Information on EC 2.4.2.25 - flavone apiosyltransferase

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The expected taxonomic range for this enzyme is: Petroselinum crispum

EC NUMBER
COMMENTARY
2.4.2.25
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RECOMMENDED NAME
GeneOntology No.
flavone apiosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-alpha-D-apiose + apigenin 7-O-beta-D-glucoside = UDP + apigenin 7-O-[beta-D-apiosyl-(1->2)-beta-D-glucoside]
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
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PATHWAY
KEGG Link
MetaCyc Link
apigenin glycosides biosynthesis
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Flavone and flavonol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-apiose:5,4'-dihydroxyflavone 7-O-beta-D-glucoside 2''-O-beta-D-apiofuranosyltransferase
7-O-beta-D-Glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
apiosyltransferase, uridine diphosphoapiose-flavone
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UDPapiose:7-O-(beta-D-glucosyl)-flavone apiosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
37332-49-3
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDPapiose + 7-O-(beta-D-glucosyl)-apigenin
UDP + 7-O-beta-D-apiofuranosyl-1,2-beta-D-glucosyl-apigenin
show the reaction diagram
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specific for UDPapiose as glycosyl donor
i.e. apiin
?
UDPapiose + 7-O-(beta-D-glucosyl)-apigenin
?
show the reaction diagram
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biosynthesis of apiin
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UDPapiose + biochanin A
?
show the reaction diagram
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i.e. 5,7-dihydroxy-4'-methoxyisoflavone-7-glucoside
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?
additional information
?
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overview: 7-O-beta-glucosides of a number of flavonoids and of 4-substituted phenols can act as acceptors, not: flavonol-3-glucoside, flavonol-7-glucoside, apigenin-8-C-glucoside, aglycones of flavonoids, glucose
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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
UDPapiose + 7-O-(beta-D-glucosyl)-apigenin
?
show the reaction diagram
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biosynthesis of apiin
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
apigenin-7-glucoside
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Chrysoeriol-7-glucoside
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iodoacetamide
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at 1 mM causes an inhibition of 55%, reversed by cysteine
p-chloromercuribenzoate
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at 1 mM inhibits the reaction completely
additional information
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no effect: EDTA, NH4+, K+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithioerythritol
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stimulates enzyme activity up to 35%, optimum concentration: 6 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.066
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apigenin-7-glucoside
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
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higher apiin yield in Tris-HCl than in phosphate buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
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gel filtration
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
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highest stability
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
albumin, 0.1 mg, significant stabilization
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solution of enzyme after hydroxylapatite chromatography in sodium phosphate buffer, pH 7.0, rapidly loses activity upon freezing
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STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, Tris-HCl, dithiothreitol, protein concentration 0.5-1 mg/ml
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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified 123fold by protamine sulfate and ammonium sulfate precipitation and chromatography on DEAE-cellulose, SephadexG-100 and hydroxylapatite
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