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羟甲基胆色素原合酶（胆色素原脱氨酶）的吡咯甲烷辅因子通过半胱氨酸-242的硫原子与蛋白质结合的证据。

Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.

作者信息

Miller A D, Hart G J, Packman L C, Battersby A R

机构信息

University of Cambridge Chemical Laboratory, U.K.

出版信息

Biochem J. 1988 Sep 15;254(3):915-8. doi: 10.1042/bj2540915.

DOI:10.1042/bj2540915
PMID:3196304
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1135172/
Abstract

The pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli is bound to the protein through the sulphur atom of a cysteine residue [Hart, Miller & Battersby (1988) Biochem. J. 252, 909-912; Beifuss, Hart, Miller & Battersby (1988) Tetrahedron Lett. 29, 2591-2594]. We show that the pyrromethane-binding residue is cysteine-242.

摘要

来自大肠杆菌的羟甲基胆色素原合酶（胆色素原脱氨酶）的吡咯甲烷辅因子通过半胱氨酸残基的硫原子与蛋白质结合[哈特、米勒和巴特斯比（1988年）《生物化学杂志》252卷，909 - 912页；贝福斯、哈特、米勒和巴特斯比（1988年）《四面体快报》29卷，2591 - 2594页]。我们证明，吡咯甲烷结合残基是半胱氨酸 - 242。

相似文献

1
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242.羟甲基胆色素原合酶（胆色素原脱氨酶）的吡咯甲烷辅因子通过半胱氨酸-242的硫原子与蛋白质结合的证据。
Biochem J. 1988 Sep 15;254(3):915-8. doi: 10.1042/bj2540915.
2
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.羟甲基胆色素原合酶（胆色素原脱氨酶）的吡咯甲烷辅因子通过半胱氨酸残基的硫原子结合的证据。
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3
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本文引用的文献

1
Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.胆色素原脱氨酶的作用机制。球形红假单胞菌中胆色素原与胆色素原脱氨酶之间稳定的酶底物共价中间体的参与情况。
Biochem J. 1981 Apr 1;195(1):177-81. doi: 10.1042/bj1950177.
2
Biosynthesis of the pigments of life: formation of the macrocycle.生命色素的生物合成：大环的形成。
Nature. 1980 May 1;285(5759):17-21. doi: 10.1038/285017a0.
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Modification of hydroxymethylbilane synthase (porphobilinogen deaminase) by pyridoxal 5'-phosphate. Demonstration of an essential lysine residue.5'-磷酸吡哆醛对羟甲基胆色素原合酶（胆色素原脱氨酶）的修饰。一个必需赖氨酸残基的证明。
Biochem J. 1984 Aug 15;222(1):93-102. doi: 10.1042/bj2220093.
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The biosynthesis of porphyrins, chlorophylls, and vitamin B12.卟啉、叶绿素和维生素B12的生物合成。
Nat Prod Rep. 1985 Dec;2(6):561-80. doi: 10.1039/np9850200561.
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The biosynthesis of porphyrins, chlorophylls, and vitamin B12.卟啉、叶绿素和维生素B12的生物合成。
Nat Prod Rep. 1985 Feb;2(1):19-47. doi: 10.1039/np9850200019.
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Primary structure of the activation segment of procarboxypeptidase A from porcine pancreas.猪胰羧肽酶原A激活片段的一级结构。
Biochem Biophys Res Commun. 1986 Dec 15;141(2):517-23. doi: 10.1016/s0006-291x(86)80203-0.
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Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.来自大肠杆菌的羟甲基胆色素原合酶（胆色素原脱氨酶）的纯化、N端氨基酸序列及性质
Biochem J. 1986 Nov 15;240(1):273-6. doi: 10.1042/bj2400273.
8
Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12.编码大肠杆菌K12胆色素原脱氨酶的hemC基因座的核苷酸序列。
Nucleic Acids Res. 1986 Aug 11;14(15):6215-26. doi: 10.1093/nar/14.15.6215.
9
Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue.羟甲基胆色素原合酶（胆色素原脱氨酶）的吡咯甲烷辅因子通过半胱氨酸残基的硫原子结合的证据。
Biochem J. 1988 Jun 15;252(3):909-12. doi: 10.1042/bj2520909.
10
The biosynthesis of porphyrins, chlorophylls, and vitamin B12.卟啉、叶绿素和维生素B12的生物合成。
Nat Prod Rep. 1987 Aug;4(4):441-69. doi: 10.1039/np9870400441.