Information on EC 2.3.1.133 - shikimate O-hydroxycinnamoyltransferase

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The expected taxonomic range for this enzyme is: Euphyllophyta

EC NUMBER
COMMENTARY
2.3.1.133
-
RECOMMENDED NAME
GeneOntology No.
shikimate O-hydroxycinnamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate
show the reaction diagram
quasi-independent bi-bi random mechanism
-
4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chlorogenic acid biosynthesis I
-
chlorogenic acid biosynthesis II
-
Flavonoid biosynthesis
-
phaselate biosynthesis
-
Phenylpropanoid biosynthesis
-
phenylpropanoid biosynthesis
-
Stilbenoid, diarylheptanoid and gingerol biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
4-coumaroyl-CoA:shikimate O-(hydroxycinnamoyl)transferase
Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, but more slowly.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CST
-
-
-
-
HCS/QT
-
-
HCT
-
-
-
-
HCT
A4ZKE4
-
HCT1
B6D7P1, B6DQK4
two cDNAs are isolated HCT1A and HCT1B which are nearly identical
HCT2
B6D7P2
-
HQT
C3PTS8
-
HST
-
-
-
-
hydroxycinnamoyl CoA quinate/shikimate hydroxycinnamoyl transferase
-
-
hydroxycinnamoyl CoA:shikimate hydroxycinnamoyl transferase
-
-
hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase
A4ZKE4
-
hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase
-
-
hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase
C3PTS8
-
hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase
C3PTS7
-
hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl transferase
-
-
-
-
hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl-transferase
E8ZAP2
-
hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyltransferase
-
-
hydroxycinnamoyl-CoA:shikimate O-hydroxycinnamoyl transferase
-
-
-
-
hydroxycinnamoyl-CoA:shikimate/quinate hydroxycinnamoyltransferase
-
-
-
-
hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase
-
-
hydroxycinnamoyltransferase
C3PTS8
-
hydroxycinnamoyltransferase
C3PTS7
-
hydroxycinnamoyltransferase
B6D7P1, B6D7P2, B6DQK4
-
hydroxycinnamoyltransferase, shikimate
-
-
-
-
OsHCT4
-
gene name
p-coumaroyl shikimate transferase
-
-
p-coumaroyl-CoA:5-O-shikimate p-coumaroyl transferase
-
-
p-coumaroyl-CoA:shikimic acid p-coumaroyl transferase
-
-
-
-
p-hydroxycinnamoyl-CoA:shikimate-p-hydroxycinnamoyl transferase
-
-
-
-
shikimate hydroxycinnamoyltransferase
-
-
-
-
shikimate hydroxycinnamoyltransferase
-
-
shikimate hydroxycinnamoyltransferase
-
-
CAS REGISTRY NUMBER
COMMENTARY
73904-44-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
D.F.L. von Schlechtendal
-
-
Manually annotated by BRENDA team
Medicago sativa L.
-
-
Manually annotated by BRENDA team
SW and EMX-1
-
-
Manually annotated by BRENDA team
gene OsHCT4
-
-
Manually annotated by BRENDA team
young green dates
-
-
Manually annotated by BRENDA team
; genes PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7
-
-
Manually annotated by BRENDA team
rye, var. Kustro
-
-
Manually annotated by BRENDA team
cDNA HCT1A (almost identical to HCT1B)
UniProt
Manually annotated by BRENDA team
cDNA HCT1B (almost identical to HCT1A)
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
A4ZKE4, -
HCT belongs to the large plant acyl-CoA-dependent BAHD acyltransferase superfamily
evolution
-
HCT is a member of the BAHD [BEAT (benzylalcohol O-acetyltransferase)] family acyltransferases; HCT is a member of the BAHD, i.e. BEAT (benzylalcohol O-acetyltransferase), family acyltransferases
evolution
-
OsHCT1 and OsHCT2 are members of the HCS/QT family, while OsHCT3 and OsHCT4 belong to a distinct group. OsHCT3 and OsHCT4 may employ a different acyl group acceptor
evolution
E8ZAP2, -
HST belongs to the large plant acyl-CoA-dependent BAHD acyltransferase superfamily characterized by mostly conserved sequence motifs, the HxxxD(G) motif containing the catalytically active histidine residue and the DFGWG motif close to the C terminus, phylogenetic analysis, overview
metabolism
A4ZKE4, -
the last step in CGA biosynthesis is generally catalysed by a specific hydroxycinnamoyl-CoA quinate hydroxycinnamoyltransferase, HQT (c.f. EC 2.3.1.99), but it can also be catalysed by the more widely distributed hydroxycinnamoyl-CoA shikimate/quinate hydroxycinnamoyltransferase, HCT, substrate specifities of the HCT key enzyme, overview
metabolism
-
HCT is likely to be involved in lignin biosynthesis, overview; PeHCT might be involved in lignin biosynthesis by formation of 4-coumaroyl shikimate
additional information
-
PeHCT contains a conserved HXXXDG motif that is found in acyltransferase
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + 3-hydroxyanthranilate
CoA + 3-(4-coumaroyl)oxyanthranilate
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + 3-hydroxybenzoate
CoA + 3-(4-coumaroyl)oxybenzoate
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + glycerol
CoA + 2-O-(4-coumaroyl)glycerol + 1-O-(4-coumaroyl)glycerol
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + L-malate
CoA + 2-O-(4-coumaryl)-L-malate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
Q8GSM7
-
-
-
r
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
C3PTS7, -
-
-
-
r
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
reaction products are detected when quinic acid is used as an acceptor, although the amount of product formed is less than 2% of that formed when shikimic acid serves as the acceptor
-
-
?
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
preferred substrate is shikimate
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-(4-coumaroyl)quinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
r
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
Q8GSM7
-
-
r
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
product determination
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
best substrate
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
best substrate
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
shikimate cannot be replaced by quinate
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
hydroxycinnamic acid-shikimate ester biosynthesis
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
enzyme appears to play a critical role in the phenylpropanoid pathway, both upstream and downstream of the 3-hydroxylation step
-
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
Q8GSM7
enzyme appears to play a critical role in the phenylpropanoid pathway, both upstream and downstream of the 3-hydroxylation step
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
biosynthetic pathway of hydroxycinnamic acid glucaric acid
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
E8ZAP2, -
preferred substrate for HST with shikimate as acceptor substrate is 4-coumaroyl-CoA
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
show the reaction diagram
-
recombinant HCT shows substrate-specificity towards shikimic acid in contrast to hydroxycinnamoyl-CoA quinate transferase, HQT, EC 2.3.1.99, preferred substrate is shikimate
-
-
?
caffeoyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
caffeoyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
caffeoyl-CoA + 3-hydroxyanthranilate
CoA + 3-caffeoyloxyanthranilate
show the reaction diagram
E8ZAP2, -
-
-
-
?
caffeoyl-CoA + 3-hydroxybenzoate
CoA + 3-caffeoyloxybenzoate
show the reaction diagram
E8ZAP2, -
-
-
-
?
caffeoyl-CoA + glycerol
CoA + ?
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + L-malate
CoA + 2-O-caffeoyl-L-malate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
-
-
-
?
caffeoyl-CoA + quinate
CoA + caffeoylquinate
show the reaction diagram
C3PTS7, -
-
-
-
r
caffeoyl-CoA + quinate
CoA + caffeoylquinate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
reaction products are detected when quinic acid is used as an acceptor, although the amount of product formed is less than 2% of that formed when shikimic acid serves as the acceptor
-
-
?
caffeoyl-CoA + quinate
CoA + 5-caffeoylquinate
show the reaction diagram
A4ZKE4, -
-
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
-
-
-
-
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
Q8GSM7
-
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
B6D7P1, B6D7P2, B6DQK4
-
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
E8ZAP2, -
-
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
not
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
condensation at 52% the rate of the reaction with p-coumaroyl-CoA
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
-
the activity is 100fold lower than the activity with coumaroyl-CoA
-
-
?
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
show the reaction diagram
A4ZKE4, -
-
-
-
r
cinnamoyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
cinnamoyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
cinnamoyl-CoA + 3-hydroxyanthranilate
CoA + 3-cinnamoyloxyanthranilate
show the reaction diagram
E8ZAP2, -
-
-
-
?
cinnamoyl-CoA + 3-hydroxybenzoate
CoA + 3-cinnamoyloxybenzoate
show the reaction diagram
E8ZAP2, -
-
-
-
?
cinnamoyl-CoA + shikimate
CoA + 5-O-cinnamoylshikimate
show the reaction diagram
-
-
-
-
?
cinnamoyl-CoA + shikimate
CoA + 5-O-cinnamoylshikimate
show the reaction diagram
-
not
-
-
?
cinnamoyl-CoA + shikimate
CoA + 5-O-cinnamoylshikimate
show the reaction diagram
E8ZAP2, -
very low activity
-
-
r
feroyl-CoA + 3-hydroxyanthranilate
CoA + 3-feroyloxyanthranilate
show the reaction diagram
E8ZAP2, -
-
-
-
?
feroyl-CoA + 3-hydroxybenzoate
CoA + 3-feroyloxybenzoate
show the reaction diagram
E8ZAP2, -
-
-
-
?
feroyl-CoA + shikimate
CoA + 5-O-feroylshikimate
show the reaction diagram
E8ZAP2, -
-
-
-
r
feruloyl-CoA + 2,3-dihydroxybenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
feruloyl-CoA + 3-aminobenzoate
CoA + ?
show the reaction diagram
E8ZAP2, -
-
-
-
?
feruloyl-CoA + glycerol
CoA + ?
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
-
-
-
-
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
-
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
Q8GSM7
-
-
-
r
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
not
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
not
-
-
r
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + 3-hydroxyanthranilate
CoA + 3-sinapoyloxyanthranilate
show the reaction diagram
E8ZAP2, -
-
-
-
r
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
not
-
-
?
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
E8ZAP2, -
very low activity
-
-
r
sinapoyl-CoA + shikimate
CoA + 5-O-sinapoylshikimate
show the reaction diagram
-
condensation at 29% the rate of the reaction with p-coumaroyl-CoA
-
-
?
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
-
condensation at 22% the rate of the reaction with p-coumaroyl-CoA
-
-
?
additional information
?
-
-
1-hydroxycinnamoyl glucose esters, gluconolactone, galactonate, glucuronate, ascorbate, malate, m-tartrate
-
-
-
additional information
?
-
-
no substrate: cinnamoyl-CoA, L-malate, D(+)-malate, L(+)-tartrate, m-tartrate, citrate, glucose, UDP-glucose, myo-inositol, tyramine, agmatine
-
-
-
additional information
?
-
Q8GSM7
no substrate: anthranilate, glucose, malate, tyramine, spermidine, spermine, putrescine, agmatine, benzyl alcohol
-
-
-
additional information
?
-
-
no substrates are 1-hydroxycinnamoyl glucose
-
-
-
additional information
?
-
-
the enzyme is involved in the phenylpropanoid pathway and the biosynthesis of curcuminoids and in lignification, the enzyme activity is modulated in plants as a mechanism to control production of specific metabolites, overview
-
-
-
additional information
?
-
-
the enzyme is part of the monolignol pathway, enzymes of this pathway are individually downregulated resulting in compositional changes in lignin and wall-bound hydroxycinnamic acids, modelling, enzyme expression and metabolism, regulation, overview
-
-
-
additional information
?
-
B6D7P1, B6D7P2, B6DQK4
no reaction products are detected when HCT1 and either hydroxycinnamoyl-CoA derivative are incubated with malic acid, Glc, or L-DOPA as acceptor
-
-
-
additional information
?
-
B6D7P1, B6D7P2, B6DQK4
no reaction products are detected when shikimic acid, quinic acid, Glc, or L-DOPA is used as an acceptor
-
-
-
additional information
?
-
-
HCT mediates formation of hydroxycinnamoylquinnate or hydroxycinnamoylshikimate
-
-
-
additional information
?
-
-
no determination of the in vivo substrate
-
-
-
additional information
?
-
A4ZKE4, -
HCT has a preference for shikimic acid over quinic acid, substrate specifities of the HCT key enzyme, overview
-
-
-
additional information
?
-
-
in vitro recombinant PeHCT shows substrate-specificity towards shikimic acid
-
-
-
additional information
?
-
-
OsHCT4 mediates the trans-esterification of glycerol as well as shikimic acid in the presence of hydroxycinnamoyl-CoA in vitro, reaction product structure determination by NMR
-
-
-
additional information
?
-
E8ZAP2, -
substrate specificity of recombinant HST: no activity with quinate and anthranilate, and tyramine, tryptamine, serotonin, dopamine, DOPA, 2-phenethylamine, phenol, as acceptors
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + quinate
CoA + 5-(4-coumaroyl)quinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
E8ZAP2, -
-
-
-
?
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
hydroxycinnamic acid-shikimate ester biosynthesis
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
enzyme appears to play a critical role in the phenylpropanoid pathway, both upstream and downstream of the 3-hydroxylation step
-
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
Q8GSM7
enzyme appears to play a critical role in the phenylpropanoid pathway, both upstream and downstream of the 3-hydroxylation step
-
-
4-coumaroyl-CoA + shikimate
CoA + 5-O-(4-coumaroyl)shikimate
show the reaction diagram
-
biosynthetic pathway of hydroxycinnamic acid glucaric acid
-
-
4-coumaroyl-CoA + shikimate
CoA + 4-coumaroylshikimate
show the reaction diagram
-
recombinant HCT shows substrate-specificity towards shikimic acid in contrast to hydroxycinnamoyl-CoA quinate transferase, HQT, EC 2.3.1.99
-
-
?
caffeoyl-CoA + quinate
CoA + 5-caffeoylquinate
show the reaction diagram
A4ZKE4, -
-
-
-
r
caffeoyl-CoA + shikimate
CoA + 5-caffeoylshikimate
show the reaction diagram
A4ZKE4, -
-
-
-
r
additional information
?
-
-
the enzyme is involved in the phenylpropanoid pathway and the biosynthesis of curcuminoids and in lignification, the enzyme activity is modulated in plants as a mechanism to control production of specific metabolites, overview
-
-
-
additional information
?
-
-
the enzyme is part of the monolignol pathway, enzymes of this pathway are individually downregulated resulting in compositional changes in lignin and wall-bound hydroxycinnamic acids, modelling, enzyme expression and metabolism, regulation, overview
-
-
-
additional information
?
-
-
HCT mediates formation of hydroxycinnamoylquinnate or hydroxycinnamoylshikimate
-
-
-
additional information
?
-
-
no determination of the in vivo substrate
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
sligthly stimulated by 3.0 mM, inhibition at 5 mM
Mg2+
-
slightly stimulated by 0.5 mM, inhibition at 5 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4,4(-diisothiocyano-2,2)-stilbene disulfonic acid
-
-
Diethylpyrocarbonate
-
80% reversion after treatment with hydroxylamine
DTT
-
concentration above 5 mM results in a marked inhibition of activity
p-chloromercuribenzenesulfonic acid
-
-
RNAi
-
HCT silencing is achieved by transformation of Pinus radiata callus cells with pHF5
-
Sodium diphosphate
-
-
Tricine
-
weak, not Tris/HCl
additional information
-
no effect: 2,3-butanedione, phenylmethylsulfonylfluoride and N-methylmaleimide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
activation
Tris/HCl
-
activation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.188
-
2,3-Dihydroxybenzoate
E8ZAP2, -
pH 7.0, 30C, with 4-coumaroyl-CoA
0.699
-
2,3-Dihydroxybenzoate
E8ZAP2, -
pH 7.0, 30C, with caffeoyl-CoA
2.404
-
3-aminobenzoate
E8ZAP2, -
pH 7.0, 30C, with 4-coumaroyl-CoA
0.449
-
3-Hydroxyanthranilate
E8ZAP2, -
pH 7.0, 30C, with caffeoyl-CoA
0.473
-
3-Hydroxyanthranilate
E8ZAP2, -
pH 7.0, 30C, with 4-coumaroyl-CoA
0.733
-
3-Hydroxybenzoate
E8ZAP2, -
pH 7.0, 30C, with caffeoyl-CoA
1.677
-
3-Hydroxybenzoate
E8ZAP2, -
pH 7.0, 30C, with 4-coumaroyl-CoA
1.1
-
3-phenylacryloyl-CoA
-
-
0.0015
-
4-Coumaroyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 3-hydroxybenzoate
0.0031
-
4-Coumaroyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 2,3-dihydroxybenzoate
0.0043
-
4-Coumaroyl-CoA
E8ZAP2, -
pH 7.0, 30C, with shikimate
0.00813
-
4-Coumaroyl-CoA
-
pH 8.0, 37C, recombinant GST-tagged enzyme, with shikimate
0.0086
-
4-Coumaroyl-CoA
-
-
0.00964
-
4-Coumaroyl-CoA
-
pH 8.0, 37C, recombinant GST-tagged enzyme, with quinate
0.0185
-
4-Coumaroyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 3-aminobenzoate
0.022
-
4-Coumaroyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 3-hydroxyanthranilate
0.024
-
4-Coumaroyl-CoA
-
-
0.0601
-
4-Coumaroyl-CoA
-
pH 7.5, 37C, with glycerol
0.5
-
4-Coumaroyl-CoA
-
-
0.6
-
4-Coumaroyl-CoA
Q8GSM7
-
1.2
-
4-Coumaroyl-CoA
-
-
8.13
-
4-Coumaroyl-CoA
-
with shikimate, pH 8.0, 37C
9.64
-
4-Coumaroyl-CoA
-
with quinate, pH 8.0, 37C
14.3
-
4-Coumaroyl-CoA
-
-
0.119
-
4-coumaroylshikimate
-
-
0.0051
-
caffeoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 3-hydroxybenzoate
0.0067
-
caffeoyl-CoA
-
-
0.0088
-
caffeoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with shikimate
0.0118
-
caffeoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 2,3-dihydroxybenzoate
0.045
-
caffeoyl-CoA
-
-
0.05
-
caffeoyl-CoA
Q8GSM7
-
0.0538
-
caffeoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with 3-hydroxyanthranilate
0.102
-
caffeoyl-CoA
-
pH 7.5, 37C, with glycerol
0.41
-
caffeoyl-CoA
-
-
12.5
-
caffeoyl-CoA
-
-
30.5
-
caffeoyl-CoA
-
-
0.0265
-
cinnamoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with shikimate
0.0051
-
Feruloyl-CoA
E8ZAP2, -
pH 7.0, 30C, with shikimate
0.006
-
Feruloyl-CoA
-
-
0.0721
-
Feruloyl-CoA
-
pH 7.5, 37C, with glycerol
0.35
-
Feruloyl-CoA
Q8GSM7
-
1.9
-
Feruloyl-CoA
-
-
15.4
-
Feruloyl-CoA
-
-
55.5
-
Feruloyl-CoA
-
-
0.00582
-
quinate
-
pH 8.0, 37C, recombinant GST-tagged enzyme, with 4-coumaroyl-CoA
0.07
-
quinate
Q8GSM7
-
5.82
-
quinate
-
with 4-coumaroyl-CoA, pH 8.0, 37C
0.0009
-
shikimate
-
pH 8.0, 37C, recombinant GST-tagged enzyme, with 4-coumaroyl-CoA
0.039
-
shikimate
-
-
0.1558
-
shikimate
-
pH 7.5, 37C, with feruloyl-CoA
0.332
-
shikimate
E8ZAP2, -
pH 7.0, 30C, with 4-coumaroyl-CoA
0.59
-
shikimate
-
with 4-coumaroyl-CoA
0.75
-
shikimate
Q8GSM7
-
0.9
-
shikimate
-
with 4-coumaroyl-CoA, pH 8.0, 37C
1
-
shikimate
-
-
2.235
-
shikimate
E8ZAP2, -
pH 7.0, 30C, with cinnamoyl-CoA
4.32
-
shikimate
-
-
5.5
-
shikimate
-
-
6.495
-
shikimate
E8ZAP2, -
pH 7.0, 30C, with caffeoyl-CoA
22.38
-
shikimate
E8ZAP2, -
pH 7.0, 30C, with feroyl-CoA
26.13
-
shikimate
E8ZAP2, -
pH 7.0, 30C, with sinapoyl-CoA
83
-
shikimate
-
with caffeoyl-CoA
0.02
-
Sinapoyl-CoA
E8ZAP2, -
pH 7.0, 30C, with shikimate
0.0859
-
glycerol
-
pH 7.5, 37C, with feruloyl-CoA
additional information
-
additional information
-
kinetics, overview
-
additional information
-
additional information
E8ZAP2, -
kinetics, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0056
-
-
-
additional information
-
-
-
additional information
-
-
change of enzyme activity during a 1-year growth period
additional information
-
-
-
additional information
-
-
-
additional information
-
-
reduction of enzyme activity in down-regulated lines is from at least 15 - 50%
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
50 mM potassium phosphate buffer
6.5
-
-
50 mM potassium phosphate buffer; pI: 4.33
6.8
-
-
50 mM potassium phosphate buffer
7
-
-
50 mM potassium phosphate buffer
7
-
E8ZAP2, -
assay at
7.1
-
-
200 mM potassium phosphate buffer
7.5
-
-
Tris-HCl
7.5
-
-
HCT enzyme activity assay
7.5
-
B6D7P1, B6D7P2, B6DQK4
assay at; assay at; assay at
7.5
-
-
assay at
8
-
-
assay at
additional information
-
-
pI: 4.63
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
about half-maximal activity at pH 5.5 and 7.5
6.1
6.7
B6D7P1, B6D7P2, B6DQK4
optimal pH range with malate as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 6.1 and 6.7 using sodium phosphate buffer
6.2
8.5
-
about half-maximal activity at pH 6.2 in potassium phosphate buffer and 8.5 in Tris-HCl puffer
6.3
7.7
-
about 80% of maximal activity at pH 6.3 and 7.7
7.5
7.9
B6D7P1, B6D7P2, B6DQK4
optimal pH range with shikimic acid as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 7.5 and 7.9 using sodium phosphate buffer; optimal pH range with shikimic acid as the acceptor, highest reaction rates are observed for both hydroxycinnamoyl-CoA derivatives between pH 7.5 and 7.9 using sodium phosphate buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
B6D7P1, B6D7P2, B6DQK4
assay at; assay at; assay at
30
-
E8ZAP2, -
assay at
37
-
-
enzyme extremely stable
37
-
-
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
above 40C rapid and irreversible loss of activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.78
-
E8ZAP2, -
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
C3PTS8
real time PCR experiments demonstrate an increase in the expression level of HQT in UV-C treated leaves
Manually annotated by BRENDA team
C3PTS7
real time PCR experiments demonstrate an increase in the expression level of HQT in UV-C treated leaves
Manually annotated by BRENDA team
B6D7P1, B6D7P2, B6DQK4
expression analyses indicate that HCT1 mRNA accumulates to 4fold higher levels in stems than in leaves; expression analyses indicate that HCT1 mRNA accumulates to 4fold higher levels in stems than in leaves; HCT2 mRNA accumulates to 10fold higher levels in leaves than in stems
Manually annotated by BRENDA team
-
1.5-2.0fold higher enzyme activity compared to leaves and rhizomes
Manually annotated by BRENDA team
-
1.6fold higher enzyme activity compared to leaves and rhizomes
Manually annotated by BRENDA team
B6D7P1, B6D7P2, B6DQK4
expression analyses indicate that HCT1 mRNA accumulates to 4fold higher levels in stems than in leaves; expression analyses indicate that HCT1 mRNA accumulates to 4fold higher levels in stems than in leaves; HCT2 mRNA accumulates to 10fold higher levels in leaves than in stems
Manually annotated by BRENDA team
additional information
-
enzyme activity is much higher in tissues that are actively producing eugenol than in tissues that are not
Manually annotated by BRENDA team
additional information
-
enzyme expression and metabolism, regulation, overview
Manually annotated by BRENDA team
additional information
-
PeHCT displays 1.5fold higher expression in the stem than in the leaf, and its expression increases during the growth stage of the leaf
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
gel filtration
40000
-
-
gel filtration
45000
50000
A4ZKE4, -
recombinant HCT, gel filtration
48000
-
-
gel filtration
48300
-
B6D7P1, B6D7P2, B6DQK4
calculated from cDNA; calculated from cDNA; calculated from cDNA
50000
-
-
gel filtration
50000
-
C3PTS8
calculated from cDNA
50000
-
C3PTS7
calculated from cDNA
58000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 70000, about, recombinant GST-tagged HCT, SDS-PAGE
?
E8ZAP2, -
x * 47100, about, sequence calculation
monomer
A4ZKE4, -
1 * 48000, recombinant enzyme, SDS-PAGE, 1 * 48464, mass spectrometry
additional information
A4ZKE4, -
the enzyme is cleaved into two fragments of 24528 Da and 23906 Da overtime. The protease-cleavage site is localized in the central part of the enzyme, corresponding to a large crossover loop connecting the N- and C-terminal domains in BAHD structures
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified recombinant HCT, sitting drop technique, mixing of 100 nl of 20 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM 2-mercaptoethanol, with 100 nl of precipitant solution containing 1.6 M magnesium sulfate, 0.1 M MES pH 6.5, 20C, 2 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
A4ZKE4, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
A4ZKE4, -
improved stability in sodium phosphate buffer and at higher pH values
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
-
-
denaturation after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol stabilizes during storage
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.1 M phosphate buffer, pH 6.5, 65% of initial activity retained for at least 85 days
-
-20C, for several months, no apparent loss of activity
-
-20C, for several months with 10-20% loss of apparent activities after thawing
-
-80C, for several months with 10-20% loss of apparent activities after thawing
-
incubation for days at room temperature, multiple freeze/thaw cycles, holding at -20C for several months, with or without the addition of 10% glycerol, no loss of activity
-
-20C, with 10% glycerol at least 30 days
-
-20C, at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant N-terminally His6-tagged HCT from Escherichia coli strain BL21 Star(DE3)pLysS by nickel affinity chromatography, dialysis, and cleavage of the tag by TEV protease, followed by gel filtration
A4ZKE4, -
crude extracts from stem material from various down-regulated and control lines are assayed for extractable HCT enzyme activity
-
recombinant enzyme
Q8GSM7
soluble recombinant GST-tagged OsHCT4 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
-
tracheary elements are cultured
-
recombinant GST-tagged HCT from Escherichia coli strain BL21 (DE3) by glutathione affinity chromatography; recombinant GST-tagged PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7 gene products from Escherichia coli strain BL21 (DE3) by glutathione affinity cromatography
-
recombinant His-tagged HST from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis
E8ZAP2, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression of N-terminally His6-tagged HCT in Escherichia coli strain BL21 Star(DE3)pLysS using a commercially available synthetic gene encoding HCT with codons optimized for Escherichia coli expression
A4ZKE4, -
recombinantly expressed in Escherichia coli
C3PTS7
an antisense construct is generated for down-regulation of HCT
-
expression in Escherichia coli
Q8GSM7
gene OsHCT4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression as soluble GST-tagged enzyme using vector pGEX 5X-1 in Escherichia coli strain BL21(DE3)
-
the amplified PCR fragments of the putative HCT cDNA clone are sequenced and cloned into a derivative of pAHC25, the resulting plasmid containing the HCT RNAi construct is named pHF5
-
expression of GST-tagged HCT in Escherichia coli strain BL21 (DE3); genes PeHCT-1, PeHCT-2, PeHCT-3, PeHCT-4, PeHCT-5, PeHCT-6, and PeHCT-7, expression as GST-tagged enzymes in Escherichia coli strain BL21 (DE3)
-
gene cbhct2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His-tagged HST in Escherichia coli strain BL21(DE3)pLysS
E8ZAP2, -
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
B6D7P1, B6D7P2, B6DQK4
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
HCT is evaluated as a target for forage quality improvement
industry
-
the global trend toward a biomaterials-based economy makes plant cell walls increasingly important as renewable resources, HCT is a metabolic entry point leading to the biosynthesis of G-lignin in coniferous gymnosperms