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Bovine liver glutamate dehydrogenase. Equilibria and kinetics of imine formation by lysine-97 with pyridoxal 5'-phosphate.

作者信息

Piszkiewicz D, Smith E L

出版信息

Biochemistry. 1971 Nov 23;10(24):4544-52. doi: 10.1021/bi00800a031.

DOI:10.1021/bi00800a031
PMID:4401129
Abstract
摘要

相似文献

1
Bovine liver glutamate dehydrogenase. Equilibria and kinetics of imine formation by lysine-97 with pyridoxal 5'-phosphate.牛肝谷氨酸脱氢酶。赖氨酸-97与磷酸吡哆醛形成亚胺的平衡与动力学。
Biochemistry. 1971 Nov 23;10(24):4544-52. doi: 10.1021/bi00800a031.
2
Bovine liver glutamate dehydrogenase. Equilibria and kinetics of inactivation by pyridoxal.牛肝谷氨酸脱氢酶。吡哆醛失活的平衡与动力学。
Biochemistry. 1971 Nov 23;10(24):4538-44. doi: 10.1021/bi00800a030.
3
[Analysis of functional groups of bovine liver glutamate-dehydrogenase through chemical modification].
Hoppe Seylers Z Physiol Chem. 1972 May;353(5):717.
4
Mechanism of inactivation of L-glutamate dehydrogenase by pyridoxal and pyridoxal phosphate.吡哆醛及磷酸吡哆醛使L-谷氨酸脱氢酶失活的机制。
Biochemistry. 1973 Oct 23;12(22):4367-73. doi: 10.1021/bi00746a011.
5
The nature of inhibition and inactivation of bovine liver glutamate dehydrogenase by pyridoxal 5'-phosphate.磷酸吡哆醛对牛肝谷氨酸脱氢酶的抑制和失活性质。
Biochem Soc Trans. 1975;3(1):78-80. doi: 10.1042/bst0030078.
6
Full-time course studies of bovine liver glutamate dehydrogenase. Simulation of inhibition by pyridoxal-5'-phosphate.牛肝谷氨酸脱氢酶的全日制课程研究。磷酸吡哆醛-5'-磷酸抑制作用的模拟。
Ital J Biochem. 1976 Jul-Aug;25(4):304-19.
7
The effect of modifying lysine-126 on the physical, catalytic and regulatory properties of bovine liver glutamate dehydrogenase.修饰赖氨酸-126对牛肝谷氨酸脱氢酶物理、催化及调节特性的影响
Biochem J. 1973 May;133(1):173-82. doi: 10.1042/bj1330173.
8
Molecular interactions of competitive inhibitors with bovine liver glutamate dehydrogenase.
J Biol Chem. 1971 Apr 10;246(7):2004-9.
9
Inactivation of bovine glutamate dehydrogenase by carbamyl phosphate and cyanate.氨甲酰磷酸和氰酸盐对牛谷氨酸脱氢酶的失活作用。
J Biol Chem. 1972 Feb 10;247(3):754-9.
10
Molecular interactions of six aromatic competitive inhibitors with bovine liver glutamate dehydrogenase.
Biochim Biophys Acta. 1972 Feb 28;258(2):343-50. doi: 10.1016/0005-2744(72)90225-2.

引用本文的文献

1
The effect of pyridoxal phosphate on the activity of aldolase from Lemna minor L.磷酸吡哆醛对浮萍（ Lemna minor L. ）醛缩酶活性的影响。
Planta. 1977 Jan;137(3):265-70. doi: 10.1007/BF00388161.
2
Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds.磷酸化芳香族化合物对兔肌肉醛缩酶的抑制作用。
Biochem J. 1997 Apr 1;323 ( Pt 1)(Pt 1):71-7. doi: 10.1042/bj3230071.
3
Is pyridoxal 5'-phosphate an affinity label for phosphate-binding sites in proteins?: The case of bovine glutamate dehydrogenase.5'-磷酸吡哆醛是蛋白质中磷酸结合位点的亲和标记物吗？：以牛谷氨酸脱氢酶为例。
Biochem J. 1993 Sep 15;294 ( Pt 3)(Pt 3):835-9. doi: 10.1042/bj2940835.
4
Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.5'-磷酸吡哆醛对羟甲基胆色素原合酶（胆色素原脱氨酶）的修饰。一个必需赖氨酸残基的证明。
Biochem J. 1984 Aug 15;222(1):93-102. doi: 10.1042/bj2220093.
5
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.牛肝谷氨酸脱氢酶。利用化学修饰研究不同氨基酸底物催化位点之间的关系以及亚基动力学不等价性的问题。
Biochem J. 1984 Sep 15;222(3):621-6. doi: 10.1042/bj2220621.
6
Protection of glutamate dehydrogenase by nicotinamide-adenine dinucleotide against reversible inactivation by pyridoxal 5'-phosphate as a sensitive indicator of conformational change induced by substrates and substrate analogues.烟酰胺腺嘌呤二核苷酸对谷氨酸脱氢酶的保护作用，使其免受5'-磷酸吡哆醛的可逆失活，以此作为底物和底物类似物诱导构象变化的敏感指标。
Biochem J. 1974 Dec;143(3):569-74. doi: 10.1042/bj1430569.
7
Kinetic analysis of protein modification reactions at equilibrium.平衡状态下蛋白质修饰反应的动力学分析。
Biochem J. 1989 Nov 1;263(3):855-9. doi: 10.1042/bj2630855.
8
The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate.牛肝谷氨酸脱氢酶的变构机制。圆二色性研究对三元复合酶-（氧化型烟酰胺腺嘌呤二核苷酸）-戊二酸构象变化的证据。
Biochem J. 1977 May 1;163(2):297-302. doi: 10.1042/bj1630297.