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Kinetic and binding effects of 1,N 6 -ethenoadenosine triphosphate to aspartate transcarbamylase.

作者信息

Chien Y, Weber G

出版信息

Biochem Biophys Res Commun. 1973 Jan 23;50(2):538-43. doi: 10.1016/0006-291x(73)90873-5.

DOI:10.1016/0006-291x(73)90873-5
PMID:4569879
Abstract
摘要

相似文献

1
Kinetic and binding effects of 1,N 6 -ethenoadenosine triphosphate to aspartate transcarbamylase.1,N6-乙烯基三磷酸腺苷对天冬氨酸转氨甲酰酶的动力学及结合效应
Biochem Biophys Res Commun. 1973 Jan 23;50(2):538-43. doi: 10.1016/0006-291x(73)90873-5.
2
Mechanism of the reaction catalyzed by the catalytic subunit of aspartate transcarbamylase. Kinetic studies with carbamyl phosphate as substrate.天冬氨酸转氨甲酰酶催化亚基所催化反应的机制。以氨甲酰磷酸为底物的动力学研究。
Biochemistry. 1973 Nov 6;12(23):4718-26. doi: 10.1021/bi00747a600.
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Modes of modifier action in E. coli aspartate transcarbamylase.
Arch Biochem Biophys. 1974 Jul;163(1):69-78. doi: 10.1016/0003-9861(74)90455-x.
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An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate.天冬氨酸转氨甲酰酶与5'-三磷酸胞苷及5'-三磷酸腺苷相互作用的平衡结合研究。
Biochemistry. 1973 Mar 27;12(7):1388-94. doi: 10.1021/bi00731a019.
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An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions.
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Interactions of Cibacron Blue F3GA and nucleotides with Escherichia coli aspartate carbamoyltransferase and its subunits.
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The interaction of tetraiodofluorescein with aspartate transcarbamylase.四碘荧光素与天冬氨酸转氨甲酰酶的相互作用。
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Regulation of aspartate carbamoyltransferase of Escherichia coli by the interrelationship of magnesium and nucleotides.
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Interaction of aspartate transcarbamylase with regulatory nucleotides.
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