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PMID: 588262 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Lysostaphin endopeptidase-catalysed transpeptidation reactions of the imino-transfer type.

The Biochemical journal ·Vol. 167 ·No. 1 ·1977-10-01 ·Pages 293-6

Sloan GL, Smith EC, Lancaster JH

Abstract

The glycylglycine endopeptidase in lysostaphin has been found capable of catalysing both hydrolysis and transpeptidation reactions when acting on glycyl peptides. The ability of the enzyme to utilize dansyldiglycine (5-dimethylaminoaphthalene-1-sulphonylglycylglycine) as an acceptor molecule in transpeptidation reactions, although it is incapable of hydrolysing the peptide bond in this compound, indicates the enzyme must be capable of forming the equivalent of an imino-enzyme intermediate during the catalytic process.

MeSH Terms
Dansyl Compounds Endopeptidases/metabolism Glycylglycine Lysostaphin/metabolism
Chemicals
Dansyl Compounds Glycylglycine Endopeptidases lysostaphin endopeptidase Lysostaphin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sloan G L
Smith E C
Lancaster J H
References (11)
11 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1977-10-01
Pages
293-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1183651
Subset
IM
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