Literature DB >> 32234

Role of vitamin B12 and enzymes related to methylmalonyl-CoA mutase in a methanol-utilizing bacterium, Protaminobacter ruber.

S Ueda, K Sato, S Shimizu.   

Abstract

A methanol-utilizing bacterium, Protaminobacter ruber, required cobalt ion or vitamin B12 as its growth factor, which could be replaced by succinate among various additions to the cobalt-deficient medium. The presence of adenosylcobalamin (adenosyl-B12)-dependent methylmalonyl-coenzyme A (CoA) mutase was demonstrated in the cell-free extracts of P. ruber. The specific activity of this mutase was not only fairly high in comparison with that reported with other organisms but also detected at a similar level throughout the cultivation period. The cell-free extracts of P. ruber grown on non-C1 compounds as a sole carbon and energy source also had methylmalonyl-CoA mutase activity. Furthermore, the extracts of this microorganism catalyzed the reactions from propionyl-CoA to succinyl-CoA and from alpha-ketoglutarate to alpha-hydroxyglutarate.

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Year:  1978        PMID: 32234     DOI: 10.3177/jnsv.24.477

Source DB:  PubMed          Journal:  J Nutr Sci Vitaminol (Tokyo)        ISSN: 0301-4800            Impact factor:   2.000


  1 in total

1.  Primary structure and activity of mouse methylmalonyl-CoA mutase.

Authors:  M F Wilkemeyer; A M Crane; F D Ledley
Journal:  Biochem J       Date:  1990-10-15       Impact factor: 3.857

  1 in total

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