Aspartate transcarbamylase. A study by transient nuclear magnetic resonance of the binding of succinate to the native enzyme and its catalytic subunit.
作者信息
Sykes B D, Schmidt P G, Stark G R
出版信息
J Biol Chem. 1970 Mar 10;245(5):1180-9.
PMID:4906846
Abstract
摘要
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Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate.天冬氨酸转氨甲酰酶的弛豫光谱。天然酶与氨甲酰磷酸的相互作用。
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Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit.天冬氨酸转氨甲酰酶的弛豫光谱。I. 5-溴胞苷三磷酸与天然酶及调节亚基的相互作用。
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Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate.天冬氨酸转氨甲酰酶。与过渡态类似物N-（膦酰乙酰基）-L-天冬氨酸的相互作用。
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Reaction of the catalytic subunit of Escherichia coli aspartate transcarbamylase with permanganate ion, a reactive structural analogue of phosphate ion.
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Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.天冬氨酸转氨甲酰酶。对L-天冬氨酸结合位点的立体特异性限制。
J Biol Chem. 1970 Mar 10;245(5):1175-9.
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Substrate anchoring and the catalytic power of enzymes.底物锚定与酶的催化能力。
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Proton magnetic resonance studies of cholinergic ligand binding to the acetylcholine receptor in its membrane environment.在膜环境中，对胆碱能配体与乙酰胆碱受体结合进行的质子磁共振研究。
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