Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system.
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.
Fujiwara
K
K
Institute for Enzyme Research, University of Tokushima, Japan.
Okamura-Ikeda
K
K
Motokawa
Y
Y
D000594:Amino Acid Oxidoreductases / Q000032:analysis*; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D050841:Glycine Dehydrogenase (Decarboxylating); D006639:Histidine / Q000502:physiology; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis*; D011732:Pyridoxal Phosphate / Q000032:analysis*
D010455:Peptides; D006639:Histidine; D011732:Pyridoxal Phosphate; D000594:Amino Acid Oxidoreductases; D050841:Glycine Dehydrogenase (Decarboxylating)