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Information on EC 2.5.1.62 - chlorophyll synthase
for references in articles please use BRENDA:EC2.5.1.62
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EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.62 chlorophyll synthase
IUBMB Comments
Requires Mg2+. The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur. The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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
showSynonyms
chlorophyll synthase, chlorophyll synthetase, chl synthase, chl synthetase, chlorophyll a synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chl synthase
ChlG
chlorophyll a synthase
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chlorophyll synthase
chlorophyll synthetase
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-
-
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synthase, chlorophyll
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
-
-
-
-
chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
ping-pong mechanism
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chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
active site structure, substrate binding mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
polyprenyl-group transfer
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-
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
chlorophyll a biosynthesis I, chlorophyll a biosynthesis II, chlorophyll a biosynthesis III, chlorophyll a2 biosynthesis, chlorophyll b2 biosynthesis, chlorophyll cycle
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SYSTEMATIC NAME
IUBMB Comments
chlorophyllide-a:phytyl-diphosphate phytyltransferase
Requires Mg2+. The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur. The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9077-08-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
chlorophyllide a + tetraprenyl diphosphate
diphosphate + 3-tetraprenylchlorophyllide a
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Substrates: 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
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phenylamino-Zn-pheophorbide b + phytyl diphosphate
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Substrates: -
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Zn chlorophyllide a + geranylgeranyl diphosphate
Zn chlorophyll a + diphosphate
Substrates: -
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Zn chlorophyllide a + phytyl diphosphate
Zn chlorophyll a + diphosphate
Substrates: -
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Zn-chlorophyllide a + phytyl diphosphate
Zn-chlorophyll a + diphosphate
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Substrates: 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
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chlorophyllide + phytyl diphosphate
chlorophyll + diphosphate
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chlorophyllide + phytyl diphosphate
chlorophyll + diphosphate
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Substrates: -
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chlorophyllide a + farnesyl diphosphate
3-farnesylchlorophyllide a + diphosphate
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Substrates: -
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chlorophyllide a + farnesyl diphosphate
3-farnesylchlorophyllide a + diphosphate
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
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Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
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Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
M0WBJ9
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
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Substrates: 42% of the activity with phythyl diphosphate
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
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Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
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Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
M0WBJ9
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: the enzyme catalyzes the final step of chlorophyll a formation under in leaves of plants
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: chlorophyllide a possesses a central Mg2+ ion
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: marked preference of phytyl diphosphate as substrate over geranylgeranyl diphosphate
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
Substrates: engineered enzyme mutant
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: -
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pheophorbide a + geranylgeranyl diphosphate
?
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Substrates: Mg2+- and Zn2+-complexes are good substrates, the Co2+-, Cu2+- and Ni2+-complexes are neither substrates nor competitive inhibitors
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pheophorbide a + geranylgeranyl diphosphate
?
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Substrates: no esterification of synthetic zinc-pheophorbide a derivatives with the stereochemistry of chlorophyllide aĀ
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additional information
?
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Substrates: phytol, farnesyl, geranylgeranniol and its monophosphate derivative are incorporated into chlorophyll only in the presence of ATP
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additional information
?
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Substrates: the esterification of chlorophyllide to chlorophyll is the last step in chlorophyll biosynthesis, pathway overview
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additional information
?
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Substrates: 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
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additional information
?
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Substrates: 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
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additional information
?
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Substrates: no activity with bacteriochlorophyllide a
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additional information
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Substrates: chlorophyll synthase has a high degree of substrate specificity
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additional information
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Substrates: 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
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additional information
?
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Substrates: hydrogen bonding or electronic interaction involving the carbomethoxy group is not essential for substrate binding
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
-
Substrates: -
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chlorophyllide a + geranylgeranyl diphosphate
geranylgeranylchlorophyllide a + diphosphate
Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
-
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
M0WBJ9
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: the enzyme catalyzes the final step of chlorophyll a formation under in leaves of plants
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
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Substrates: -
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chlorophyllide a + phytyl diphosphate
chlorophyll a + diphosphate
Substrates: -
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additional information
?
-
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Substrates: the esterification of chlorophyllide to chlorophyll is the last step in chlorophyll biosynthesis, pathway overview
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additional information
?
-
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Substrates: 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
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additional information
?
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Substrates: chlorophyll synthase has a high degree of substrate specificity
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
M0WBJ9
light-harvesting-like potein 3, Lil3, assembles with proteins regulating chlorophyll synthesis in etioplasts from barley, and it participates in the regulation of chlorophyllide a esterification. The protein is involved in the regulation of tetrapyrrol biosynthesis, and plant responses to light-stress. Chlorophyll synthase directly interacts with protochlorophyllide-oxidoreductase (EC 1.3.1.33), and light-harvesting-like potein 3, Lil3. Chlorophyllide- and geranylgeranyl diphosphate-dependent assembly of Lil3. Geranylgeranyl reductase (EC 1.3.1.83) interacts with chlorophyll synthase, protochlorophyllide-oxidoreductase, and with itself, but not with light-harvesting-like potein 3. The high-light-inducible protein HliD is not required by the enzyme CHS
-
additional information
-
light-harvesting-like potein 3, Lil3, assembles with proteins regulating chlorophyll synthesis in etioplasts from barley, and it participates in the regulation of chlorophyllide a esterification. The protein is involved in the regulation of tetrapyrrol biosynthesis, and plant responses to light-stress. Chlorophyll synthase directly interacts with protochlorophyllide-oxidoreductase (EC 1.3.1.33), and light-harvesting-like potein 3, Lil3. Chlorophyllide- and geranylgeranyl diphosphate-dependent assembly of Lil3. Geranylgeranyl reductase (EC 1.3.1.83) interacts with chlorophyll synthase, protochlorophyllide-oxidoreductase, and with itself, but not with light-harvesting-like potein 3. The high-light-inducible protein HliD is not required by the enzyme CHS
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cerium
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cerium addition significantly relieves the inhibition of chlorophyll biosynthesis in maize caused by magnesium deficiency and increases chlorophyll content. cerium may partly substitue for magnesium
Magnesium
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magnesium deficiency leads to decrease of chlorophyll contents in maize leaves, with concomitant decrease in the expression levels of magnesium chelatase, magnesium-protoporphyrin IX methyltransferase, and chlorophyll synthase. Magnesium deficiency significantly inhibits the transformation from coproporphyrinogen III or protoporphyrin IX to chlorophyll. Cerium addition significantly relieves the inhibition of chlorophyll biosynthesis in maize caused by magnesium deficiency and increases chlorophyll content
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bacteriochlorophyllide a
-
competitive inhibitor, effect is reversed by an increased level of chlroophyllide a, no cell growth of 50 microM
N-Phenylmaleimide
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since the wild-type enzyme and all other Cys-mutants with the exception of the mutant C304A are inhibited, it is concluded that the inhibitor binds to a non-essential Cys residue to abolish activity
additional information
-
hairpin structure in plasmid is tran-activated by the yeast transcription factor that is active in veins of leaves and petiols leads to post-transcriptional silencing of the enzyme by RNA interference
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
geranylgeranyl diphosphate
-
lysate mixed into reaction buffer (120 mM potassium acetate, 10 mM magnesium acetate, 50 mM HEPES-KOH, pH 7.6, 14 mM 2-mercaptoethanol, 10% glycerol, and 0.5 mM ATP), 30Ā°C
0.32
phytyl diphosphate
-
lysate mixed into reaction buffer (120 mM potassium acetate, 10 mM magnesium acetate, 50 mM HEPES-KOH, pH 7.6, 14 mM 2-mercaptoethanol, 10% glycerol, and 0.5 mM ATP), 30Ā°C
0.09
chlorophyllide a
pH 7.6, 30Ā°C, recombinant wild-type enzyme
0.11
chlorophyllide a
pH 7.6, 30Ā°C, recombinant enzyme mutant I44F
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
bacteriochlorophyllide a
-
in the presence of sufficient geranylgeranyl diphosphate as substrate, lysate mixed into reaction buffer (120 mM potassium acetate, 10 mM magnesium acetate, 50 mM HEPES-KOH, pH 7.6, 14 mM 2-mercaptoethanol, 10% glycerol, and 0.5 mM ATP), 30Ā°C
1.14
bacteriochlorophyllide a
-
in the presence of sufficient phytyl diphosphate as substrate, lysate mixed into reaction buffer (120 mM potassium acetate, 10 mM magnesium acetate, 50 mM HEPES-KOH, pH 7.6, 14 mM 2-mercaptoethanol, 10% glycerol, and 0.5 mM ATP), 30Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
spectrophotometric assay method development with Zn-chlorophyllide a as substrate, a method based on the spectral differences between Zn-chlorophyll a and chlorophyll a, overview
additional information
leaf segments are laid out on buffer-moistened filter paper containing Zn chlorophyllide a for 8 h in the dark, formed product is analyzed by HPLC, overexpression leads to 120-140% chlorophyll synthase activity, expression of the antisense RNA reduces activity to less than 20% and 40%
additional information
leaf segments are laid out on buffer-moistened filter paper containing Zn chlorophyllide a for 8 h in the dark, formed product is analyzed by HPLC, overexpression leads to 120-140% chlorophyll synthase activity, expression of the antisense RNA reduces activity to less than 20% and 40%
additional information
-
leaf segments are laid out on buffer-moistened filter paper containing Zn chlorophyllide a for 8 h in the dark, formed product is analyzed by HPLC, overexpression leads to 120-140% chlorophyll synthase activity, expression of the antisense RNA reduces activity to less than 20% and 40%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enhancer trap line J1511 with yeast transcription factor GAL4-VP16
-
-
brenda
Nicotiana tabacum cv. Samsun NN, transgenic tobacco plants
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
nearly normal or partially reduced activity in bleached leaf tissue compared with green primary leaves
brenda
-
nearly normal or partially reduced activity in bleached leaf tissue compared with green primary leaves
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
peripheral membrane protein which releases its product into the membrane
brenda
-
chlorophyll synthetase activity is relocated from transforming prolamellar bodies to developing thylakoids during irradiation of dark-grown Triticum aestivum
brenda
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chlorophyll synthetase activity is relocated from transforming prolamellar bodies to developing thylakoids during irradiation of dark-grown Triticum aestivum
brenda
-
enzyme is present in an inactive state
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
additional information
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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the interaction between ChlG and Ycf39 is disrupted by high light stress
additional information
the interaction between ChlG and Ycf39 is disrupted by high light stress
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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