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Information on EC 1.1.1.353 - versiconal hemiacetal acetate reductase and Organism(s) Aspergillus parasiticus and UniProt Accession B9WYE6

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IUBMB Comments
Isolated from the mold Aspergillus parasiticus. Involved in a metabolic grid that leads to aflatoxin biosynthesis.
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This record set is specific for:
Aspergillus parasiticus
UNIPROT: B9WYE6
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The taxonomic range for the selected organisms is: Aspergillus parasiticus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
vha reductase, vha reductase i, vha reductase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
VHA reductase
-
-
-
-
VHA reductase I
VHA reductase II
vrdA
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
versiconol-acetate:NADP+ oxidoreductase
Isolated from the mold Aspergillus parasiticus. Involved in a metabolic grid that leads to aflatoxin biosynthesis.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1'-hydroxyversicolorone + NADPH + H+
versicolorone + NADP+
show the reaction diagram
-
-
-
r
versiconal + NADPH + H+
versiconol + NADP+
show the reaction diagram
-
-
-
r
versiconal hemiacetal acetate + NADPH + H+
versiconol acetate + NADP+
show the reaction diagram
-
-
-
r
1'-hydroxyversicolorone + NADPH + H+
versicolorone + NADP+
show the reaction diagram
-
-
-
-
r
versiconal + NADPH + H+
versiconol + NADP+
show the reaction diagram
-
-
-
-
r
versiconal hemiacetal acetate + NADPH + H+
versiconol acetate + NADP+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
versiconal + NADPH + H+
versiconol + NADP+
show the reaction diagram
-
-
-
-
r
versiconal hemiacetal acetate + NADPH + H+
versiconol acetate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0254 - 0.0354
versiconal hemiacetal acetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00362
-
crude extract, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C
0.027
-
isoform VHA reductase II, after 7.5fold purification, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C
0.052
-
isoform VHA reductase I, after 14.4fold purification, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
isoform VHA reductase I
9
-
isoform VHA reductase II
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
no activity is detected below pH 4.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
isoform VHA reductase II, isoelectric focusing
6.6
-
isoform VHA reductase I, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the vrdA is not an aflatoxin biosynthesis gene, although it actually participates in aflatoxin biosynthesis in cells because of its group substrate specificity to intermediates in aflatoxin biosynthesis
metabolism
-
the enzyme is specifically involved in aflatoxin biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VRDA_ASPPA
343
0
38698
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38566
x * 38566, calculated from amino acid sequence
39000
-
10 * 39000, isoform VHA reductase I, SDS-PAGE
390000
-
gel filtration
40000
-
10 * 40000, isoform VHA reductase II, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38566, calculated from amino acid sequence
homodecamer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, phenyl Sepharose column chromatography, DEAE-Sepharose column chromatography, Sephacryl S-300 gel filtration, hydroxylapatite column chromatography, and Matrex gel Green A chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsushima, K.; Ando, Y.; Hamasaki, T.; Yabe, K.
Purification and characterization of two versiconal hemiacetal acetate reductases involved in aflatoxin biosynthesis
Appl. Environ. Microbiol.
60
2561-2567
1994
Aspergillus parasiticus, Aspergillus parasiticus NUIH-26
Manually annotated by BRENDA team
Yabe, K.; Chihaya, N.; Hamamatsu, S.; Sakuno, E.; Hamasaki, T.; Nakajima, H.; Bennett, J.W.
Enzymatic conversion of averufin to hydroxyversicolorone and elucidation of a novel metabolic grid involved in aflatoxin biosynthesis
Appl. Environ. Microbiol.
69
66-73
2003
Aspergillus parasiticus, Aspergillus parasiticus NIAH-26
Manually annotated by BRENDA team
Shima, Y.; Shiina, M.; Shinozawa, T.; Ito, Y.; Nakajima, H.; Adachi, Y.; Yabe, K.
Participation in aflatoxin biosynthesis by a reductase enzyme encoded by vrdA gene outside the aflatoxin gene cluster
Fungal Genet. Biol.
46
221-231
2009
Aspergillus parasiticus (B9WYE6)
Manually annotated by BRENDA team