Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I.

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作者信息

Truffa-Bachi P, Veron M, Cohen G N

出版信息

CRC Crit Rev Biochem. 1974;2(3):379-415. doi: 10.3109/10409237409105452.

DOI:10.3109/10409237409105452

PMID:4155358

Abstract

摘要

相似文献

Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I.

CRC Crit Rev Biochem. 1974;2(3):379-415. doi: 10.3109/10409237409105452.

Relaxation studies on an allosteric enzyme: aspartokinase I-homoserine dehydrogenase I.

Cold Spring Harb Symp Quant Biol. 1972;36:193-8. doi: 10.1101/sqb.1972.036.01.026.

Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 (lambda). Activation by monovalent cations and an analysis of the effect of the adenosine triphosphate-magnesium ion complex on this activation process.大肠杆菌K12（λ）的天冬氨酸激酶I-高丝氨酸脱氢酶I。单价阳离子的激活作用以及三磷酸腺苷-镁离子复合物对该激活过程影响的分析。

J Biol Chem. 1975 Feb 25;250(4):1242-50.

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain.

Eur J Biochem. 1972 Aug 4;28(4):520-7. doi: 10.1111/j.1432-1033.1972.tb01939.x.

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. 4. Isolation, molecular weight, amino acid analysis and behaviour of the sulfhydryl groups of the protein catalyzing the two activities.

Eur J Biochem. 1968 Jun;5(1):73-80. doi: 10.1111/j.1432-1033.1968.tb00339.x.

Augmentation by -aspartyl phosphate of threonine control of the dehydrogenase activity of the aspartokinase-homoserine dehydrogenase complex.

Biochem Biophys Res Commun. 1972 Oct 6;49(1):159-63. doi: 10.1016/0006-291x(72)90023-x.

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K-12. Incubation of the enzyme in alkaline conditions: dissociation and disulfide-bridge formation.大肠杆菌K-12的苏氨酸敏感型高丝氨酸脱氢酶和天冬氨酸激酶活性。在碱性条件下对酶进行孵育：解离和二硫键形成。

Eur J Biochem. 1976 Mar 1;62(3):485-90. doi: 10.1111/j.1432-1033.1976.tb10182.x.

Characterization of the threonine-sensitive aspartokinase--homoserine dehydrogenase of Escherichia coli K12 by transient electric birefringence.

Arch Biochem Biophys. 1974 Jan;160(1):205-14. doi: 10.1016/s0003-9861(74)80027-5.

The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Specific inactivation of the homoserine dehydrogenase activity by the affinity label, 2-amino-4-oxo-5-chloropentanoic acid.大肠杆菌K12的苏氨酸敏感型高丝氨酸脱氢酶和天冬氨酸激酶活性。亲和标记物2-氨基-4-氧代-5-氯戊酸对高丝氨酸脱氢酶活性的特异性失活作用。

Eur J Biochem. 1975 Jan 2;50(2):425-30. doi: 10.1111/j.1432-1033.1975.tb09819.x.

Interaction of substrates and inhibitors with the homoserine dehydrogenase of kinase-inactivated aspartokinase I.底物和抑制剂与激酶失活的天冬氨酸激酶I的高丝氨酸脱氢酶的相互作用。

Biochemistry. 1977 Apr 19;16(8):1541-8. doi: 10.1021/bi00627a002.

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Kinetic and spectroscopic evidence of cation-induced conformation changes in yeast K+ -activated aldehyde dehydrogenase.阳离子诱导酵母钾离子激活醛脱氢酶构象变化的动力学和光谱学证据。

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