EC 1.1.1.306 - S-(hydroxymethyl)mycothiol dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.306

Names

Accepted name:
S-(hydroxymethyl)mycothiol dehydrogenase
Other names:
NAD/factor-dependent formaldehyde dehydrogenase
mycothiol-dependent formaldehyde dehydrogenase
Systematic name:
S-(hydroxymethyl)mycothiol:NAD+ oxidoreductase

Reaction

Cofactor

Comments:

S-hydroxymethylmycothiol is believed to form spontaneously from formaldehyde and mycothiol. This enzyme oxidizes the product of this spontaneous reaction to S-formylmycothiol, in a reaction that is analogous to EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00058
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Misset-Smits, M., Van Ophem, P.W., Sakuda, S. and Duine, J.A.
    Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-α-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase.
    FEBS Lett. 409: 221-222 (1997). [PMID: 9202149]
  2. Norin, A., Van Ophem, P.W., Piersma, S.R., Person, B., Duine, J.A. and Jornvall, H.
    Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaryotic alcohol dehydrogenase's - primary structure, conformational modelling and functional correlations.
    Eur. J. Biochem. 248: 282-289 (1997). [PMID: 9346279]
  3. Vogt, R. N., Steenkamp, D. J., Zheng, R., Blanchard, J. S.
    The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase.
    Biochem. J. 374: 657-666 (2003). [PMID: 12809551]
  4. Rawat, M., Av-Gay, Y.
    Mycothiol-dependent proteins in actinomycetes.
    FEMS Microbiol. Rev. 31: 278-292 (2007). [PMID: 17286835]

[EC 1.1.1.306 created 2010 as EC 1.2.1.66, transferred 2010 to EC 1.1.1.306]