KEGG   ENZYME: 1.14.13.111Help
Entry
EC 1.14.13.111              Enzyme                                 

Name
methanesulfonate monooxygenase (NADH);
mesylate monooxygenase;
mesylate,reduced-FMN:oxygen oxidoreductase;
MsmABC;
methanesulfonic acid monooxygenase;
MSA monooxygenase;
MSAMO
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
methanesulfonate,NADH:oxygen oxidoreductase
Reaction(IUBMB)
methanesulfonate + NADH + H+ + O2 = formaldehyde + NAD+ + sulfite + H2O [RN:R09513]
Reaction(KEGG)
Substrate
methanesulfonate [CPD:C11145];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
formaldehyde [CPD:C00067];
NAD+ [CPD:C00003];
sulfite [CPD:C00094];
H2O [CPD:C00001]
Comment
A flavoprotein. Methanesulfonate is the simplest of the sulfonates and is a substrate for the growth of certain methylotrophic microorganisms. Compared with EC 1.14.14.5, alkanesulfonate monooxygenase, this enzyme has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methanesulfonate to butanesulfonate) and excludes all larger molecules, such as arylsulfonates [1]. The enzyme from the bacterium Methylosulfonomonas methylovora is a multicomponent system comprising a hydroxylase, a reductase (MsmD) and a ferredoxin (MsmC). The hydroxylase has both large (MsmA) and small (MsmB) subunits, with each large subunit containing a Rieske-type [2Fe-2S] cluster. cf. EC 1.14.14.34, methanesulfonate monooxygenase (FMNH2).
History
EC 1.14.13.111 created 2009 as EC 1.14.14.6, transferred 2010 to EC 1.14.13.111, modified 2016
Pathway
Sulfur metabolism
Orthology
K16968  
methanesulfonate monooxygenase subunit alpha
K16969  
methanesulfonate monooxygenase subunit beta
Genes
BCT: 
BUE: 
PPK: 
PPNO: 
PRB: 
BPA: 
BBR: 
BBM: 
BBH: 
BBX: 
PUT: 
MPT: 
Mpe_A0919(msmS2) Mpe_A0920(msmB)
MNO: 
FIL: 
FIY: 
APB: 
 » show all
Taxonomy
Reference
1  [PMID:10094704]
  Authors
de Marco P, Moradas-Ferreira P, Higgins TP, McDonald I, Kenna EM, Murrell JC
  Title
Molecular analysis of a novel methanesulfonic acid monooxygenase from the methylotroph Methylosulfonomonas methylovora.
  Journal
J. Bacteriol. 181 (1999) 2244-51.
  Sequence
Reference
2  [PMID:8932698]
  Authors
Higgins TP, Davey M, Trickett J, Kelly DP, Murrell JC
  Title
Metabolism of methanesulfonic acid involves a multicomponent monooxygenase enzyme.
  Journal
Microbiology. 142 ( Pt 2) (1996) 251-60.
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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