Glutamic acid γ-monohydroxamate and hydroxylamine are alternate substrates for Escherichia coli asparagine synthetase B

Biochemistry

Volumn 35, Issue 9, 1996, Pages 3031-3037

  Boehlein, Susan K ^a   Schuster, Sheldon M ^a,b   Richards, Nigel G J ^c  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF FLORIDA   (United States)

^c University of Florida   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARAGINE; ASPARTATE AMMONIA LIGASE; GLUTAMIC ACID GAMMA HYDROXAMIC ACID; HYDROXYLAMINE; NITROGEN;

AMINO ACID SUBSTITUTION; AMINO ACID SYNTHESIS; ARTICLE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE MUTATION; NITROGEN METABOLISM; NONHUMAN; PRIORITY JOURNAL;

ASPARTATE AMINOTRANSFERASES; ASPARTATE-AMMONIA LIGASE; ENZYME INHIBITORS; ESCHERICHIA COLI; GLUTAMATES; HYDROXAMIC ACIDS; HYDROXYLAMINE; HYDROXYLAMINES; ISOENZYMES; KINETICS; MODELS, CHEMICAL; PLASMIDS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 0029670135     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952505l     Document Type: Article

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