2.5.1.62: chlorophyll synthase
This is an abbreviated version!
For detailed information about chlorophyll synthase, go to the full flat file.
Word Map on EC 2.5.1.62
-
2.5.1.62
-
photosystems
-
protochlorophyllide
-
phytol
-
bacteriochlorophyll
-
tetrapyrrole
-
chelatase
-
geranylgeraniol
-
etioplasts
-
bacteriochlorophyllide
-
chlorophyllase
-
mg-protoporphyrin
-
magnesium-protoporphyrin
-
chlide
-
high-light-inducible
-
prolamellar
-
insertase
-
chlorophyll-binding
-
nadph:protochlorophyllide
-
synthesis
-
agriculture
-
food industry
- 2.5.1.62
-
photosystems
- protochlorophyllide
- phytol
- bacteriochlorophyll
- tetrapyrrole
- chelatase
- geranylgeraniol
- etioplasts
- bacteriochlorophyllide
- chlorophyllase
- mg-protoporphyrin
-
magnesium-protoporphyrin
-
chlide
-
high-light-inducible
-
prolamellar
-
insertase
-
chlorophyll-binding
-
nadph:protochlorophyllide
- synthesis
- agriculture
- food industry
Reaction
Synonyms
Chl synthase, Chl synthetase, Chl-synthase, Chl-synthetase, ChlG, chlorophyll a synthase, chlorophyll synthase, chlorophyll synthetase, CHS, NtCHLG, synthase, chlorophyll
ECTree
2.5.1.62 chlorophyll synthaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.5.1.62 - chlorophyll synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C109A
-
mutant enzyme exhibits nearly no enzymatic activity, N-phenylmaleimide results in an additional decrease of activity
C130A
-
mutant enzyme shows reduced activity and sensitivity to N-phenylmaleimide
C137A
-
mutant enzyme is not impaired in enzymatic activity and shows the same inhibition by N-phenylmaleimide as the wild-type enzyme
C262A
-
mutant enzyme is not impaired in enzymatic activity and shows the same inhibition by N-phenylmaleimide as the wild-type enzyme
C304A
-
as active as the wild-type enzyme, mutant enzyme is not inhibited by N-phenylmaleimide
P198S
the chlorophyll-deficient mutant yellow-green leaf1 (ygl1) with amino acid substitution P198S shows yellow-green leaves in young plants with decreased chlorophyll synthesis, increased level of tetrapyrrole intermediates, and delayed chloroplast development, and exhibits approximately 35.22% and 21.75% esterification of chlorophyllide a with geranylgeranly diphosphate and phytyl diphosphate, respectively, compared to wild type recombinant enzyme
I44F
naturyll occuring mutant, that also shows bacteriochlorophyl syntase activity, EC 2.5.1.133
additional information
additional information
-
a hair-pin construct is activated in the chlorophyll synthase gene in veins and cells neighboring veins, photosynthesis is reduced in these cells, growth and fitness of the plants are compromised
additional information
-
deletion of the presequence yields a protein with full activity, even further deletion of the N-terminus including amino acid residues 1-87 results in a core protein that is still enzymatically active. Deletion of the 88 N-terminal residues yields a protein without enzymatic activity. At the C-terminus, only one residue H378 can be deleted without loss of activity, while deletion of S77 together with H378, and all shorter sequences show no activity
additional information
-
barley mutant albostrains show a severe block in chloroplast development as a result of a mutationally induced lack in plastid ribosomes, phenotype: white leaves due to chlorophyll deficiency, analysis of the tetrapyrrole biosynthetic pathway shows that the mutant has reduced activity of Mg-chelatase, Fe-chelatase, and Mg-protoporphyrin IX methyltransferase, several other enzymes involved in the pathway are deregulated, e.g. the chlorophyll synthetase, carotenoid content in leaves, overview
additional information
M0WBJ9
chlorophyll synthase is fused to the N-terminus of the Cub moiety protein to generate BTC-CHS
additional information
-
chlorophyll synthase is fused to the N-terminus of the Cub moiety protein to generate BTC-CHS
additional information
construction of a yidC-Flag/DELTAyidC strain that produces near-native amounts of the C-terminally FLAG-tagged YidC and normal levels of photosynthetic complexes, a very low amount of ChlG coelutes with YidC-FLAG. The HliD-less strain of Synechocystis lacks ChlG subcomplexes and accumulates chlorophyllide. The increased pool of chlorophyllide can be the consequence of lowered ChlG activity but can also arise from a defect in chlorophyll recycling
additional information
improvements to photosynthetic efficiency could be achieved by manipulating pigment biosynthetic pathways of photosynthetic organisms in order to increase the spectral coverage for light absorption via development of organisms that can produce both bacteriochlorophylls and chlorophylls, engineering of the bacteriochlorophyll-utilizing anoxygenic phototroph Rhodobacter sphaeroides to make chlorophyll a. Deletion of genes responsible for the bacteriochlorophyll-specific modifications of chlorophyllide and replacement of the native bacteriochlorophyll synthase with a cyanobacterial chlorophyll synthase results in the production of chlorophyll a. Chlorophyll a can be assembled in vivo into the plant water-soluble chlorophyll protein, heterologously produced in Rhodobacter sphaeroides, method optimization, overview
