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Enzyme Nomenclature
Information on EC 2.3.1.99 - quinate O-hydroxycinnamoyltransferase
Word Map on EC 2.3.1.99
- 2.3.1.99
-
chlorogenic
- phenol
- tuberosum
- caffeoyl-coa
- potato
-
solanum
- medicine
- cinnamate
-
phenylpropanoids
- trans-cinnamate
- tubers
- agriculture
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.99
-
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RECOMMENDED NAME
GeneOntology No.
quinate O-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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, displays hydroxycinnamoyl-Coenzyme A:quinate hydroxycinnamoyl transferase activity and chlorogenate:chlorogenate transferase activity
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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the enzyme belongs to the superfamily of BAHD acyltransferases. The conserved sequence motifs HxxxDG and DFGWG are surrounded by differing amino acid environments which show typical features for hydroxycinnamoyl-CoA:hydroxyphenyllactic acid hydroxycinnamoyltransferase, RAS, and hydroxycinnamoyl-CoA:shikimic acid hydroxycinnamoyltransferase/hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase, HST/HQT
metabolism
metabolism
polyphenol metabolism and chlorogenic acid synthesis pathway involving the enzyme, overview
metabolism
polyphenol metabolism and chlorogenic acid synthesis pathway involving the enzyme, overview
metabolism
HQT is involved in one of three possible pathways of chlorogenate biosynthesis, overview
metabolism
-
quinate is used as acceptor molecule by a HQT and 4-coumaroylquinate is formed, which is hydroxylated by a member of the CYP98A family to chlorogenic acid
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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
caffeoyl-CoA + quinate
CoA + 3-O-caffeoylquinate
-
i.e. chlorogenate
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
feruloyl-CoA shows 10fold lower activity than caffeoyl-CoA with shikimate as substrate
-
-
?
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
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-
?
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
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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
-
coumaric acid, caffeic acid cannot replace coumaroyl-CoA
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-
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
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best substrate
-
-
r
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 + 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 + shikimate
CoA + 5-O-caffeoylshikimate
caffeoyl-CoA is the most efficient acyl group donor with shikimate as substrate
-
-
?
feruloyl-CoA + quinate
CoA + O-feruloylquinate
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condensation at 10% the rate of the reaction with coumaroyl-CoA
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-
r
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
?
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gene silencing results in a dwarf phenotype and changes in lignin composition, enzyme is involved in phenylpropanoid biosynthesis
-
-
-
additional information
?
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analysis of enzymes involved in biosynthesis of curcuminoids
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-
additional information
?
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enzyme involved in the biosynthesis of chlorogenic acid
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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
?
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the enzyme controls shikimate and quinate ester intermediates in phenylpropanoid metabolism
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-
additional information
?
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the enzyme is required for the synthesis of chlorogenic acid
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-
additional information
?
-
the enzyme is required for the synthesis of chlorogenic acid
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-
-
additional information
?
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-
the enzyme plays a critical role in phenylpropanoid biosynthetic pathway
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-
additional information
?
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no activity is detected with quinate and feruloyl-CoA or sinapoyl-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
?
-
the enzyme is required for the synthesis of chlorogenic acid
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-
-
additional information
?
-
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the enzyme is required for the synthesis of chlorogenic acid
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-
-
additional information
?
-
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enzyme plays a role in the endergonic processes involved in the synthetic reactions leading to esterification of quinic acid with hydroxycinnamoyl residues
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-
-
additional information
?
-
-
analysis of enzymes involved in biosynthesis of ginger
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
C3PTS8
the enzyme catalyzes the esterification of quinic acid
-
-
?
caffeoyl-CoA + quinate
CoA + chlorogenic acid
C3PTS7
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
C3PTS8
the enzyme catalyzes the esterification of quinic acid
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
C3PTS7
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
?
-
-
enzyme involved in the biosynthesis of chlorogenic acid
-
-
-
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
?
-
Q8GSM7
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
?
-
Q70G33
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
?
-
Q70G32
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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INHIBITORS
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
change of enzyme activity during a 1-year growth period
additional information
-
change of enzyme activity during growth and ripening
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression in leaves is below the detection level of the immunological method, only faint level in flowers
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme catalyzes different reactions in different compartments
enzyme catalyzes different reactions in different compartments
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
65% loss of activity after 5 min, phosphate buffer protects: 12% loss after 5 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
recombinant His-tagged HQT from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of His-tagged HQT in Escherichia coli
expression in Escherichia coli as fusion protein with 15 amino acid S-TAG
HQT, DNA and amino acid sequence determination and analysis, phylogenetic analysis
HQT, DNA and amino acid sequence determination and analysis, phylogenetic analysis, PCR real-time expression analysis, recombinant expression in Escherichia coli
recombinant protein fused to glutathione-S-transferase is expressed in
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in the expression level of HQT in UV-C treated leaves
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H276Y
58% of wild-type activity for production of dicaffeoylquinic acids, 92% of wild-type hydroxycinnamoyltranferase activity
additional information
-
downregulation of enzyme by antisense RNA or RNA interference results in compositional changes in lignin and wall-bound hydroxycinnamic acids. No changes in the levels of acylated flavonoids are observed
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
overexpression of the enzyme in tomato causes plants to accumulate higher levels of chlorogenic acid, with no side-effects on the levels of other soluble phenolics. Plants show improved antioxidant capacity and resistance to infection by bacterial pathogens. Tomatoes with elevated levels of chlorogenic acid could be used in foods with specific benefits for human health
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.99)
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