Literature DB >> 3134526

Occurrence and characterization of cyanocobalamin reductase (NADPH; CN-eliminating) involved in decyanation of cyanocobalamin in Euglena gracilis.

F Watanabe1, Y Oki, Y Nakano, S Kitaoka.   

Abstract

The activity of an enzyme involved in decyanation of cyanocobalamin was found in the cell homogenate of Euglena gracilis. The enzyme essentially required FAD or FMN, and NADPH as cofactors. The apparent Km for cyanocobalamin and NADPH were 7.1 microM and 0.2 mM, respectively. The enzyme reaction obeyed allosteric kinetics towards FAD ([FAD]0.5 = 30 microM, n = 2.7; as calculated by the Hill plots). The Euglena enzyme was located in the mitochondria.

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Year:  1988        PMID: 3134526     DOI: 10.3177/jnsv.34.1

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


  1 in total

1.  Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment.

Authors:  Shouqiang Cheng; Thomas A Bobik
Journal:  J Bacteriol       Date:  2010-07-23       Impact factor: 3.490

  1 in total

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