Complex formation of apo-enzyme, coenzyme and substrate of D-amino acid oxidase. III. Crystallization of artificial Michaelis complexes.
作者信息
YAGI K, OZAWA T
出版信息
Biochim Biophys Acta. 1962 Jan 29;56:20-6.
PMID:14008698
Abstract
摘要
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Complex formation of apo-enzyme, coenzyme and substrate of D-amino acid oxidase. II. Spectrophotometric analysis using a substrate-substitute.D-氨基酸氧化酶的脱辅基酶、辅酶和底物的复合物形成。II. 使用底物替代物的分光光度分析。
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Complex formation of apo-enzyme, coenzyme and substrate of D-amino acid oxidase. IV. Changes in physico-chemical properties of the protein.D-氨基酸氧化酶的脱辅酶、辅酶和底物的复合物形成。IV. 蛋白质物理化学性质的变化。
Biochim Biophys Acta. 1962 Aug 13;62:397-401. doi: 10.1016/0006-3002(62)90269-x.
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Crystallization of Michaelis complex of D-amino acid oxidase.D-氨基酸氧化酶米氏复合物的结晶
Biochim Biophys Acta. 1962 Jun 18;60:200-1. doi: 10.1016/0006-3002(62)90394-3.
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COMPLEX FORMATION OF APOENZYME, COENZYME AND SUBSTRATE OF D-AMINO ACID OXIDASE. V. CHANGE IN CONFORMATION OF THE PROTEIN BY FORMING A MODEL OF ENZYME-SUBSTRATE COMPLEX.D-氨基酸氧化酶的脱辅酶、辅酶与底物的复合物形成。V. 通过构建酶-底物复合物模型研究蛋白质构象的变化。
Biochim Biophys Acta. 1963 Sep 3;77:20-6. doi: 10.1016/0006-3002(63)90465-7.
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Binding of the sulphydryl group in D-amino-acid oxidase apo-protein with flavin adenine dinucleotide.D-氨基酸氧化酶脱辅基蛋白中的巯基与黄素腺嘌呤二核苷酸的结合。
Nature. 1959 Oct 17;184(Suppl 16):1227-8. doi: 10.1038/1841227a0.
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Complex formation of apo-enzyme, co-enzyme and substrate of D-amino acid oxidase. I. Kinetic analysis using indicators.D-氨基酸氧化酶的脱辅基酶、辅酶和底物的复合物形成。I. 使用指示剂的动力学分析。
Biochim Biophys Acta. 1960 Aug 26;42:381-7. doi: 10.1016/0006-3002(60)90815-5.
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[On the crystallization and the purification of D-amino acid oxidase].[关于D-氨基酸氧化酶的结晶与纯化]
Bull Soc Chim Biol (Paris). 1960;42:569-82.
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Change of absorption spectrum of flavin adenine dinucleotide by its bining with both D-amino acid oxidase apo-protein and benzoate.黄素腺嘌呤二核苷酸与D-氨基酸氧化酶脱辅基蛋白及苯甲酸盐结合后吸收光谱的变化
Nature. 1959 Dec 19;184(Suppl 25):1938-9. doi: 10.1038/1841938a0.
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Crystallization of the complex of D-amino-acid oxidase and benzoate.D-氨基酸氧化酶与苯甲酸盐复合物的结晶
Nature. 1960 Nov 26;188:745-6. doi: 10.1038/188745a0.
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