Open AccessSerine Transhydroxymethylase from Rabbit Liver
Author(s) -
BOSSA Francesco,
BARRA Donatella,
MARTINI Filippo,
SCHIRCH La Verne,
FASELLA Paolo
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb11029.x
Subject(s) - thermolysin , chymotrypsin , biochemistry , enzyme , sequence (biology) , serine , cofactor , peptide sequence , amino acid , chemistry , binding site , biology , microbiology and biotechnology , trypsin , gene
The amino acid sequence of′ the coenzyme‐binding site of serine transhydroxymethylase from rabbit liver has been determined. After reduction with NaBi1 4 and aminoethylation, a first sample of enzyme was digested with thermolysin and a single phosphopyridoxyl peptide was isolated. A second sample of similarly treated enzyme was digested with chymotrypsin and three phosphopyridoxyl peptides clearly originating from a unique coenzyme‐binding site were isolated. Sequence analysis of these peptides indicate the following structure: Val‐Val‐Thr‐Thr‐Thr‐His‐Lys (Pxy) ‐Thr‐Leu. Sequence homologies of the active site of various pyridoxalphosphate enzymes are discussed in terms of a possible catalytic role and of evolution of this class of proteins.