Information on EC 2.3.1.98 - chlorogenate-glucarate O-hydroxycinnamoyltransferase

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The expected taxonomic range for this enzyme is: Solanum lycopersicum

EC NUMBER
COMMENTARY hide
2.3.1.98
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RECOMMENDED NAME
GeneOntology No.
chlorogenate-glucarate O-hydroxycinnamoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
caffeoylglucarate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
chlorogenate:glucarate O-(hydroxycinnamoyl)transferase
Galactarate can act as acceptor, more slowly. Involved with EC 2.3.1.99 quinate O-hydroxycinnamoyltransferase in the formation of caffeoylglucarate in tomato.
CAS REGISTRY NUMBER
COMMENTARY hide
126124-92-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the sequence determines SlCGT as a GDSL lipase-like protein, representing it as a member of the SGNH protein superfamily. Lipases of this family employ a catalytic triad of Ser-Asp-His with Ser as nucleophile of the GDSL motif. The catalytic triad of the GDSL lipase is not essential for SlCGT enzymatic activity. SlCGT is therefore an example of a GDSL lipase-like protein that has lost hydrolytic activity and has acquired a completely new function in plant metabolism, functioning in secondary metabolism as acyltransferase in synthesis of hydroxycinnamate esters by employing amino acid residues different from the lipase catalytic triad
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-O-caffeoylquinic acid + galactaric acid
quinate + caffeoylgalactaric acid
show the reaction diagram
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-
?
5-O-caffeoylquinic acid + glucaric acid
quinate + caffeoylglucaric acid
show the reaction diagram
chlorogenate + glucarate
quinate + 2-O-caffeoylglucarate
show the reaction diagram
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
5-O-caffeoylquinic acid + galactaric acid
quinate + caffeoylgalactaric acid
show the reaction diagram
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?
5-O-caffeoylquinic acid + glucaric acid
quinate + caffeoylglucaric acid
show the reaction diagram
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?
chlorogenate + glucarate
quinate + 2-O-caffeoylglucarate
show the reaction diagram
E7AIM3
the enzyme catalyzes the formation of caffeoylglucarate and caffeoylgalactarate using chlorogenate, i.e. 5-O-caffeoylquinate, as acyl donor
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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150% of activity compared to the activity without addition of divalent ions
Mg2+
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125% of activity compared to the activity without addition of divalent ions
additional information
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EDTA has no effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PMSF
treatment of purified SlCGT with 1, 10, and 50 mM PMSF leads to strong decreases in caffeoyl transfer activities to 60%, 40%, and 0% activity, respectively
additional information
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p-chloromercuribenzoate is no inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
chlorogenic acid
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1.7
galactaric acid
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0.4
glucaric acid
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.45
purified native enzyme, pH 6.0, 30°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 6.2
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50% of maximal activity at pH 4.2 and pH 6.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.01
sequence calculation, mature CGT without signal sequence
5.25
sequence calculation, CGT with signal sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
at different stages of ripening
Manually annotated by BRENDA team
apoplastic space of tomato leaves
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
apoplastic space of tomato leaves
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39950
x * 40000, about, SDS-PAGE, x * 39950, mature CGT without signal sequence, sequence calculation, x * 42580, CGT with signal sequence, sequence calculation
42580
x * 40000, about, SDS-PAGE, x * 39950, mature CGT without signal sequence, sequence calculation, x * 42580, CGT with signal sequence, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, about, SDS-PAGE, x * 39950, mature CGT without signal sequence, sequence calculation, x * 42580, CGT with signal sequence, sequence calculation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing causes 20-30% loss of activity
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purification has to be carried out at 4°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months, no apparent loss of activity with crude extract or purified enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native SlCGT 585fold from seedlings by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, ultrafiltration, gel filtration, and again anion exchange chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene SlCGT, functional expression in Nicotiana benthamiana leaves using Agrobacterium tumefaciens strain GV2260 transfection method
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D328A
site-directed mutagenesis, the mutant shows 40% reduced activity
S27A
site-directed mutagenesis, the mutant shows 13% reduced activity