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PMID: 1009937 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Serine transhydroxymethylase from rabbit liver. Sequence of anonapeptide at the pyridoxal-5'-phosphate-binding site.

European journal of biochemistry ·Vol. 70 ·No. 2 ·1976-11-15 ·Pages 397-401

Bossa F, Barra D, Martini F, Schirch LV, Fasella P

Abstract

The amino acid sequence of the coenzyme-binding site of serine transhydroxymethylase from rabbit liver has been determined. After reduction with NaBH4 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-His(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.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Binding Sites Borohydrides Glycine Hydroxymethyltransferase/metabolism Liver/enzymology Peptide Fragments/analysis Protein Binding Pyridoxal Phosphate Rabbits Transferases/metabolism
Chemicals
Amino Acids Borohydrides Peptide Fragments Pyridoxal Phosphate Transferases Glycine Hydroxymethyltransferase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bossa F
Barra D
Martini F
Schirch L V
Fasella P
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1976-11-15
Pages
397-401
Language
English
Region
England
NLM ID
0107600
Subset
IM
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