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.
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。
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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。
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本文引用的文献
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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。
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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。
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