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Mechanistic studies of glutamine synthetase from Escherichia coli: kinetic evidence for two reaction intermediates in biosynthetic reaction

Proceedings of the National Academy of Sciences of the United States of America

Feb 1, 1976

S G Rhee, P Boon Chock

PMID: 1758

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Abstract

Fast reaction techniques were used to study the kinetics of protein fluorescence intensity changes that are associated with the reactions of unadenylylated Escherichia coli glutamine synthetase [L-glutamate: ammonia ligase (ADP-forming), EC 6.3.1.2] with its substrates. It was establish...read more

Mentioned in this Paper

Alkalescens-Dispar Group
Enzyme Activation
Glutamate-Ammonia Ligase
Magnesium
Paper Details
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    • References3
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  • Mechanistic studies of glutamine synthetase from Escherichia coli: kinetic evidence for two reaction intermediates in biosynthetic reaction

    Proceedings of the National Academy of Sciences of the United States of America

    Feb 1, 1976

    S G Rhee, P Boon Chock

    PMID: 1758

    DOI:

    Abstract

    Fast reaction techniques were used to study the kinetics of protein fluorescence intensity changes that are associated with the reactions of unadenylylated Escherichia coli glutamine synthetase [L-glutamate: ammonia ligase (ADP-forming), EC 6.3.1.2] with its substrates. It was establish...read more

    Mentioned in this Paper

    Alkalescens-Dispar Group
    Enzyme Activation
    Glutamate-Ammonia Ligase
    Magnesium

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    Paper Details
    References
    • References3
    • Citations13
    • References3
    • Citations13
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