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. 1989 Jun 1;260(2):339–343. doi: 10.1042/bj2600339

Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues.

E N Marsh 1, P F Leadlay 1
PMCID: PMC1138674  PMID: 2569860

Abstract

Adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii contains no intramolecular disulphide bridges, but two of the six thiol groups in the heterodimer are only revealed after reduction of the denatured enzyme with dithiothreitol. The available evidence suggests that they are present in disulphide linkages to unknown thiols of low Mr. The two specifically masked cysteine residues are Cys-535 in the alpha-subunit and Cys-517 in the beta-subunit, which occupy exactly homologous positions in each chain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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