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PMID: 179530 Published · ppublish English Journal Article

Yeast phosphoglycerate mutate. Cyanogen bromide cleavage and amino acid sequence of an active-site peptide.

The Biochemical journal ·Vol. 153 ·No. 2 ·1976-02-01 ·Pages 145-9

Fothergill LA, Hodgson GI

Abstract

The molecular weight and amino acid composition of phosphoglycerate mutase from yeast were determined. CNBr cleavage produced a large (190-residue) fragment and a small (60-residue) fragment. Tryptic and chymotryptic peptides derived from the large fragment were fractionated by ion-exchange chromatography. Peptides from two histidine-containing regions were isolated and the amino acid sequences were determined. Correlation of these data with X-ray-crystallographic evidence shows that the histidine residue in the sequence Arg-Leu Asn-Glu-Arg-His-Tyr-Gly-Asp-Leu-Glu-Gly-Lys is located at the active site.

MeSH Terms
Amino Acid Sequence Binding Sites Cyanogen Bromide Molecular Weight Peptide Fragments/analysis Phosphoglycerate Mutase/analysis Phosphotransferases/analysis Saccharomyces cerevisiae/enzymology
Chemicals
Peptide Fragments Phosphotransferases Phosphoglycerate Mutase Cyanogen Bromide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fothergill L A
Hodgson G I
References (21)
21 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1976-02-01
Pages
145-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1172556
Subset
IM
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