Properties and purification of N-acetylmuramyl-L-alanine amidase from Staphylococcus aureus H.

Journal of bacteriology ·Vol. 112 ·No. 2 ·1972-11-00 ·Pages 932-9

Singer HJ, Wise EM, Park JT

Abstract

The principal autolytic enzyme activity of the cell sap of Staphylococcus aureus H has been purified 400-fold. It is an N-acetylmuramyl-l-alanine amidase. This enzyme has a molecular weight of 8 to 10 x 10(5), a pH optimum of 7.3, an ionic strength optimum of 0.16 m and a K(m) of 10(-3)m murein repeating units.

MeSH Terms

Alanine/biosynthesis Amidohydrolases/analysis,antagonists & inhibitors,isolation & purification,metabolism Amino Acids/biosynthesis Amino Sugars/biosynthesis Autolysis Cell Wall/metabolism Cell-Free System Centrifugation, Density Gradient Chromatography, Ion Exchange Cytoplasm/enzymology Enzyme Activation Hydrogen-Ion Concentration Molecular Weight Penicillins Peptidoglycan/metabolism Staphylococcus/enzymology,metabolism Stereoisomerism Ultrafiltration

Chemicals

Amino Acids Amino Sugars Penicillins Peptidoglycan Amidohydrolases Alanine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Singer H J

Wise E M

Park J T

References (20)

20 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.112.2.932-939.1972

Published

1972-11-00

Pages

932-9

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC251505

Subset

External Links

PubMed source DOI: 10.1128/jb.112.2.932-939.1972 PMC Full Text View journal details

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Properties and purification of N-acetylmuramyl-L-alanine amidase from Staphylococcus aureus H.

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