Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system

Biochem Biophys Res Commun. 1987 Dec 16;149(2):621-7. doi: 10.1016/0006-291x(87)90413-x.

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.

MeSH terms

  • Amino Acid Oxidoreductases / analysis*
  • Amino Acid Sequence
  • Animals
  • Chickens
  • Glycine Dehydrogenase (Decarboxylating)
  • Histidine / physiology
  • Molecular Sequence Data
  • Peptides / analysis*
  • Pyridoxal Phosphate / analysis*

Substances

  • Peptides
  • Histidine
  • Pyridoxal Phosphate
  • Amino Acid Oxidoreductases
  • Glycine Dehydrogenase (Decarboxylating)