Literature DB >> 418814

A bacterial phenylalanine aminotransferase lacking pyridoxal 5'-phosphate as cofactor.

G W Jack, P C McMahon.   

Abstract

A bacterium has been isolated from soil which metabolises phenylalanine initially through the action of a phenylalanine aminotransferase. This enzyme has been purified by conventional techniques and affinity chromatography and shown to be unusual among aminotransferases in not containing pyridoxal 5'-phosphate as cofactor.

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Year:  1978        PMID： 418814     DOI： 10.1016/0005-2744(78)90037-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

1.  Characterization of amino acid aminotransferases of Methanococcus aeolicus.

Authors:  R Y Xing; W B Whitman
Journal:  J Bacteriol       Date:  1992-01       Impact factor: 3.490

2.  Conversion of l- and d-Phenylalanine to Phenylacetate via Phenylpyruvate in Sorghum Leaf Extracts.

Authors:  H A Stafford; L L Lewis
Journal:  Plant Physiol       Date:  1979-08       Impact factor: 8.340

3.  The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes.

Authors:  I G Fotheringham; S A Dacey; P P Taylor; T J Smith; M G Hunter; M E Finlay; S B Primrose; D M Parker; R M Edwards
Journal:  Biochem J       Date:  1986-03-15       Impact factor: 3.857
  3 in total

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