Negative co-operativity in glutamate dehydrogenase: coenzyme-binding studies.
作者信息
Melzi d'Eril G, Dalziel K
出版信息
Biochem J. 1972 Nov;130(1):3P. doi: 10.1042/bj1300003pa.
Abstract
摘要
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Negative co-operativity in glutamate dehydrogenase: coenzyme-binding studies.
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本文引用的文献
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Circular dichroism studies on the complex between beef liver glutamate dehydrogenase and NADH.
FEBS Lett. 1971 Dec 1;19(2):149-151. doi: 10.1016/0014-5793(71)80500-8.
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Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase.
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Bovine liver glutamate dehydrogenase: tentative amino acid sequence; identification of a reactive lysine; nitration of a specific tyrosine and loss of allosteric inhibition by guanosine triphosphate.
Proc Natl Acad Sci U S A. 1970 Oct;67(2):724-30. doi: 10.1073/pnas.67.2.724.
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Sedimentation equilibrium studies on glutamic dehydrogenase.
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The binding of oxidized coenzymes by glutamate dehydrogenase and the effects of glutarate and purine nucleotides.
Biochem J. 1972 Feb;126(4):975-84. doi: 10.1042/bj1260975.
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Active centre equivalent weight of glutamate dehydrogenase from dry weight determinations and spectrophotometric titrations of abortive complexes.
Biochim Biophys Acta. 1971 Oct;250(1):47-50. doi: 10.1016/0005-2744(71)90118-5.
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Evidence for two nicotinamide binding sites on L-glutamate dehydrogenase.
Biochem Biophys Res Commun. 1971 Nov;45(4):964-71. doi: 10.1016/0006-291x(71)90431-1.
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Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes.
Biochem J. 1969 Dec;115(4):621-31. doi: 10.1042/bj1150621.
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