Atp-dependent inactivation of escherichia coli γ-glutamylcysteine synthetase by l-glutamic acid γ-monohydroxamate

Bioscience, Biotechnology and Biochemistry

Volumn 62, Issue 7, 1998, Pages 1455-1457

  Katoh, Makoto ^a   Hiratake, Jun ^a   Oda, Jun’ichi ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

ADP forming peptide ligase; ATP dependence; Enzyme inactivation; L glutamic acid monohydroxamate; glutamylcysteine synthetase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTATE AMINOTRANSFERASE; ENZYME INHIBITOR; GLUTAMATE CYSTEINE LIGASE; GLUTAMATE GAMMA HYDROXAMIC ACID; GLUTAMATE-GAMMA-HYDROXAMIC ACID; GLUTAMIC ACID DERIVATIVE; HYDROXAMIC ACID;

ARTICLE; DRUG ANTAGONISM; ENZYMOLOGY; ESCHERICHIA COLI; PHOSPHORYLATION;

ADENOSINE TRIPHOSPHATE; ASPARTATE AMINOTRANSFERASES; ENZYME INHIBITORS; ESCHERICHIA COLI; GLUTAMATE-CYSTEINE LIGASE; GLUTAMATES; HYDROXAMIC ACIDS; PHOSPHORYLATION;

EID: 0032111648     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1455     Document Type: Article

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