Information on EC 1.1.1.348 - vestitone reductase

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The expected taxonomic range for this enzyme is: Medicago sativa

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EC NUMBER
COMMENTARY hide
1.1.1.348
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RECOMMENDED NAME
GeneOntology No.
vestitone reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3R,4R)-4'-methoxyisoflavan-2',4,7-triol + NADP+ = (3R)-vestitone + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glyceollin biosynthesis I
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maackiain biosynthesis
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medicarpin biosynthesis
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Isoflavonoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(3R,4R)-4'-methoxyisoflavan-2',4,7-triol:NADP+ 4-oxidoreductase
This plant enzyme catalyses the penultimate step in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. This activity was previously classified as part of EC 1.1.1.246, pterocarpin synthase, which is now known to be catalysed by two enzymes, vestitone reductase and EC 4.2.1.139, medicarpin synthase.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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vestitone reductase is the penultimate enzyme in medicarpin biosynthesis
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-vestitone + NADPH + H+
(3R,4R)-4'-methoxyisoflavan-2',4,7-triol + NADP+
show the reaction diagram
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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
(3R)-vestitone + NADPH + H+
(3R,4R)-4'-methoxyisoflavan-2',4,7-triol + NADP+
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vestitone
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vestitone reductase is noticeably inhibited by vestitone concentrations in excess of 0.05 mM, the activity being inhibited over 40% at 0.25 mM vestitone
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
(3R)-vestitone
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in 0.2 M sodium phosphate buffer, pH 6.0, at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25
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crude extract, in 0.2 M sodium phosphate buffer, pH 6.0, at 30°C
461.1
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after 1844fold purification, in 0.2 M sodium phosphate buffer, pH 6.0, at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the highest levels of transcript is in the root
Manually annotated by BRENDA team
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relatively high transcript levels are found in the nodule samples
Manually annotated by BRENDA team
additional information
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not detected in stem, petiole and leaf
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 35918, calculated from amino acid sequence; x * 38000, SDS-PAGE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Tris-HCl (pH 8.0), 20% (w/v) polyethylene glycol 6000, 0.1 M MgCl2, at 4°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-NTA agarose column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
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PEG fractionation, Red-agarose column chromatography, MonoQ column chromatography, and DEAE-Sephacel gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli DH5alpha cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activity of vestitone reductase increases approximately 3fold 6 h after treatment with an elicitor preparation derived from yeast in alfalfa suspension cell culture. The activity remains at maximal level for 40 h
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the levels of vestitone reductase transcript greatly increase within 2 h of elicitor addition to alfalfa cell suspension cultures
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y164A
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the mutation abolishes enzymatic activity
Y164G
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the mutation abolishes enzymatic activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.348)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)