Mechanism of serine hydroxymethylase catalyzed cleavage of L-erythro-beta-phenylserine: pH dependence of elementary kinetic processes from spectroscopic, pre-steady kinetic, and competitive inhibition studies.
作者信息
Ching W M, Kallen R G
出版信息
Biochemistry. 1979 Mar 6;18(5):821-30. doi: 10.1021/bi00572a013.
PMID:33702
Abstract
摘要
相似文献
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Mechanism of serine hydroxymethylase catalyzed cleavage of L-erythro-beta-phenylserine: pH dependence of elementary kinetic processes from spectroscopic, pre-steady kinetic, and competitive inhibition studies.
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Serine hydroxymethylase. Specificity of bond cleaveage to form quinonoid intermediates and rate of holoenzyme formation.
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Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation.甘氨酸裂解反应的机制：甘氨酸C-2位氢原子在与H蛋白相连的中间体上的保留以及丝氨酸羟甲基转移酶无法催化甘氨酸脱羧反应的证据。
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Decarboxylation of glycine by serine hydroxymethyltransferase in the presence of lipoic acid.在硫辛酸存在的情况下，丝氨酸羟甲基转移酶催化甘氨酸脱羧。
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Human Cytosolic and Mitochondrial Serine Hydroxymethyltransferase Isoforms in Comparison: Full Kinetic Characterization and Substrate Inhibition Properties.人胞质和线粒体丝氨酸羟甲基转移酶同工型的比较：完整的动力学表征和底物抑制特性
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