N-acetylmuramyl-L-alanine amidase of Vi phage III.

Abstract:

:1. A lytic enzyme was isolated from Vi phage III-induced lysate of Salmonella typhi, and purified about 200-fold by chromatography on IRC-50, CM-cellulose, and Sephadex G-75 columns. 2. Both E. coli B murein and muropeptide C6 were digested on incubation with the lytic enzyme. The main product of murein and muropeptide C6 digestion is identical with tetrapeptide Ala-Glu-DAP-Ala. The release of amino groups during digestion was not accompanied by the appearance of either reducing groups or hexosamines. 3. It is concluded that Vi phage III-induced lytic enzyme is N-acetylmuramyl-L-alanine amidase, which cleaves the amide bond between N-acetylmuramic acid and L-alanine.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Jastrzemski KB

subject

Has Abstract

pub_date

1975-01-01 00:00:00

pages

207-304

issue

4

eissn

0001-527X

issn

1734-154X

journal_volume

22

pub_type

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