KEGG   ENZYME: 1.1.1.328Help
Entry
EC 1.1.1.328                Enzyme                                 

Name
nicotine blue oxidoreductase;
nboR (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
3,3'-bipyridine-2,2',5,5',6,6'-hexol:NADP+ 11-oxidoreductase
Reaction(IUBMB)
3,3'-bipyridine-2,2',5,5',6,6'-hexol + NAD(P)+ = (E)-2,2',5,5'-tetrahydroxy-6H,6'H-[3,3'-bipyridinylidene]-6,6'-dione + NAD(P)H + H+ [RN:R10131 R10132]
Reaction(KEGG)
Substrate
3,3'-bipyridine-2,2',5,5',6,6'-hexol [CPD:C20381];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
(E)-2,2',5,5'-tetrahydroxy-6H,6'H-[3,3'-bipyridinylidene]-6,6'-dione [CPD:C16152];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme, characterized from the nicotine degrading bacterium Arthrobacter nicotinovorans, catalyses the reduction of "nicotine blue" to its hydroquinone form (the opposite direction from that shown). Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. The main role of the enzyme may be to prevent the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. The enzyme possesses a slight preference for NADH over NADPH.
History
EC 1.1.1.328 created 2012
Pathway
Nicotinate and nicotinamide metabolism
Microbial metabolism in diverse environments
Orthology
K19190  
nicotine blue oxidoreductase
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 » show all
Taxonomy
Reference
1  [PMID:17293530]
  Authors
Mihasan M, Chiribau CB, Friedrich T, Artenie V, Brandsch R
  Title
An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism.
  Journal
Appl. Environ. Microbiol. 73 (2007) 2479-85.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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