KEGG   ENZYME: 1.1.1.394Help
Entry
EC 1.1.1.394                Enzyme                                 

Name
aurachin B dehydrogenase;
AuaH
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
aurachin B:NAD+ 3-oxidoreductase
Reaction(IUBMB)
aurachin B + NAD+ + H2O = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ (overall reaction) [RN:R11149];
(1a) 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide + NAD+ = 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide + NADH + H+ [RN:R11147];
(1b) aurachin B + H2O = 4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide (spontaneous) [RN:R11148]
Reaction(KEGG)
Substrate
aurachin B [CPD:C21140];
NAD+ [CPD:C00003];
H2O [CPD:C00001];
4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide
Product
4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline 1-oxide;
NADH [CPD:C00004];
H+ [CPD:C00080];
4-[(2E,6E)-farnesyl]-3,4-dihydroxy-2-methyl-3,4-dihydroquinoline 1-oxide (spontaneous)
Comment
The enzyme from the bacterium Stigmatella aurantiaca catalyses the final step in the conversion of aurachin C to aurachin B. In vivo the enzyme catalyses the reduction of 4-[(2E,6E)-farnesyl]-4-hydroxy-2-methyl-3-oxo-3,4-dihydroquinoline-1-oxide to form 4-[(2E,6E)-farnesyl]-2-methyl-1-oxo-3,4-dihydroquinoline-3,4-diol (note that the reactions written above proceed from right to left), which then undergoes a spontaneous dehydration to form aurachin B.
History
EC 1.1.1.394 created 2016
Pathway
ec00998  Biosynthesis of secondary metabolites - other antibiotics
ec01100  Metabolic pathways
Orthology
K21271  aurachin B dehydrogenase
Genes
MXA: MXAN_5850
MFU: LILAB_17010
MSD: MYSTI_06459
MYM: A176_001055
CCX: COCOR_06367(ybjS)
SUR: STAUR_6523
AGE: AA314_08678
Taxonomy
Reference
1  [PMID:22907798]
  Authors
Katsuyama Y, Harmrolfs K, Pistorius D, Li Y, Muller R
  Title
A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase.
  Journal
Angew Chem Int Ed Engl 51:9437-40 (2012)
DOI:10.1002/anie.201204138
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.394
IUBMB Enzyme Nomenclature: 1.1.1.394
ExPASy - ENZYME nomenclature database: 1.1.1.394
BRENDA, the Enzyme Database: 1.1.1.394

DBGET integrated database retrieval system