Information on EC 1.1.1.352 - 5'-hydroxyaverantin dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.352
-
RECOMMENDED NAME
GeneOntology No.
5'-hydroxyaverantin dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(1'S,5'R)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+
show the reaction diagram
(2)
-
-
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(1'S,5'S)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+
show the reaction diagram
(1)
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-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(1'S,5'S)-averufin biosynthesis
-
-
Aflatoxin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(1'S,5'S)-hydroxyaverantin:NAD+ oxidoreductase
Isolated from the aflatoxin-producing mold Aspergillus parasiticus [2]. Involved in aflatoxin biosynthesis. 5'-Oxoaverantin will spontaneously form averufin by intramolecular ketalisation. cf. EC 4.2.1.142, 5'-oxoaverantin cyclase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1'S,5'S)-hydroxyaverantin + NAD+
5'-oxoaverantin + NADH + H+
show the reaction diagram
5'-hydroxyaverantin + NAD(P)+
5'-oxoaverantin + NAD(P)H + H+
show the reaction diagram
5'-hydroxyaverantin + NAD+
5'-oxoaverantin + NADH + H+
show the reaction diagram
5'-hydroxyaverantin + NADP+
5'-oxoaverantin + NADPH + H+
show the reaction diagram
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
5'-hydroxyaverantin + NAD+
5'-oxoaverantin + NADH + H+
show the reaction diagram
5'-hydroxyaverantin + NADP+
5'-oxoaverantin + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
-
no activity with NAD+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,6-dihydroxy-5-methoxy-6a-methylcyclohexa[de]indano-[7,6-e]cyclopenta[c]2H-pyran-1,9-dione
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TAEMC161, specific inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0426 - 0.083
5'-hydroxyaverantin
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
4,6-dihydroxy-5-methoxy-6a-methylcyclohexa[de]indano-[7,6-e]cyclopenta[c]2H-pyran-1,9-dione
Aspergillus parasiticus
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in 50 mM Tris-HCl buffer (pH 8.5), at 33°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000032
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crude enzyme, in 60 mM potassium phosphate buffer (pH 7.5), at 30°C
0.00613
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cell extract, at pH 7.5 and 37°C
0.0222
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after 694fold purification, in 60 mM potassium phosphate buffer (pH 7.5), at 30°C
0.552
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after 90fold purification, at pH 7.5 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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no activity is detected above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25873
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3 * 25873, calculated from amino acid sequence
25918
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3 * 25918 MALDI TOF mass spectrometry
28000
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2 * 28000, SDS-PAGE
29600
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2 * 29600, calculated from amino acid sequence
33000
-
3 * 33000, SDS-PAGE
60000
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gel filtration
100000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotrimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, butyl-Toyopearl 650 M column chromatography
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ammonium sulfate precipitation, DE 52 column chromatography, butyl Toyopearl column chromatography, hydroxyapatite column chromatography, Mono Q column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration
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DEAE Sepharose CL-6B column chromatography, phenyl Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE