EC 6.2.1.44 - 3-(methylthio)propionyl—CoA ligase

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IntEnz Enzyme Nomenclature
EC 6.2.1.44

Names

Accepted name:
3-(methylthio)propionyl—CoA ligase
Other names:
DmdB
MMPA-CoA ligase
methylmercaptopropionate-coenzyme A ligase
3-methylmercaptopropionyl-CoA ligase
Systematic name:
3-(methylsulfanyl)propanoate:CoA ligase (AMP-forming)

Reaction

Cofactor

Comments:

The enzyme is part of a dimethylsulfoniopropanoate demethylation pathway in the marine bacteria Ruegeria pomeroyi and Pelagibacter ubique. It also occurs in some nonmarine bacteria capable of metabolizing dimethylsulfoniopropionate (e.g. Burkholderia thailandensis, Pseudomonas aeruginosa, and Silicibacter lacuscaerulensis). It requires Mg2+ [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Reisch, C. R., Stoudemayer, M. J., Varaljay, V. A., Amster, I. J., Moran, M. A., Whitman, W. B.
    Novel pathway for assimilation of dimethylsulphoniopropionate widespread in marine bacteria.
    Nature 473 : 208-211 (2011). [PMID: 21562561]
  2. Bullock, H. A., Reisch, C. R., Burns, A. S., Moran, M. A., Whitman, W. B.
    Regulatory and functional diversity of methylmercaptopropionate coenzyme A ligases from the dimethylsulfoniopropionate demethylation pathway in Ruegeria pomeroyi DSS-3 and other proteobacteria.
    J. Bacteriol. 196 : 1275-1285 (2014). [PMID: 24443527]

[EC 6.2.1.44 created 2014]