| Literature DB >> 3426593 |
K Fujiwara1, K Okamura-Ikeda, Y Motokawa.
Abstract
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.Entities:
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Year: 1987 PMID: 3426593 DOI: 10.1016/0006-291x(87)90413-x
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575