 1 glycosylation site at position 151
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
A0A1X0M486
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no glycoprotein
A0A0B6FPX1
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
-
no glycoprotein
the enzyme sequence contains no glycosylation site
no glycoprotein
-
the enzyme sequence contains no glycosylation site
no modification
-
side-chain modification
-
glycoprotein
side-chain modification
-
the sugar group not only stabilizes the enzyme, but also is essential for the manifestation of enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Chlase gene, DNA and amino acid sequence determination and anaylsis, expression of precursor full-length wild-type Chlase and of a mutant ChlaseDELTAN lacking the N-terminal 21 amino acids, which corresponds to the mature enzyme, in two heterologous plant systems: in Cucurbita pepo cv. Maayan plants using a ZYMV-based viral vector infective clone system and inoculation of cotyledons, and transiently in Nicotiana tabacum cv. Samsun NN chloroplast membranes of protoplasts, expression of full-length and truncated enzyme versions as thioredoxin fusion proteins in Escherichia coli
DNA and amino acid sequence determination and analysis, isozyme sequence comparisons, and phylogenetic analysis and tree, the isozymes from cultivars TN57, CN1927, and CYY8467 share 95% identity, and an eight-nucleotide sequence of Chlase in CYY8467 is missing due to a frame-shift mutation of the Chlase gene leading to early termination of gene translation
DNA and amino acid sequence determination and analysis, isozyme sequence comparisons, and phylogenetic analysis and tree, the isozymes from cultivars TN57, CN1927, and CYY8467 share 95% identity, and an eight-nucleotide sequence of Chlase2 in CYY8467 is missing due to a frame-shift mutation of the Chlase gene leading to early termination of gene translation implying that a frame shift mutation of the Chlase gene has evolved in CYY8467
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosseta-Gami B (DE3) cells
expressed in Escherichia coli strain BL21(DE3)
expression as His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
expression of antisense construct of gene CLH3 in broccoli plants using Agrobacterium tumefaciens-mediated transformation
expression of antisense constructs of gene CLH1 in broccoli plants using Agrobacterium tumefaciens-mediated transformation
expression of antisense constructs of gene CLH2 in broccoli plants using Agrobacterium tumefaciens-mediated transformation
expression of gene ATHCOR1 in Escherichia coli BL21 as maltose-binding protein fusion protein, cloning of the gene into an expression vector for transformation of Arabidopsis thaliana plants
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene ADK38_11350, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene ADK43_31155, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene ADK78_03330, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
gene ADL21_28415, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene ADL28_40565, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene ADL32_23315, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
A0A0X3WMQ3
gene AJAP_22265, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene AMED_0735, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene ATCLH1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene AW19_2954, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
A0A0B6FPX1
gene BC342_33805, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene BE15_26615, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene BG04_602, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene BOLC2T10484H, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene BOLC5T30519H, functional recombinant expression of C-terminally His-tagged enzyme BoCHL1 in Escherichia coli strain BL21(DE3)
gene BV96_01378, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
A0A031JJ58
gene BXO91_01455, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
A0A1X0M486
gene BZ13_341, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene CACLH, sequence analysis, comparisons, and phylogenetic analysis, overview. Recombinant expression as insoluble protein in Escherichia coli
gene cce_5094, sequence comparisons, recombinant expression of the N-terminally T7-tagged enzyme (T7 tag sequence is MASMTGGQQMG)in Escherichia coli strain BL21(DE3)
gene Cha6605_2121, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene chl1, DNA and amino acid sequence determination and anaylsis, transient expression of isozyme AtCLH1 as GFP-tagged protein, e.g. in senescent mesophyll protoplasts, expression analysis
gene chl2, DNA and amino acid sequence determination and anaylsis, transient expression of isozyme AtCLH2 as GFP-tagged protein, e.g. in senescent mesophyll protoplasts, expression analysis
gene chl2, expression anaylsis, recombinant expression in Escherichia coli strain BL21 (DE3)
gene Chlase1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene CJJ17_24065, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene CLH, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene CLH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant C-terminally GFP-tagged enzyme expression driven by a CAMV35S promoter is determined in chloroplasts of Arabidopsis thaliana mesophyll protoplasts (isolated from 3-4-week-old well-expanded leaves yet to flower), recombinant overexpression of soluble N-terminally T7-tagged enzyme in Escherichia coli strain BL21(DE3)
gene clh1, recombinant expression of YFP-tagged enzyme in Arabidopsis thaliana, the YFP-tagged enzyme is detected outside of chloroplasts in leaf protoplasts prepared from plants constitutively expressing CLH1-YFP
gene CLH1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Csa_2G222090, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene CSB93_3304, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene DDY18_06460, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene DF19_10980, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
gene DJ90_4464, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene DJ93_5833, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene DM39_4274, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene DM48_2363, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
gene DR71_1130, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene DV20_35655, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene ERS008472_03552, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene ERS008530_03671, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene F775_31213, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene F775_31213, sequence analysis, comparisons, and phylogenetic analysis, overview. Recombinant expression as soluble protein in Escherichia coli
gene FG87_12610, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene FM21_30765, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
gene GKIL_3644, sequence analysis, comparisons, and phylogenetic analysis, overview
gene H489_0111595, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene HMPREF9554_01030, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene JCGZ_02225, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene KALB_5797, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene LK07_10060, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene LL06_17325, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene LP52_09115, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene MAB_3744, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Micau_5231, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene MTR_1g041385, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Namu_1618, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Nos7524_0754, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene P354_07750, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene QR77_15265, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene SAMN05660733_05076, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene Sare_3190, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SAVERM_2604, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene SD37_17575, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SD80_11705, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SETIT_9G266700v2, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SGM_2508, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SL103_16385, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene SNA_20280, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene Theco_3404, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene TK50_20200, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene TRIUR3_22141, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene TU94_29540, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene UK23_27830, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene VAB18032_29991, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene VZ95_07895, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene XU06_03985, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
gene Y717_00135, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene YC6258_05192, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Z051_21130, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble and soluble protein in Escherichia coli
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Recombinant expression as soluble protein in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
gene Chlase1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Chlase1, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene DJ90_4464, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
gene DJ90_4464, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
gene F775_31213, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene F775_31213, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene F775_31213, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Nos7524_0754, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
gene Nos7524_0754, sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
XP_010934773
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
XP_010326690
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as insoluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
XP_008355440
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
XP_008235366
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
sequence analysis, comparisons, and phylogenetic analysis, overview. Expression as soluble protein
-
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Shioi, Y.; Sasa, T.
Purification of solubilized chlorophyllase from Chlorella protothecoides
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Auxenochlorella protothecoides
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Inactivation of chlorophyllase by negatively charged plant membrane lipids
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Phaeodactylum tricornutum
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Molecular mass estimation of chlorophyllase in situ by radiation inactivation analysis. Studies on the composition of the isolated enzyme
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1985
Phaeodactylum tricornutum
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Melia azedarach, Tetragonia tetragonoides
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Secale cereale
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Hydrophobic chromatographic purification of ethylene-enhanced chlorophyllase from Citrus unshiu fruits
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Purification of ethylene-enhanced chlorophyllase from Citrus unshiu fruits
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Phaeodactylum tricornutum
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The activity of Triton X-100 soluble chlorophyllase in liposomes
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Phaseolus vulgaris
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Beta vulgaris
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Secale cereale
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Citrus sinensis, Petroselinum crispum
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Biochim. Biophys. Acta
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Phaeodactylum tricornutum
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Terpstra, W.; Lambers, J.W.J.
Interactions between chlorophyllase, chlorophyll a, plant lipids and Mg2+
Biochim. Biophys. Acta
746
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1983
Phaeodactylum tricornutum
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Tanaka, K.; Kakuno, T.; Yamashita, J.; Horio, T.
Action of chlorophyllase purified from rye seedlings on light-harvesting bacteriochlorophyll of chromatophores and spheroplasts from Rhodospirillum rubrum
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1983
Secale cereale
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Studies on chlorophyllase. The mechanism of the action of lecithin liposomes on enzyme activity and the function of the carbohydrate moiety of the enzyme
Biochim. Biophys. Acta
681
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1982
Phaeodactylum tricornutum
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Terpstra, W.
Influence of lecithin liposomes on chlorophyllase-catalyzed chlorophyll hydrolysis: comparison of intramembraneous and solubilized Phaeodactylum chlorophyllase
Biochim. Biophys. Acta
600
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1980
Phaeodactylum tricornutum
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Nishiyama, Y.; Kitamura, M.; Tamura, S.; Watanabe, T.
Purification and substrate specificity of chlorophyllase from Chlorella regularis
Chem. Lett.
1
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Chlorella regularis
-
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Tsuchiya, T.; Ohta, H.; Masuda, T.; Mikami, B.; Kita, N.; Shioi, Y.; Takamiya, K.
Purification and characterization of two isozymes of chlorophyllase from mature leaves of Chenopodium album
Plant Cell Physiol.
38
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1997
Chenopodium album
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Scheumann, V.; Schoch, S.; Rudiger, W.
Chlorophyll b reduction during senescence of barley seedlings
Planta
209
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1999
Hordeum vulgare
brenda
Fernandez-Lopez, J.A.; Almela, L.; Almansa, M.S.; Lopez-Roca, J.M.
Partial purification and properties of chlorophyllase from chlorotic Citrus limon leaves
Phytochemistry
31
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1992
Citrus limon
-
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Samaha, H.; Kermasha, S.
Biocatalysis of chlorophyllase in a ternary micellar system containing Span 85 using purified and oxidized pheophytins as substrates
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Phaeodactylum tricornutum
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Gaffar, R.; Kermasha, S.; Bisakowski, B.
Biocatalysis of immobilized chlorophyllase in a ternary micellar system
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Phaeodactylum tricornutum
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Tsuchiya, T.; Ohta, H.; Okawa, K.; Iwamatsu, A.; Shimada, H.; Masuda, T.; Takamiya, K.
Cloning of chlorophyllase, the key enzyme in chlorophyll degradation: finding of a lipase motif and the induction by methyl jasmonate
Proc. Natl. Acad. Sci. USA
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1999
Chenopodium album (Q9LE89), Chenopodium album
brenda
Khalyfa, A.; Kermasha, S.; Marsot, P.; Goetghebeur, M.
Purification and characterization of chlorophyllase from alga Phaeodactylum tricornutum by preparative native electrophoresis
Appl. Biochem. Biotechnol.
53
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1995
Phaeodactylum tricornutum
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Khalyfa, A.; Kermasha, S.; Khamessan, A.; Marsot, P.; Alli, I.
Purification and characterization of chlorophyllase from alga (Phaeodactylum tricornutum) by preparative isoelectric focusing
Biosci. Biotechnol. Biochem.
57
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1993
Phaeodactylum tricornutum
-
brenda
Kermasha, S.; Khalyfa, A.; Marsot, P.; Alli, I.; Fournier, R.
Biomass production, purification and characterization of chlorophyllase from alga (Phaeodactylum tricornutum)
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15
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1992
Phaeodactylum tricornutum
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Effects of delta-aminolevulinic acid on pigment formation and chlorophyllase activity in French bean leaf
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Phaseolus vulgaris
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Todorov, D.T.; Karanov, E.N.; Smith, A.R.; Hall, M.A.
Chlorophyllase activity and chlorophyll content in wild type and eti5 mutant of Arabidopsis thaliana subjected to low and high temperatures
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Arabidopsis thaliana
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Encapsulation of chlorophyllase in hydrophobically modified hydrogel
J. Mol. Catal. B
19-20
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2002
Phaeodactylum tricornutum
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Hornero-Mendez, D.; Minguez-Mosquera, M.I.
Chlorophyll disappearance and chlorophyllase activity during ripening of Capsicum annuum L. fruits
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Capsicum annuum
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Roca, M.; Minguez-Mosquera, M.I.
Involvement of chlorophyllase in chlorophyll metabolism in olive varieties with high and low chlorophyll content
Physiol. Plant.
117
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Olea europaea
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Tsuchiya, T.; Suzuki, T.; Yamada, T.; Shimada, H.; Masuda, T.; Ohta, H.; Takamiya, K.
Chlorophyllase as a serine hydrolase: identification of a putative catalytic triad
Plant Cell Physiol.
44
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2003
Chenopodium album
brenda
Benedetti, C.E.; Arruda, P.
Altering the expression of the chlorophyllase gene ATHCOR1 in transgenic Arabidopsis caused changes in the chlorophyll-to-chlorophyllide ratio
Plant Physiol.
128
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Arabidopsis thaliana
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Arkus, K.A.; Cahoon, E.B.; Jez, J.M.
Mechanistic analysis of wheat chlorophyllase
Arch. Biochem. Biophys.
438
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Triticum aestivum
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Janave, M.T.; Sharma, A.
Partial purification of chlorophyll degrading enzymes from Cavendish banana (Musa Cavendishii)
Indian J. Biochem. Biophys.
41
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Musa cavendishii
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Karboune, S.; Neufeld, R.; Kermasha, S.
Immobilization and biocatalysis of chlorophyllase in selected organic solvent systems
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Phaeodactylum tricornutum
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Yang, C.M.; Wang, M.C.; Lu, Y.F.; Chang, I.F.; Chou, C.H.
Humic substances affect the activity of chlorophyllase
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Pachira macrocarpa
brenda
Kariola, T.; Brader, G.; Li, J.; Palva, E.T.
Chlorophyllase 1, a damage control enzyme, affects the balance between defense pathways in plants
Plant Cell
17
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2005
Arabidopsis thaliana (O22527), Arabidopsis thaliana
brenda
Tang, L.; Okazawa, A.; Itoh, Y.; Fukusaki, E.i.; Kobayashi, A.
Expression of chlorophyllase is not induced during autumnal yellowing in Ginkgo biloba
Z. Naturforsch. C
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Ginkgo biloba (Q7Y0K5), Ginkgo biloba
brenda
Okazawa, A.; Tango, L.; Itoh, Y.; Fukusaki, E.; Kobayashi, A.
Characterization and subcellular localization of chlorophyllase from Ginkgo biloba
Z. Naturforsch. C
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Ginkgo biloba (Q7Y0K5), Ginkgo biloba
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Arkus, K.A.; Jez, J.M.
Development of a high-throughput purification method and a continuous assay system for chlorophyllase
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Phaeodactylum tricornutum
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Gender-specific responses of Piper betle L. to low temperature stress: changes in chlorophyllase activity
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Piper betle
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Yi, Y.; Kermasha, S.; Neufeld, R.
Characterization of sol-gel entrapped chlorophyllase
Biotechnol. Bioeng.
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2006
Phaeodactylum tricornutum
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Schenk, N.; Schelbert, S.; Kanwischer, M.; Goldschmidt, E.E.; Doermann, P.; Hoertensteiner, S.
The chlorophyllases AtCLH1 and AtCLH2 are not essential for senescence-related chlorophyll breakdown in Arabidopsis thaliana
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Arabidopsis thaliana (O22527), Arabidopsis thaliana (Q9M7I7), Arabidopsis thaliana
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AtCLH2, a typical but possibly distinctive chlorophyllase gene in Arabidopsis
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Arabidopsis thaliana (Q9M7I7)
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Harpaz-Saad, S.; Azoulay, T.; Arazi, T.; Ben-Yaakov, E.; Mett, A.; Shiboleth, Y.M.; Hoertensteiner, S.; Gidoni, D.; Gal-On, A.; Goldschmidt, E.E.; Eyal, Y.
Chlorophyllase is a rate-limiting enzyme in chlorophyll catabolism and is posttranslationally regulated
Plant Cell
19
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2007
Citrus sinensis (Q9MV14)
brenda
Chen, L.O.; Lin, C.; Kelkar, S.M.; Chang, Y.; Shaw, J.
Transgenic broccoli (Brassica oleracea var. italica) with antisense chlorophyllase (BoCLH1) delays postharvest yellowing
Plant Sci.
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Brassica oleracea (Q8GTM2), Brassica oleracea (Q8GTM3), Brassica oleracea (Q8GTM4)
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Chen, R.; Liu, H.; Huang, Q.; Sun, G.; Huang, D.
Changes of chlorophyll and anthocyanin content and related enzyme activities of flower stalk in Chinese kale under different light intensities
Acta Hortic.
769
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Brassica oleracea
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Arkus, K.A.; Jez, J.M.
An integrated protein chemistry laboratory. Chlorophyll and chlorophyllase
Biochem. Mol. Biol. Educ.
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2008
Triticum aestivum
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Azoulay Shemer, T.; Harpaz-Saad, S.; Belausov, E.; Lovat, N.; Krokhin, O.; Spicer, V.; Standing, K.G.; Goldschmidt, E.E.; Eyal, Y.
Citrus chlorophyllase dynamics at ethylene-induced fruit color-break: a study of chlorophyllase expression, posttranslational processing kinetics, and in situ intracellular localization
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Citrus limon
brenda
Gupta, S.; Kumar, N.; Gupta, S.
Utility of chlorophyllase activity in mango (Mangifera indica L. Var. Dasheheri) peel for assessing state of ripening
National Academy Science Letters
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Mangifera indica
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Kaosamphan, A.; Yamauchi, N.; Srilaong, V.; Aiamla-Or, S.; Wongs-Aree, C.; Uthairatanakij, A.
Involvement of chlorophyllase on chlorophyll degradation in stored broccoli florets and its control by UV treatment
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Brassica oleracea
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Lee, G.C.; Chepyshko, H.; Chen, H.H.; Chu, C.C.; Chou, Y.F.; Akoh, C.C.; Shaw, J.F.
Genes and biochemical characterization of three novel chlorophyllase isozymes from Brassica oleracea
J. Agric. Food Chem.
58
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Brassica oleracea (Q8GTM2), Brassica oleracea (Q8GTM3), Brassica oleracea (Q8GTM4), Brassica oleracea
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Buechert, A.M.; Civello, P.M.; Martinez, G.A.
Chlorophyllase versus pheophytinase as candidates for chlorophyll dephytilation during senescence of broccoli
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Brassica oleracea (Q8GTM3), Brassica oleracea (Q8GTM4)
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Azoulay-Shemer, T.; Harpaz-Saad, S.; Cohen-Peer, R.; Mett, A.; Spicer, V.; Lovat, N.; Krokhin, O.; Brand, A.; Gidoni, D.; Standing, K.G.; Goldschmidt, E.E.; Eyal, Y.
Dual N- and C-terminal processing of citrus chlorophyllase precursor within the plastid membranes leads to the mature enzyme
Plant Cell Physiol.
52
70-83
2011
Citrus limon (B6DX58)
brenda
Sytykiewicz, H.; Sprawka, I.; Czerniewicz, P.; Sempruch, C.; Leszczy?ski, B.; Sikora, M.
Biochemical characterisation of chlorophyllase from leaves of selected Prunus species--a comparative study
Acta Biochim. Pol.
60
457-465
2013
Prunus domestica, Prunus padus, Prunus cerasus
brenda
Yang, C.H.; Yen, C.C.; Jheng, J.J.; Wang, C.Y.; Chen, S.S.; Huang, P.Y.; Huang, K.S.; Shaw, J.F.
Immobilization of Brassica oleracea chlorophyllase 1 (BoCLH1) and Candida rugosa lipase (CRL) in magnetic alginate beads: an enzymatic evaluation in the corresponding proteins
Molecules
19
11800-11815
2014
Brassica oleracea
brenda
Chen, M.; Yang, J.; Liu, C.; Lin, K.; Yang, C.
Molecular, structural, and phylogenetic characterization of two chlorophyllase isoforms in Pachira macrocarpa
Plant Syst. Evol.
300
633-643
2014
Pachira macrocarpa (C1JZ61), Pachira macrocarpa (C1JZ62)
brenda
Kraj, W.
Chlorophyll degradation and the activity of chlorophyllase and Mg-dechelatase during leaf senescence in Fagus sylvatica
Dendrobiology
74
43-57
2015
Fagus sylvatica
-
brenda
Nowak, P.M.; Wozniakiewicz, M.; Michalik, M.; Fiedor, L.; Koscielniak, P.
Capillary coating as an important factor in optimization of the off-line and on-line MEKC assays of the highly hydrophobic enzyme chlorophyllase
Anal. Bioanal. Chem.
409
1493-1501
2017
Arabidopsis thaliana
brenda
Sharafi, E.; Dehestani, A.; Farmani, J.; Parizi, A.
Bioinformatics evaluation of plant chlorophyllase, the key enzyme in chlorophyll degradation
Appl. Food Biotechnol.
4
167-178
2017
Aegilops tauschii (N1R2K4), Amborella trichopoda (W1NV63), Arabidopsis lyrata subsp. lyrata (D7KI46), Arabidopsis thaliana (O22527), Beta vulgaris (A0A0J8FQE7), Brassica napus (A0A078ILD2), Brassica oleracea (Q8GTM3), Chenopodium album (Q9LE89), Citrus limon (B6DX58), Citrus sinensis (Q9MV14), Citrus unshiu (Q94LX1), Cucumis sativus (A0A0A0LNT6), Elaeis guineensis (XP_010934773), Ginkgo biloba (Q7Y0K5), Jatropha curcas (A0A067KVU1), Malus domestica (XP_008355440), Medicago truncatula (A0A072VHG0), Oryza sativa Japonica Group (Q7XEJ4), Pachira macrocarpa (C1JZ62), Phoenix dactylifera, Picea sitchensis (C0PR35), Picrorhiza kurrooa (A0A024CJ54), Piper betle (Q7XJ36), Populus trichocarpa (B9HUR3), Prunus mume (XP_008235366), Pyrus x bretschneideri (G3K720), Sesamum indicum, Setaria italica (K4AC16), Solanum lycopersicum (XP_010326690), Solanum pennellii (F1BPW6), Solanum tuberosum (M1A7S9), Triticum aestivum (W6EIP8), Triticum urartu (M8AD49), Vitis vinifera (F6HI77), Zea mays (B4FAJ2)
-
brenda
Chou, Y.L.; Lee, Y.L.; Yen, C.C.; Chen, L.F.; Lee, L.C.; Shaw, J.F.
A novel recombinant chlorophyllase from cyanobacterium Cyanothece sp. ATCC 51142 for the production of bacteriochlorophyllide a
Biotechnol. Appl. Biochem.
63
371-377
2016
Crocosphaera subtropica ATCC 51142 (B1X2S9)
brenda
Sharafi, E.; Farmani, J.; Parizi, A.; Dehestani, A.
In search of engineered prokaryotic chlorophyllases a bioinformatics approach
Biotechnol. Bioprocess Eng.
23
507-524
2018
Enterobacter cloacae, Bacillus licheniformis, Burkholderia gladioli, Burkholderia mallei, Nocardia otitidiscaviarum, Rhodococcus rhodnii, Yersinia pestis, Yersinia pseudotuberculosis, Rhodococcus erythropolis, Serratia marcescens, Streptomyces achromogenes, Streptomyces californicus, Streptomyces alboviridis, Kitasatospora aureofaciens, Streptomyces collinus, Streptomyces galbus, Streptomyces vinaceus, Yersinia enterocolitica, Burkholderia thailandensis, Burkholderia multivorans, Yersinia aldovae, Aquincola tertiaricarbonis, Enterobacteriaceae bacterium, Oscillatoria acuminata, Saccharothrix syringae, Catenuloplanes japonicus, Acetobacter nitrogenifigens, Salinispora pacifica, Ktedonobacter racemifer, Streptacidiphilus anmyonensis, Streptomyces cellulosae, Streptomyces mutabilis, Streptacidiphilus neutrinimicus, Streptacidiphilus melanogenes, Streptomyces olindensis, Burkholderia oklahomensis, Pseudoalteromonas piscicida, Streptacidiphilus jeojiense, Streptacidiphilus oryzae, Streptomyces xiaopingdaonensis, Pseudorhizobium pelagicum, Nocardia jiangxiensis, Paenibacillus sp. FSL H8-457, Streptomyces xylophagus, Staphylococcus sp. TE8, Amycolatopsis jejuensis, Nocardia pneumoniae, Nocardia cerradoensis, Saccharomonospora piscinae, Paenibacillus fonticola, Thalassospira australica, Martelella mediterranea, Curtobacterium flaccumfaciens (A0A022LGW9), Sphingomonas paucimobilis (A0A031JJ58), Amycolatopsis rifamycinica (A0A066TZN0), Amycolatopsis japonica (A0A075UY09), Corynebacterium sp. (A0A088QGQ9), Burkholderia cenocepacia (A0A088UE24), Bacillus mycoides (A0A090YBL8), Paenibacillus macerans (A0A090YRL6), Hoeflea sp. BAL378 (A0A098T8B9), Priestia megaterium (A0A0B6AMR7), Yersinia frederiksenii (A0A0B6FPX1), Nocardia vulneris (A0A0C1D845), Streptomyces sp. 150FB (A0A0C2B4W5), Streptomonospora alba (A0A0C2JR10), Scytonema tolypothrichoides (A0A0C2MA34), Streptomyces cyaneogriseus subsp. noncyanogenus (A0A0C5GKK1), Gynuella sunshinyii (A0A0C5VRG3), Micromonospora carbonacea (A0A0D0X120), Streptomyces natalensis (A0A0D7CJH6), Lentzea aerocolonigenes (A0A0F0GNE4), Elstera litoralis (A0A0F3ITG4), Amycolatopsis mediterranei (A0A0H3CWX4), Kibdelosporangium sp. MJ126-NF4 (A0A0K3BD68), Streptomyces varsoviensis (A0A0L8QS29), Rhodococcus rhodochrous (A0A0M8PDN7), Streptomyces rimosus subsp. rimosus (A0A0M9XD02), Yersinia intermedia (A0A0T9MSN6), Yersinia kristensenii (A0A0T9QQS0), Streptomyces violaceusniger (A0A0X3VIK1), Streptomyces griseus subsp. griseus (A0A0X3WMQ3), Streptomyces albus (A0A0X7JI19), Sorangium cellulosum (A0A150QHW0), Amycolatopsis orientalis (A0A193BYG1), Streptomyces lydicus (A0A1D7VLK8), Streptomyces olivaceus (A0A1D8SZ30), Microbispora rosea (A0A1N7H723), Lentzea albidocapillata (A0A1W2F5U3), Rhodococcus qingshengii (A0A1X0M486), Streptomyces pluripotens (A0A221NWZ6), Pseudomonas aeruginosa (A0A2R3IPM7), Streptomyces scopuliridis (A0A2T7T9L5), Flavobacterium sp. (A0A354DAG3), Streptomyces albulus (A0A401QPU9), Gordonia polyisoprenivorans (A0A846WHQ0), Salinispora arenicola (A8LV05), Mycobacteroides abscessus (B1MG73), Francisella philomiragia (C6YVF8), Nakamurella multipartita (C8XFP8), Micromonospora aurantiaca (D9TCV0), Treponema phagedenis (E7NSJ0), Streptomyces griseoaurantiacus (F3NH94), Micromonospora maris (F4F8Y9), Nocardia brasiliensis (K0EM71), Nostoc sp. PCC 7524 (K9QM01), Chamaesiphon minutus (K9UDL2), Thermobacillus composti (L0EJP9), Streptomyces avermitilis (Q82K00), Gloeobacter kilaueensis (U5QQD5), Kutzneria albida (W5WDD1), Mycobacteroides abscessus JCM 13569 (B1MG73), Streptomyces avermitilis JCM 5070 (Q82K00), Nocardia brasiliensis ATCC 700358 (K0EM71), Nakamurella multipartita Y-104 (C8XFP8), Salinispora arenicola CNS-205 (A8LV05), Streptomyces avermitilis MA-4680 (Q82K00), Yersinia frederiksenii Y225 (A0A0B6FPX1), Thermobacillus composti KWC4 (L0EJP9), Nakamurella multipartita DSM 44233 (C8XFP8), Priestia megaterium ATCC 14581 (A0A0B6AMR7), Micromonospora maris AB-18-032 (F4F8Y9), Streptomyces griseoaurantiacus M045 (F3NH94), Mycobacteroides abscessus CIP 104536 (B1MG73), Mycobacteroides abscessus DSM 44196 (B1MG73), Enterobacteriaceae bacterium ATCC 29904, Mycobacteroides abscessus ATCC 19977 (B1MG73), Burkholderia thailandensis 34, Amycolatopsis mediterranei U-32 (A0A0H3CWX4), Streptomyces avermitilis NBRC 14893 (Q82K00), Nakamurella multipartita ATCC 700099 (C8XFP8), Streptomyces avermitilis NCIMB 12804 (Q82K00), Streptomyces avermitilis NRRL 8165 (Q82K00), Mycobacteroides abscessus NCTC 13031 (B1MG73), Nakamurella multipartita JCM 9543 (C8XFP8), Corynebacterium sp. ATCC 6931 (A0A088QGQ9), Mycobacteroides abscessus TMC 1543 (B1MG73), Treponema phagedenis F0421 (E7NSJ0), Kutzneria albida DSM 43870 (W5WDD1), Nakamurella multipartita NBRC 105858 (C8XFP8), Nakamurella multipartita CIP 104796 (C8XFP8), Thermobacillus composti JCM 13945 (L0EJP9), Francisella philomiragia ATCC 25015 (C6YVF8), Gloeobacter kilaueensis JS1 (U5QQD5), Streptomyces avermitilis ATCC 31267 (Q82K00), Streptomyces albulus PD-1 (A0A401QPU9), Streptomyces natalensis ATCC 27448 (A0A0D7CJH6), Priestia megaterium NBRC 15308 (A0A0B6AMR7), Rhodococcus rhodochrous KG-21 (A0A0M8PDN7), Streptomyces avermitilis DSM 46492 (Q82K00), Burkholderia oklahomensis C6786, Yersinia pseudotuberculosis PA3606, Thermobacillus composti DSM 18247 (L0EJP9), Curtobacterium flaccumfaciens UCD-AKU (A0A022LGW9), Micromonospora aurantiaca DSM 43813 (D9TCV0), Yersinia aldovae 670-83, Pseudoalteromonas piscicida JCM 20779, Streptomyces scopuliridis RB72 (A0A2T7T9L5)
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brenda
Shen, Y.; Li, J.; Gu, R.; Yue, L.; Zhan, X.; Xing, B.
Phenanthrene-triggered chlorosis is caused by elevated chlorophyll degradation and leaf moisture
Environ. Pollut.
220
1311-1321
2017
Triticum aestivum (A0A096ZNF0), Triticum aestivum
brenda
Szafranska, K.; Reiter, R.J.; Posmyk, M.M.
Melatonin improves the photosynthetic apparatus in pea leaves stressed by paraquat via chlorophyll breakdown regulation and its accelerated de novo synthesis
Front. Plant Sci.
8
878
2017
Pisum sativum
brenda
Chou, Y.L.; Ko, C.Y.; Yen, C.C.; Chen, L.F.; Shaw, J.F.
A novel recombinant chlorophyllase1 from Chlamydomonas reinhardtii for the production of chlorophyllide derivatives
J. Agric. Food Chem.
63
9496-9503
2015
Chlamydomonas reinhardtii (A8J2S9), Chlamydomonas reinhardtii
brenda
Chou, Y.; Ko, C.; Chen, L.; Yen, C.; Shaw, J.
Purification and immobilization of the recombinant Brassica oleracea chlorophyllase 1 (BoCLH1) on DIAIONCR11 as potential biocatalyst for the production of chlorophyllide and phytol
Molecules
20
3744-3757
2015
Brassica oleracea (Q8GTM4), Brassica oleracea
brenda
Hu, X.; Makita, S.; Schelbert, S.; Sano, S.; Ochiai, M.; Tsuchiya, T.; Hasegawa, S.F.; Hoertensteiner, S.; Tanaka, A.; Tanaka, R.
Reexamination of chlorophyllase function implies its involvement in defense against chewing herbivores
Plant Physiol.
167
660-670
2015
Arabidopsis thaliana (O22527), Arabidopsis thaliana (Q9M7I7), Arabidopsis thaliana Col-0 (O22527), Arabidopsis thaliana Col-0 (Q9M7I7)
brenda
Chen, S.; Wang, S.; Huang, M.; Lin, K.; Hua, S.; Lu, H.; Lai, Y.; Yang, C.
Physiological and molecular analyses of chlorophyllase in sweet potatoes with different-colored leaves
South Afr. J. Bot.
114
272-279
2018
Ipomoea batatas (A0A2U8KGL8), Ipomoea batatas (A0A2U8KGM2), Ipomoea batatas (A0A2U8KGN4)
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brenda