KEGG   ENZYME: 1.1.1.352Help
Entry
EC 1.1.1.352                Enzyme                                 

Name
5'-hydroxyaverantin dehydrogenase;
HAVN dehydrogenase;
adhA (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
(1'S,5'S)-hydroxyaverantin:NAD+ oxidoreductase
Reaction(IUBMB)
(1) (1'S,5'S)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+ [RN:R10310];
(2) (1'S,5'R)-hydroxyaverantin + NAD+ = 5'-oxoaverantin + NADH + H+ [RN:R10311]
Reaction(KEGG)
Substrate
(1'S,5'S)-hydroxyaverantin [CPD:C20500];
NAD+ [CPD:C00003];
(1'S,5'R)-hydroxyaverantin [CPD:C20501]
Product
5'-oxoaverantin [CPD:C20502];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
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.
History
EC 1.1.1.352 created 2013
Pathway
Aflatoxin biosynthesis
Orthology
K17652  
5'-hydroxyaverantin dehydrogenase
Genes
PAN: 
ANI: 
AOR: 
AOR_1_34014(AO090026000016)
AFV: 
Taxonomy
Reference
1  [PMID:11055914]
  Authors
Chang PK, Yu J, Ehrlich KC, Boue SM, Montalbano BG, Bhatnagar D, Cleveland TE
  Title
adhA in Aspergillus parasiticus is involved in conversion of 5'-hydroxyaverantin  to averufin.
  Journal
Appl. Environ. Microbiol. 66 (2000) 4715-9.
  Sequence
Reference
2  [PMID:14602595]
  Authors
Sakuno E, Yabe K, Nakajima H
  Title
Involvement of two cytosolic enzymes and a novel intermediate, 5'-oxoaverantin, in the pathway from 5'-hydroxyaverantin to averufin in aflatoxin biosynthesis.
  Journal
Appl. Environ. Microbiol. 69 (2003) 6418-26.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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