Literature DB >> 5416664

The mechanism of transamination. Function of the histidyl residue at the active site of supernatant aspartate transaminase.

D L Peterson, M Martinez-Carrion.   

Abstract

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Year:  1970        PMID： 5416664

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  4 in total

1.  Identification of amino acid residues essential for enzyme activity of sheep liver 5,10-methylenetetrahydrofolate reductase.

Authors:  K Varalakshmi; H S Savithri; N A Rao
Journal:  Biochem J       Date:  1986-05-15       Impact factor: 3.857

2.  The sequences of the coenzyme-binding peptide in the cytoplasmic and the mitochondrial aspartate aminotransferases from sheep liver.

Authors:  M Campos-Cavieres; C P Milstein
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

3.  Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase.

Authors:  G C Ford; G Eichele; J N Jansonius
Journal:  Proc Natl Acad Sci U S A       Date:  1980-05       Impact factor: 11.205

4.  A three-component monooxygenase from Rhodococcus wratislaviensis may expand industrial applications of bacterial enzymes.

Authors:  Makoto Hibi; Dai Fukuda; Chihiro Kenchu; Masutoshi Nojiri; Ryotaro Hara; Michiki Takeuchi; Shunsuke Aburaya; Wataru Aoki; Kimihiko Mizutani; Yoshihiko Yasohara; Mitsuyoshi Ueda; Bunzo Mikami; Satomi Takahashi; Jun Ogawa
Journal:  Commun Biol       Date:  2021-01-04
  4 in total

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