Fujiwara K, Okamura-Ikeda K, Motokawa Y
Institute for Enzyme Research, University of Tokushima, Japan.
Biochem Biophys Res Commun. 1987 Dec 16;149(2):621-7. doi: 10.1016/0006-291x(87)90413-x.
A pyridoxal 5'-phosphate-containing peptide which contained 54 amino acid residues was isolated from chicken liver P-protein of the glycine cleavage system following reduction with NaB3H4, carboxymethylation, and proteolysis with lysylendopeptidase. Two peptides which comprise the two halves of the phosphopyridoxyl peptide were isolated from apo-P-protein. Sequence analysis of these three peptides provided the primary structure of the phosphopyridoxyl peptide and revealed that the cofactor is linked to Lys-35. The pyridoxal 5'-phosphate-binding site has the His-Lys(PLP)-X structure characteristic of known pyridoxal 5'-phosphate-dependent amino acid decarboxylases, tryptophan synthase, and serine hydroxymethyltransferase.
在用NaB₃H₄还原、羧甲基化并经赖氨酰内肽酶进行蛋白水解后,从甘氨酸裂解系统的鸡肝P蛋白中分离出一种含54个氨基酸残基的5'-磷酸吡哆醛肽。从脱辅基P蛋白中分离出构成磷酸吡哆醛肽两半部分的两个肽段。对这三个肽段的序列分析给出了磷酸吡哆醛肽的一级结构,并显示辅因子与赖氨酸-35相连。5'-磷酸吡哆醛结合位点具有已知的5'-磷酸吡哆醛依赖性氨基酸脱羧酶、色氨酸合酶和丝氨酸羟甲基转移酶所特有的His-Lys(PLP)-X结构。