Literature DB >> 352693

The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli.

J T Powell, J F Morrison.   

Abstract

A simple and convenient procedure is described for the isolation in good yield of two amino-transferases from various strains of Escherichia coli. On the basis of their substrate specificities one of the enzymes has been classified as an aromatic amino acid aminotransferase and the other as an aspartate aminotransferase, but both act on a wide range of substrates. Pyridoxal phosphate is bound more strongly to the aspartate aminotransferase than to the aromatic amino transferase which cannot be fully re-activated after removal of the prosthetic group. Both enzymes are composed of two subunits which appear to be identical.

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Year:  1978        PMID： 352693     DOI： 10.1111/j.1432-1033.1978.tb12388.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  22 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.  An aminotransferase from Lactococcus lactis initiates conversion of amino acids to cheese flavor compounds.

Authors:  M Yvon; S Thirouin; L Rijnen; D Fromentier; J C Gripon
Journal:  Appl Environ Microbiol       Date:  1997-02       Impact factor: 4.792

3.  Genetic characterization of the major lactococcal aromatic aminotransferase and its involvement in conversion of amino acids to aroma compounds.

Authors:  L Rijnen; S Bonneau; M Yvon
Journal:  Appl Environ Microbiol       Date:  1999-11       Impact factor: 4.792

4.  Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis.

Authors:  J T Powell; J F Morrison
Journal:  J Bacteriol       Date:  1978-10       Impact factor: 3.490

5.  Transaminase B from Escherichia coli: quaternary structure, amino-terminal sequence, substrate specificity, and absence of a separate valine-alpha-ketoglutarate activity.

Authors:  F C Lee-Peng; M A Hermodson; G B Kohlhaw
Journal:  J Bacteriol       Date:  1979-08       Impact factor: 3.490

6.  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

7.  Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli.

Authors:  Bryson D Bennett; Elizabeth H Kimball; Melissa Gao; Robin Osterhout; Stephen J Van Dien; Joshua D Rabinowitz
Journal:  Nat Chem Biol       Date:  2009-06-28       Impact factor: 15.040

8.  Identification of homophenylalanine biosynthetic genes from the cyanobacterium Nostoc punctiforme PCC73102 and application to its microbial production by Escherichia coli.

Authors:  Kento Koketsu; Satoshi Mitsuhashi; Kazuhiko Tabata
Journal:  Appl Environ Microbiol       Date:  2013-01-25       Impact factor: 4.792

9.  A hydrolase from Lactobacillus sakei moonlights as a transaminase.

Authors:  Quirin Sinz; Simone Freiding; Rudi F Vogel; Wilfried Schwab
Journal:  Appl Environ Microbiol       Date:  2013-01-25       Impact factor: 4.792

10.  Metabolomics-driven quantitative analysis of ammonia assimilation in E. coli.

Authors:  Jie Yuan; Christopher D Doucette; William U Fowler; Xiao-Jiang Feng; Matthew Piazza; Herschel A Rabitz; Ned S Wingreen; Joshua D Rabinowitz
Journal:  Mol Syst Biol       Date:  2009-08-18       Impact factor: 11.429
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