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chlorophyllide + phytyl diphosphate
chlorophyll + diphosphate
chlorophyllide a + farnesyl diphosphate
3-farnesylchlorophyllide a + diphosphate
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
chlorophyllide a + tetraprenyl diphosphate
diphosphate + 3-tetraprenylchlorophyllide a
-
ping-pong mechanism. Tetraprenyl diphosphate must bind to the enzyme as the first substrate and esterification occurs when the pre-loaded enzyme meets the second substrate
-
-
?
phenylamino-Zn-pheophorbide b + phytyl diphosphate
?
-
-
-
-
?
pheophorbide a + geranylgeranyl diphosphate
?
Zn chlorophyllide a + geranylgeranyl diphosphate
Zn chlorophyll a + diphosphate
-
-
-
?
Zn chlorophyllide a + phytyl diphosphate
Zn chlorophyll a + diphosphate
-
-
-
?
Zn-chlorophyllide a + phytyl diphosphate
Zn-chlorophyll a + diphosphate
-
Zn-chlorophyllide a possesses a central Zn2+ ion instead of Mg2+, can be used as as the substrate for chlorophyll synthetase in briefly illuminated etiolated rye leaves
-
-
?
Zn-pheophorbide a + phytyl diphosphate
?
-
-
-
-
?
Zn-pheophorbide b + phytyl diphosphate
?
-
-
-
-
?
additional information
?
-
chlorophyllide + phytyl diphosphate
chlorophyll + diphosphate
-
-
-
-
?
chlorophyllide + phytyl diphosphate
chlorophyll + diphosphate
-
-
-
-
?
chlorophyllide a + farnesyl diphosphate
3-farnesylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + farnesyl diphosphate
3-farnesylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
M0WBJ9
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
42% of the activity with phythyl diphosphate
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
?
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
M0WBJ9
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
the enzyme catalyzes the final step of chlorophyll a formation under in leaves of plants
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
chlorophyllide a possesses a central Mg2+ ion
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
marked preference of phytyl diphosphate as substrate over geranylgeranyl diphosphate
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
engineered enzyme mutant
-
-
?
chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
-
-
-
?
pheophorbide a + geranylgeranyl diphosphate
?
-
Mg2+- and Zn2+-complexes are good substrates, the Co2+-, Cu2+- and Ni2+-complexes are neither substrates nor competitive inhibitors
-
-
?
pheophorbide a + geranylgeranyl diphosphate
?
-
no esterification of synthetic zinc-pheophorbide a derivatives with the stereochemistry of chlorophyllide aĀ
-
-
?
additional information
?
-
-
phytol, farnesyl, geranylgeranniol and its monophosphate derivative are incorporated into chlorophyll only in the presence of ATP
-
-
?
additional information
?
-
-
the esterification of chlorophyllide to chlorophyll is the last step in chlorophyll biosynthesis, pathway overview
-
-
?
additional information
?
-
-
esterification of chlorophyllide to chlorophyll, substrate binding mechanism and specificity, enzyme might form a complex with NADPH:protochlorophyllide oxidoreductase which catalyzes the last but one step in the pathway, analysis of enzyme activity with substrate derivatives bearing large, space-filling substituents reveals that the substrates cannot be bound to both enzymes simultaneously, overview
-
-
?
additional information
?
-
-
metabolic control of the tetrapyrrole biosynthetic pathway for porphyrin distribution, e.g. by different metabolic feedback loops, bidirectional communication between plastids and nucleus, carotenoid content in leaves, overview
-
-
?
additional information
?
-
-
no activity with bacteriochlorophyllide a
-
-
?
additional information
?
-
chlorophyll synthase has a high degree of substrate specificity
-
-
?
additional information
?
-
ultrafast time-resolved absorption spectroscopy is used to follow chlorophyll a and carotenoid excited-state dynamics in the complex of N-terminally 3xFlag-tagged Chl synthase with high-light inducible proteins, steady-state absorption spectra, overview. Cyanobacterial high-light inducible proteins (Hlips)/the enzyme complex exhibit significant chlorophyll a quenching via energy transfer from the Qy state of Chl a to the S1 state of the carotenoid, kinetics
-
-
?
additional information
?
-
-
hydrogen bonding or electronic interaction involving the carbomethoxy group is not essential for substrate binding
-
-
?
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evolution
the predicted sequence of ChlG of Synechocystis sp. PCC 6803 is considerably similar (35% identity) to that of Rhodobacter sphaeroides BchG, each enzyme has a high level of substrate specificity to distinguish its own substrate from the other. But the BchG activity of Synechocystis chlorophyll synthase mutant ChlGI44F and the ChlG activity of bacteriochlorophyll synthase mutant BchGF28I suggest that ChlG/EC 2.5.1.62 and BchG/EC 2.5.1.133 are evolutionarily related enzymes
malfunction
-
gene silencing in vein cells and neighboring cells reduces chlorophyll accumulation around veins by 60-90%, CO2 fixation by minor veins from the xylem stream and the amount of specific metabolites such as soluble sugars associated with carbohydrate metabolism and the shikimate pathway are reduced, the abundance of transcripts encoding components of phosphoenolpyruvate generating pathways are altered, leaf senescence, growth rate, and seed size are reduced
malfunction
reduced enzyme activity does not result in accumulation of chlorophyllide, it causes reduced 5-aminolevulinic acid formation and Mg chelatase and ferrochelatase activity, growth is retarded, leaves are pale green (20% wild type chlorophyll content), overexpression is correlated with enhanced 5-aminolevulinic acid synthesizing capacity and more chelatase activity, the results point to a feedback control of the biosynthesis pathway, the phenotype is not distinguishable from the wild type
malfunction
mutant dlt4-1 is pale green and heat sensitive due to the reduced Chl content. Besides Chl synthase, Lhcb1, a light-harvesting Chl a/b-binding protein, is reduced to about 60% of the wild-type level in chlg-1. The chlG missense mutation is responsible for a light-dependent, heat-induced cotyledon bleaching phenotype. Following heat treatment, mutant chlg-1 but not wild-type seedlings accumulate a substantial level of chlorophyllide a, which results in a surge of phototoxic singlet oxygen. The mutation destabilized the chlorophyll synthase proteins and causes a conditional blockage of esterification of chlorophyllide a after heat stress. Accumulation of chlorophyllide a after heat treatment occurs during recovery in the dark in the light-grown but not the etiolated seedlings, suggesting that the accumulated chlorophyllides were not derived from de novo biosynthesis but from de-esterification of the existing chlorophylls. The triple mutant harboring the ChlG mutant allele and null mutations of chlorophyllase 1 (CLH1) and CLH2 indicates that the known chlorophyllases are not responsible for the accumulation of chlorophyllide a in chlg-1
metabolism
enzyme catalyzes the last step in the chlorophyll biosynthetic pathway
metabolism
identification of a link between chlorophyll biosynthesis and the Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. This close physical linkage coordinates the arrival of pigments and nascent apoproteins to produce photosynthetic pigment protein complexes with minimal risk of accumulating phototoxic unbound chlorophylls
metabolism
M0WBJ9
light-harvesting-like potein 3, Lil3, participates in the regulation of chlorophyllide a esterification
physiological function
chlorophyll synthase is an important enzyme of the chlorophyll biosynthetic pathway catalyzing attachment of phytol/geranylgeraniol tail to the chlorophyllide molecule
physiological function
chlorophyll synthase is involved in reutilization of chlorophyllide during chlorophyll turnover
physiological function
the enzymatically active complex of cyanobacterial chlorophyll synthase with the high-light-inducible protein HliD associates with the Ycf39 protein, a putative assembly factor for photosystem II, and the YidC/Alb3 insertase, there is also evidence for the presence of SecY and ribosome subunits in the complex. Protein HliD is apparently required for assembly of FLAG-tagged enzyme ChlG into larger complexes with other proteins such as Ycf39. The ChG-HliD subcomplex contains chlorophyll, chlorophyllide, and carotenoids
additional information
M0WBJ9
in the presence of light or chlorophyllide, chlorophyll synthase interacts with protochlorophyllide-oxidoreductase, EC 1.3.1.33, and light-harvesting-like potein 3, Lil3
additional information
-
in the presence of light or chlorophyllide, chlorophyll synthase interacts with protochlorophyllide-oxidoreductase, EC 1.3.1.33, and light-harvesting-like potein 3, Lil3
additional information
residue I44 is important for the substrate specificities of ChlG
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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
D147A
-
mutant enzyme without activity
D150A
-
mutant enzyme without activity
D154A
-
mutant enzyme without activity
N146A
-
mutant enzyme without activity
R151A
-
mutant enzyme with 35% of the activity compared to wild-type enzyme
R161A
-
mutant enzyme without activity
R161H
-
mutant enzyme with 1% activity compared to wild type enzyme
R161K
-
mutant enzyme with 34% activity compared to wild type enzyme
R284A
-
mutant enzyme shows wild-type activity
R91A
-
mutant enzyme without activity
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
-
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
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Schmid, H.C.; Rassadina, V.; Oster, U.; Schoch, S.; Rüdiger, W.
Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is an obligatory step in chlorophyll biosynthesis
Biol. Chem.
383
1769-1778
2002
Avena sativa
brenda
Oster, U.; Bauer, C.E.; Rüdiger, W.
Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli
J. Biol. Chem.
272
9671-9676
1997
Synechocystis sp.
brenda
Rüdiger, W.; Benz, J.; Guthoff.C.
Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes
Eur. J. Biochem.
109
193-200
1980
Avena sativa
brenda
Vezitskii, A.Y.; Lezhneva, L.A.; Scherbakov, R.A.; Rassadina, V.V.; Averina, N.G.
Activity of chlorophyll synthetase and chlorophyll b reductase in the chlorophyll-deficient plastome mutant of sunflower
Russ. J. Plant Physiol.
46
502-506
1999
Helianthus annuus
-
brenda
Schmid, H.C.; Oster, U.; Kogel, J.; Lenz, S.; Rüdiger, W.
Cloning and characterisation of chlorophyll synthase from Avena sativa
Biol. Chem.
382
903-911
2001
Avena sativa
brenda
Lindsten, A.; Welch, C.J.; Schoch, S.; Ryberg, A.; Rüdiger, W.; Sundqvist, C.
Chlorophyll synthetase is latent in well preserved prolamellar bodies of etiolated wheat
Physiol. Plant.
80
277-285
1990
Triticum aestivum
-
brenda
Lindsten, A.; Wiktorsson, B.; Ryberg, M.; Sundqvist, C.
Chlorophyll synthetase activity is relocated from transforming prolamellar bodies to developing thylakoids during irradiation of dark-grown wheat
Physiol. Plant.
88
29-36
1993
Triticum aestivum
-
brenda
Dogbo, O.; Bardat, F.; Camara, B.
Terpenoid metabolism in plastids: activity, localization and substrate specificity of chlorophyll synthetase in Capsicum annuum plastids
Physiol. Veg.
22
75-82
1984
Capsicum annuum
-
brenda
Kreuz, K.; Kleinig, H.
Chlorophyll synthetase in chlorophyll-free chromoplasts
Plant Cell Rep.
1
40-42
1981
Narcissus pseudonarcissus
brenda
Hess, W.R.; Blank-Huber, M.; Fieder, B.; Boerner, T.; Ruediger, W.
Chlorophyll synthetase and chloroplast tRNAGlu are present in heat-bleached, ribosome-deficient plastids
J. Plant Physiol.
139
427-430
1992
Avena sativa, Secale cereale
-
brenda
Helfrich, M.; Ruediger, W.
Various metallopheophorbides as substrates for chlorophyll synthetase
Z. Naturforsch. C
47
231-238
1992
Triticum aestivum
-
brenda
Helfrich, M.; Schoch, S.; Lempert, U.; Cmiel, E.; Ruediger, W.
Chlorophyll synthetase cannot synthesize chlorophyll a'
Eur. J. Biochem.
219
267-275
1994
Triticum aestivum
brenda
Ruediger, W.; Bohm, S.; Helfrich, M.; Schulz, S.; Schoch, S.
Enzymes of the last steps of chlorophyll biosynthesis: modification of the substrate structure helps to understand the topology of the active centers
Biochemistry
44
10864-10872
2005
Avena sativa
brenda
Yaronskaya, E.; Ziemann, V.; Walter, G.; Averina, N.; Boerner, T.; Grimm, B.
Metabolic control of the tetrapyrrole biosynthetic pathway for porphyrin distribution in the barley mutant albostrians
Plant J.
35
512-522
2003
Hordeum vulgare
brenda
Shcherbakov, R.A.; Shalygo, N.V.
Determination of chlorophyll synthetase activity in green tobacco leaves using exogenous Zn-chlorophyllide a
J. Appl. Spectr.
73
103-106
2006
Nicotiana tabacum
-
brenda
Blomqvist, L.A.; Ryberg, M.; Sundqvist, C.
Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development
Photosynth. Res.
96
37-50
2008
Triticum aestivum
brenda
Wu, Z.; Zhang, X.; He, B.; Diao, L.; Sheng, S.; Wang, J.; Guo, X.; Su, N.; Wang, L.; Jiang, L.; Wang, C.; Zhai, H.; Wan, J.
A chlorophyll-deficient rice mutant with impaired chlorophyllide esterification in chlorophyll biosynthesis
Plant Physiol.
145
29-40
2007
Oryza sativa (A4GUA1), Oryza sativa
brenda
Kim, E.J.; Lee, J.K.
Competitive inhibitions of the chlorophyll synthase of Synechocystis sp. strain PCC 6803 by bacteriochlorophyllide a and the bacteriochlorophyll synthase of Rhodobacter sphaeroides by chlorophyllide a
J. Bacteriol.
192
198-207
2010
Synechocystis sp. PCC 6803
brenda
Janacek, S.H.; Trenkamp, S.; Palmer, B.; Brown, N.J.; Parsley, K.; Stanley, S.; Astley, H.M.; Rolfe, S.A.; Paul Quick, W.; Fernie, A.R.; Hibberd, J.M.
Photosynthesis in cells around veins of the C(3) plant Arabidopsis thaliana is important for both the shikimate pathway and leaf senescence as well as contributing to plant fitness
Plant J.
59
329-343
2009
Arabidopsis thaliana
brenda
Shalygo, N.; Czarnecki, O.; Peter, E.; Grimm, B.
Expression of chlorophyll synthase is also involved in feedback-control of chlorophyll biosynthesis
Plant Mol. Biol.
71
425-436
2009
Nicotiana tabacum (C3W4Q1), Nicotiana tabacum (C3W4Q2), Nicotiana tabacum
brenda
Zhou, M.; Gong, X.; Ying, W.; Chao, L.; Hong, M.; Wang, L.; Fashui, H.
Cerium relieves the inhibition of chlorophyll biosynthesis of maize caused by magnesium deficiency
Biol. Trace Elem. Res.
143
468-477
2011
Zea mays
brenda
Hitchcock, A.; Jackson, P.J.; Chidgey, J.W.; Dickman, M.J.; Hunter, C.N.; Canniffe, D.P.
Biosynthesis of chlorophyll a in a purple bacterial phototroph and assembly into a plant chlorophyll-protein complex
ACS Synth. Biol.
5
948-954
2016
Synechocystis sp. PCC 6803 (Q55145)
brenda
Niedzwiedzki, D.M.; Tronina, T.; Liu, H.; Staleva, H.; Komenda, J.; Sobotka, R.; Blankenship, R.E.; Polivka, T.
Carotenoid-induced non-photochemical quenching in the cyanobacterial chlorophyll synthase-HliC/D complex
Biochim. Biophys. Acta
1857
1430-1439
2016
Synechocystis sp. PCC 6803 (Q55145)
brenda
Kim, E.J.; Kim, H.; Lee, J.K.
The photoheterotrophic growth of bacteriochlorophyll synthase-deficient mutant of Rhodobacter sphaeroides is restored by I44F mutant chlorophyll synthase of Synechocystis sp. PCC 6803
J. Microbiol. Biotechnol.
26
959-966
2016
Synechocystis sp. PCC 6803 (Q55145)
brenda
Chidgey, J.W.; Linhartova, M.; Komenda, J.; Jackson, P.J.; Dickman, M.J.; Canniffe, D.P.; Konik, P.; Pilny, J.; Hunter, C.N.; Sobotka, R.
A cyanobacterial chlorophyll synthase-HliD complex associates with the Ycf39 protein and the YidC/Alb3 insertase
Plant Cell
26
1267-1279
2014
Synechocystis sp. PCC 6803 (Q55145)
brenda
Lin, Y.P.; Lee, T.Y.; Tanaka, A.; Charng, Y.Y.
Analysis of an Arabidopsis heat-sensitive mutant reveals that chlorophyll synthase is involved in reutilization of chlorophyllide during chlorophyll turnover
Plant J.
80
14-26
2014
Arabidopsis thaliana (Q38833)
brenda
Mork-Jansson, A.; Bue, A.K.; Gargano, D.; Furnes, C.; Reisinger, V.; Arnold, J.; Kmiec, K.; Eichacker, L.A.
Lil3 assembles with proteins regulating chlorophyll synthesis in barley
PLoS ONE
10
e0133145
2015
Hordeum vulgare (M0WBJ9), Hordeum vulgare
brenda
Proctor, M.S.; Chidgey, J.W.; Shukla, M.K.; Jackson, P.J.; Sobotka, R.; Hunter, C.N.; Hitchcock, A.
Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertase
FEBS Lett.
592
3062-3073
2018
Chlamydomonas reinhardtii (A8JFJ1), Arabidopsis thaliana (Q38833)
brenda
Yu, X.; Hu, S.; He, C.; Zhou, J.; Qu, F.; Ai, Z.; Chen, Y.; Ni, D.
Chlorophyll metabolism in postharvest tea (Camellia sinensis L.) leaves Variations in color values, chlorophyll derivatives, and gene expression levels under different withering treatments
J. Agric. Food Chem.
67
10624-10636
2019
Camellia sinensis
brenda