Literature DB >> 4147977

Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphate.

A Brown, J M Culver, H F Fisher.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1973        PMID: 4147977     DOI: 10.1021/bi00746a011

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


× No keyword cloud information.
  4 in total

1.  Ox liver glutamate dehydrogenase. The role of lysine-126 reappraised in the light of studies of inhibition and inactivation by pyridoxal 5'-phosphate.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-09       Impact factor: 3.857

2.  Modification of pig M4 lactate dehydrogenase by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-07       Impact factor: 3.857

3.  The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal5'-phosphate. A demonstration that covalent modification with this reagent completely abolishes catalytic activity.

Authors:  S S Chen; P C Engel
Journal:  Biochem J       Date:  1975-05       Impact factor: 3.857

4.  Ox liver glutamate dehydrogenase. The use of chemical modification to study the relationship between catalytic sites for different amino acid substrates and the question of kinetic non-equivalence of the subunits.

Authors:  S E Syed; P C Engel
Journal:  Biochem J       Date:  1984-09-15       Impact factor: 3.857

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.