KEGG   ENZYME: 1.5.99.14Help
Entry
EC 1.5.99.14                Enzyme                                 

Name
6-hydroxypseudooxynicotine dehydrogenase
Class
Oxidoreductases;
Acting on the CH-NH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one:acceptor 6-oxidoreductase (hydroxylating)
Reaction(IUBMB)
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H2O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor [RN:R07514]
Reaction(KEGG)
Substrate
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one [CPD:C01297];
acceptor [CPD:C00028];
H2O [CPD:C00001]
Product
1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one [CPD:C15986];
reduced acceptor [CPD:C00030]
Comment
Contains a cytidylyl molybdenum cofactor [3]. The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans [1,2].
History
EC 1.5.99.14 created 2012
Pathway
Nicotinate and nicotinamide metabolism
Microbial metabolism in diverse environments
Orthology
K19185  
6-hydroxypseudooxynicotine dehydrogenase subunit alpha
K19186  
6-hydroxypseudooxynicotine dehydrogenase subunit beta
K19187  
6-hydroxypseudooxynicotine dehydrogenase subunit gamma
Genes
ROP: 
ROP_27460(kdhL) ROP_27510(kdhM) ROP_27520(kdhB)
ROA: 
Taxonomy
Reference
1
  Authors
Freudenberg, W., Konig, K. and Andreesen, J. R.
  Title
Nicotine dehydrogenase from Arthrobacter oxidans: A molybdenum-containing hydroxylase.
  Journal
FEMS Microbiology Letters 52 (1988) 13-18.
Reference
2  [PMID:7815950]
  Authors
Grether-Beck S, Igloi GL, Pust S, Schilz E, Decker K, Brandsch R
  Title
Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans.
  Journal
Mol. Microbiol. 13 (1994) 929-36.
Reference
3  [PMID:16820521]
  Authors
Sachelaru P, Schiltz E, Brandsch R
  Title
A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans.
  Journal
Appl. Environ. Microbiol. 72 (2006) 5126-31.
  Sequence
[up:Q933N0]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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