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Modification of carboxyl groups in bovine carboxypeptidase A. I. Inactivation of the enzyme by N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K).

作者信息

Pétra P H

出版信息

Biochemistry. 1971 Aug 17;10(17):3163-70. doi: 10.1021/bi00793a001.

DOI:10.1021/bi00793a001
PMID:5165841
Abstract
摘要

相似文献

1
Modification of carboxyl groups in bovine carboxypeptidase A. I. Inactivation of the enzyme by N-ethyl-5-phenylisoxazolium-3'-sulfonate (Woodward's reagent K).牛羧肽酶A中羧基的修饰。I. N-乙基-5-苯基异恶唑鎓-3'-磺酸盐（伍德沃德试剂K）使该酶失活
Biochemistry. 1971 Aug 17;10(17):3163-70. doi: 10.1021/bi00793a001.
2
Affinity labeling of bovine carboxypeptidase A Leu by N-bromoacetyl-N-methyl-L-phenylalanine. I. Kinetics of inactivation.用N-溴乙酰基-N-甲基-L-苯丙氨酸对牛羧肽酶A亮氨酸进行亲和标记。I. 失活动力学
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3
Modification of carboxyl groups in bovine carboxypeptidase A. II. Chemical identification of a functional glutamic acid residue and other reactive groups.牛羧肽酶A中羧基的修饰。II. 一个功能性谷氨酸残基和其他反应性基团的化学鉴定
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4
Kinetics of carboxypeptidase A. II. Inhibitors of the hydrolysis of oligopeptides.羧肽酶A的动力学。II. 寡肽水解的抑制剂。
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5
Spectral properties of cobalt carboxypeptidase. The effects of substrates and inhibitors.羧肽酶钴的光谱特性。底物和抑制剂的影响。
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6
Evidence for an essential carboxyl group for yeast phosphoglycerate kinase. Reaction with Woodward's reagent K.
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7
Hybrid formation of carboxypeptidase A and fraction II of procarboxypeptidase A.羧肽酶A与羧肽酶原A的II组分的杂交形成
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8
Low pH dimerization behavior of active-site derivatives of bovine -chymotrypsin.
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9
The heterogeneity of bovine carboxypeptidase A. I. The chromatographic purification of carboxypeptidase A (Anson).牛羧肽酶A的异质性。I. 羧肽酶A（安森）的色谱纯化
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Relaxation spectra of proteinases. Isomerizations of carboxypeptidase A (Cox) and (Anson).蛋白酶的弛豫光谱。羧肽酶A（考克斯）和（安森）的异构化。
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Woodward's reagent K reacts with histidine and cysteine residues in Escherichia coli and Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases.伍德沃德试剂K与大肠杆菌和酿酒酵母磷酸烯醇式丙酮酸羧激酶中的组氨酸和半胱氨酸残基发生反应。
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4
Woodward's reagent K inactivation of Escherichia coli L-threonine dehydrogenase: increased absorbance at 340-350 nm is due to modification of cysteine and histidine residues, not aspartate or glutamate carboxyl groups.伍德沃德试剂K使大肠杆菌L-苏氨酸脱氢酶失活：340 - 350纳米处吸光度增加是由于半胱氨酸和组氨酸残基的修饰，而非天冬氨酸或谷氨酸羧基的修饰。
Protein Sci. 1996 Feb;5(2):382-90. doi: 10.1002/pro.5560050223.
5
3-Carboxy-4-nitrophenyl-dithio-1,1',2-trisnorsqualene: a site-directed inactivator of yeast oxidosqualene cyclase.
Lipids. 1993 Oct;28(10):903-6. doi: 10.1007/BF02537498.
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Studies on the active site of human leukocytic pyrogen.人白细胞热原活性部位的研究。
Inflammation. 1982 Mar;6(1):63-78. doi: 10.1007/BF00910720.
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Carboxypeptidase A mechanisms.羧肽酶A的作用机制。
Proc Natl Acad Sci U S A. 1980 Jul;77(7):3875-8. doi: 10.1073/pnas.77.7.3875.
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Inactivation of yeast hexokinase by 2-aminothiophenol. Evidence for a 'half-of-the-sites' mechanism.2-氨基硫酚对酵母己糖激酶的失活作用。“半位点”机制的证据。
Biochem J. 1988 Sep 15;254(3):819-27. doi: 10.1042/bj2540819.
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Reaction of Woodward's reagent K with D-xylose isomerases. Modification of an active site carboxylate residue.伍德沃德试剂K与D-木糖异构酶的反应。活性位点羧酸盐残基的修饰。
Biochem J. 1989 May 15;260(1):163-9. doi: 10.1042/bj2600163.
10
Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum.嗜热栖热放线菌内切葡聚糖酶D中具有催化重要性的羧基残基的修饰。
Biochem J. 1992 Jul 1;285 ( Pt 1)(Pt 1):319-24. doi: 10.1042/bj2850319.