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Information on EC 2.3.1.99 - quinate O-hydroxycinnamoyltransferase
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EC Tree
2.3.1.99 quinate O-hydroxycinnamoyltransferaseIUBMB Comments
Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, but more slowly. Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 chlorogenate---glucarate O-hydroxycinnamoyltransferase, in the formation of caffeoyl-CoA in tomato.
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Word Map
- 2.3.1.99
-
chlorogenic
- phenol
-
phenylpropanoids
- tubers
- potato
-
solanum
- tuberosum
-
quinic
- trans-cinnamate
- cinnamate
- caffeoyl-coa
- agriculture
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
hydroxycinnamoyl-coa quinate hydroxycinnamoyl transferase, shikimate/quinate hydroxycinnamoyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CQT
-
-
-
-
HCT
HQT
hydroxycinnamoyl CoA:quinate hydroxycinnamyl transferase
-
-
-
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hydroxycinnamoyl CoA:quinate O-hydroxycinnamyltransferase
-
-
-
-
hydroxycinnamoyl coenzyme A-quinate transferase
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-
-
-
hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase
hydroxycinnamoyltransferase
hydroxycinnamoyltransferase, quinate
-
-
-
-
shikimate/quinate hydroxycinnamoyltransferase
HQT
-
-
-
-
hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase
-
hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + quinate = CoA + O-feruloylquinate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA:quinate O-(hydroxycinnamoyl)transferase
Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, but more slowly. Involved in the biosynthesis of chlorogenic acid in sweet potato and, with EC 2.3.1.98 chlorogenate---glucarate O-hydroxycinnamoyltransferase, in the formation of caffeoyl-CoA in tomato.
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CAS REGISTRY NUMBER
COMMENTARY
60321-02-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
-
-
-
?
sinapoyl-CoA + quinate
CoA + 5-O-sinapoylquinate
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at 21% the rate of the reaction with feruloyl-CoA
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
best substrate
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
no substrates are citrate, malate, L-(+)-tartrate, UDP-glucose, myo-inositol, tyramine, agmatine
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
cinnamoyl-CoA cannot replace coumaroyl-CoA
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
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not: glucose
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
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at 39% the rate of the reaction with feruloyl-CoA
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
best substrate
-
-
r
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
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coumaric acid, caffeic acid cannot replace coumaroyl-CoA
-
-
r
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
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poor substrates of the reverse reaction are the 3'- or 4'-coumaroylquinates
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-
r
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
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not: glucose
-
-
r
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
-
best substrate
-
-
r
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
reaction of EC 2.3.1.133
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
reaction of EC 2.3.1.133
-
-
?
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
i.e. chlorogenic acid
?
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
i.e. chlorogenic acid
r
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
condensation at 10% the rate of the reaction with feruloyl-CoA
i.e. chlorogenic acid
?
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
i.e. chlorogenic acid
?
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
i.e. chlorogenic acid
r
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
i.e. chlorogenic acid
r
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
-
-
-
r
caffeoyl-CoA + quinate
CoA + chlorogenic acid
the enzyme catalyzes the esterification of quinic acid
-
-
?
caffeoyl-CoA + quinate
CoA + chlorogenic acid
the enzyme catalyzes the esterification of quinic acid
-
-
?
caffeoyl-CoA + quinate
CoA + chlorogenic acid
-
i.e. chlorogenate
-
?
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
reaction of EC 2.3.1.133
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
reaction of EC 2.3.1.133
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
reaction of EC 2.3.1.133
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
caffeoyl-CoA is the most efficient acyl group donor with shikimate as substrate
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-
?
CoA + 5-O-caffeoylquinate
caffeoyl-CoA + quinate
-
-
-
r
feruloyl-CoA + quinate
CoA + O-feruloylquinate
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condensation at 10% the rate of the reaction with coumaroyl-CoA
-
-
r
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
reaction of EC 2.3.1.133
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
feruloyl-CoA shows 10fold lower activity than caffeoyl-CoA with shikimate as substrate
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
reaction of EC 2.3.1.133
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
4-coumaroyl-CoA is the most efficient acyl group donor with quinate as substrate
-
-
?
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
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poor substrate
-
-
?
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
-
-
-
?
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
-
-
-
?
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
-
-
-
?
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
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poor substrate
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-
?
additional information
?
-
-
gene silencing results in a dwarf phenotype and changes in lignin composition, enzyme is involved in phenylpropanoid biosynthesis
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-
?
additional information
?
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analysis of enzymes involved in biosynthesis of curcuminoids
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-
?
additional information
?
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no cosubstrates with quinate: caffeoyl-CoA, feruloyl-CoA
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-
-
additional information
?
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gene silencing results in a decrease in syringyl units and an increases in p-hydroxyphenyl units in lignin, enzyme is involved in phenylpropanoid biosynthesis
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-
?
additional information
?
-
the enzyme controls shikimate and quinate ester intermediates in phenylpropanoid metabolism
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?
additional information
?
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme plays a critical role in phenylpropanoid biosynthetic pathway
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-
?
additional information
?
-
no activity is detected with quinate and feruloyl-CoA or sinapoyl-CoA
-
-
?
additional information
?
-
no cosubstrates with quinate: caffeoyl-CoA, feruloyl-CoA
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-
-
additional information
?
-
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enzyme involved in the biosynthesis of chlorogenic acid
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-
?
additional information
?
-
-
enzyme involved in the biosynthesis of chlorogenic acid
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-
?
additional information
?
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
enzyme plays a role in the endergonic processes involved in the synthetic reactions leading to esterification of quinic acid with hydroxycinnamoyl residues
-
-
?
additional information
?
-
-
analysis of enzymes involved in biosynthesis of ginger
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
caffeoyl-CoA + quinate
CoA + chlorogenic acid
the enzyme catalyzes the esterification of quinic acid
-
-
?
caffeoyl-CoA + quinate
CoA + chlorogenic acid
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
the enzyme catalyzes the esterification of quinic acid
-
-
?
additional information
?
-
-
gene silencing results in a dwarf phenotype and changes in lignin composition, enzyme is involved in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
-
analysis of enzymes involved in biosynthesis of curcuminoids
-
-
?
additional information
?
-
-
gene silencing results in a decrease in syringyl units and an increases in p-hydroxyphenyl units in lignin, enzyme is involved in phenylpropanoid biosynthesis
-
-
?
additional information
?
-
the enzyme controls shikimate and quinate ester intermediates in phenylpropanoid metabolism
-
-
?
additional information
?
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme plays a critical role in phenylpropanoid biosynthetic pathway
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of chlorogenic acid
-
-
?
additional information
?
-
-
enzyme involved in the biosynthesis of chlorogenic acid
-
-
?
additional information
?
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
the enzyme is required for the synthesis of chlorogenic acid
-
-
?
additional information
?
-
-
enzyme plays a role in the endergonic processes involved in the synthetic reactions leading to esterification of quinic acid with hydroxycinnamoyl residues
-
-
?
additional information
?
-
-
analysis of enzymes involved in biosynthesis of ginger
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-[2-Acetamido]-2-iminodiacetic acid
-
i.e. N-[carbamoylmethyl]iminodiacetic acid or ADA
additional information
-
no effect: 2,3-butanedione, phenylmethylsulfonylfluoride and N-methylmaleimide
-
additional information
-
no inhibition by bovine serum albumin, Mg2+ or dithioerythritol
-
additional information
-
not: shikimate; very slight inhibition by Mg2+, Be2+, Ca2+, Cd2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
A Picea abies linkage map based on SNP markers identifies QTLs for four aspects of resistance to Heterobasidion parviporum infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.519
4-coumaroyl-CoA
cosubstrate quinate, pH not specified in the publication, 30°C
0.146
5-O-caffeoylquinate
cosubstrate CoA, pH not specified in the publication, 30°C
0.227
5-O-caffeoylquinate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
0.265
5-O-caffeoylquinate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
0.421
caffeoyl-CoA
cosubstrate quinate, pH 7.0, 25°C
0.914
caffeoyl-CoA
cosubstrate quinate, pH not specified in the publication, 30°C
1.296
caffeoyl-CoA
cosubstrate quinate, pH 7.0, 25°C
0.077
quinate
cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C
0.13
quinate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
0.203
quinate
cosubstrate caffeoyl-CoA, pH not specified in the publication, 30°C
0.444
quinate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
2.473
shikimate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
2.69
shikimate
cosubstrate caffeoyl-CoA, pH 7.0, 25°C
5.579
shikimate
cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.88
4-coumaroyl-CoA
cosubstrate quinate, pH not specified in the publication, 30°C
0.9
5-O-caffeoylquinate
cosubstrate CoA, pH not specified in the publication, 30°C
1.3
caffeoyl-CoA
cosubstrate quinate, pH not specified in the publication, 30°C
0.15
shikimate
cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C
1.65
quinate
cosubstrate caffeoyl-CoA, pH not specified in the publication, 30°C
2.75
quinate
cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY