Literature DB >> 12153329

Room-temperature synthesis of L-alanine using the alanine dehydrogenase of the hyperthermophilic archaeon Archaeoglobus fulgidus.

Alexander J H Vadas1, Imke Schröder, Harold G Monbouquette.   

Abstract

Alanine dehydrogenase from the hyperthermophilic archaeon Archaeoglobus fulgidus was used at room temperature for batch synthesis of L-alanine by the reductive amination of pyruvate. The reaction mixture included yeast formate dehydrogenase for regeneration of NADH with formate as electron donor. The synthesis of L-alanine at room temperature was accompanied by no detectable loss of alanine dehydrogenase activity over 139 h and > or =99% consumption of pyruvate. The total number of enzyme turnovers was 5.1 million. This work demonstrates the potential utility of novel hyperthermostable enzymes that can be both very active and highly stable at moderate temperature.

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Year:  2002        PMID: 12153329     DOI: 10.1021/bp025528h

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  1 in total

1.  A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin.

Authors:  Imke Schröder; Alexander Vadas; Eric Johnson; Sierin Lim; Harold G Monbouquette
Journal:  J Bacteriol       Date:  2004-11       Impact factor: 3.490

  1 in total

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