Information on EC 2.3.1.99 - quinate O-hydroxycinnamoyltransferase

Word Map on EC 2.3.1.99
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.99
-
RECOMMENDED NAME
GeneOntology No.
quinate O-hydroxycinnamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + quinate = CoA + O-feruloylquinate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylpropanoid biosynthesis
-
-
Stilbenoid, diarylheptanoid and gingerol biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
60321-02-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
loquat
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
apple, cv. Golden Delicious
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
rye, var. Kustro
-
-
Manually annotated by BRENDA team
potato, var. Homeguard
-
-
Manually annotated by BRENDA team
syn. Solenostemon scutellarioides
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + quinate
CoA + 5-O-(4-coumaroyl)quinate
show the reaction diagram
caffeoyl-CoA + quinate
CoA + 3-O-caffeoylquinate
show the reaction diagram
-
i.e. chlorogenate
-
?
caffeoyl-CoA + quinate
CoA + 5-O-caffeoylquinate
show the reaction diagram
caffeoyl-CoA + quinate
CoA + chlorogenic acid
show the reaction diagram
caffeoyl-CoA + shikimate
CoA + 5-O-caffeoylshikimate
show the reaction diagram
feruloyl-CoA + quinate
CoA + O-feruloylquinate
show the reaction diagram
feruloyl-CoA + shikimate
CoA + 5-O-feruloylshikimate
show the reaction diagram
feruloyl-CoA shows 10fold lower activity than caffeoyl-CoA with shikimate as substrate
-
-
?
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
show the reaction diagram
p-coumaroyl-CoA + shikimate
CoA + 5-O-(p-coumaroyl)shikimate
show the reaction diagram
sinapoyl-CoA + quinate
CoA + 5-O-sinapoylquinate
show the reaction diagram
-
at 21% the rate of the reaction with feruloyl-CoA
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + quinate
CoA + 4-coumaroylquinate
show the reaction diagram
-
-
-
-
?
caffeoyl-CoA + quinate
CoA + 3-O-caffeoylquinate
show the reaction diagram
D1L8A9
-
-
-
?
caffeoyl-CoA + quinate
CoA + chlorogenic acid
show the reaction diagram
p-coumaroyl-CoA + quinate
CoA + 5-O-(p-coumaroyl)quinate
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,4(diisothiocyano-2,2)-stilbene disulfonic acid
-
-
Ca2+
-
inhibition at 5 mM
caffeic acid
-
-
Cinnamic acid
-
-
coumaric acid
-
-
Diethylpyrocarbonate
-
reversion after treatment with hydroxylamine
DTT
-
concentration above 5 mM results in a marked inhibition of activity
ferulic acid
-
-
hydroxylamine
-
-
Mg2+
-
inhibition at 5 mM
N-[2-Acetamido]-2-iminodiacetic acid
-
i.e. N-[carbamoylmethyl]iminodiacetic acid or ADA
p-chloromercuribenzenesulfonic acid
-
-
quinic acid
-
-
Sodium diphosphate
-
-
tricine
-
-
Tris/HCl
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 14.3
caffeoyl-CoA
0.06 - 0.151
chlorogenic acid
0.021 - 0.084
CoA
0.003 - 10
coumaroyl-CoA
0.092
coumaroylquinate
-
-
0.009 - 11.4
Feruloyl-CoA
0.15 - 0.6
p-Coumaroyl-CoA
0.43 - 4.3
quinate
0.75 - 11.82
shikimate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82
caffeic acid
-
-
0.94
Cinnamic acid
-
-
0.7
coumaric acid
-
-
1.17
ferulic acid
-
-
1.1
quinic acid
-
-
0.074
Zn2+
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0042
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.9
-
about half-maximal activity at pH 5.6 and 7.9
6.9 - 8
-
about 80% of maximal activity at pH 6.9 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 6.2
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high enzyme content
Manually annotated by BRENDA team
-
low level of expression
Manually annotated by BRENDA team
-
low level of expression
Manually annotated by BRENDA team
additional information
-
expression in leaves is below the detection level of the immunological method, only faint level in flowers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme catalyzes different reactions in different compartments
Manually annotated by BRENDA team
enzyme catalyzes different reactions in different compartments
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14900
-
3 * 14900, SDS-PAGE
41500
-
gel filtration
48000
x * 48000, about, sequence calculation
50000
x * 50000, recombinant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
-
3 * 14900, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
65% loss of activity after 5 min, phosphate buffer protects: 12% loss after 5 min
80
-
denaturation after 5 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 33% loss of activity after 10 months
-
-20C, at least 2 months
-
-20C, at least 6 months
-
-20C, for several months, no apparent loss of activity
-
-20C, with 10% glycerol at least 30 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
recombinant His-tagged HQT from Escherichia coli by nickel affinity chromatography
recombinant protein fused to glutathione-S-transferase
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
expression in Escherichia coli as fusion protein with 15 amino acid S-TAG
expression in Escherichia coli as fusion protein with 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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in the expression level of HQT in UV-C treated leaves
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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