NDLI: Purification and Characterization ofN-Acetylmuramyl-l-alanine Amidase fromStreptomyces globisporus1829

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Purification and Characterization ofN-Acetylmuramyl-l-alanine Amidase fromStreptomyces globisporus1829

Content Provider	Scilit
Author	Kawata, Shigeo Takemura, Tadashi Takase, Yoshiyuki Yokogawa, Kanae
Copyright Year	1984
Description	The enzyme, N-acetylmuramyl-l-alanine amidase (mucopeptide aminohydrolase EC 3.5.1.18) was found in mutanolysin, which was purified partially from the cultural broth of Streptomyces globisporus 1829. This enzyme was highly purified. The overall purification was 37.5-fold with a yield of 19.2% from mutanolysin. The molecular weight of the enzyme was 18,500 as determined by plate gel filtration. The enzyme was inhibited by $Cu^{++}$. This enzyme has a preference for substances of lower molecular weight and seems to be dependent on the prior action of a hexosamidase. This enzyme is not bacteriolytic per se.
Related Links	https://www.tandfonline.com/doi/pdf/10.1080/00021369.1984.10866139?needAccess=true
Ending Page	269
Page Count	9
Starting Page	261
ISSN	09168451
e-ISSN	13476947
DOI	10.1080/00021369.1984.10866139
Journal	Bioscience, Biotechnology, and Biochemistry
Issue Number	2
Volume Number	48
Language	English
Publisher	Informa UK Limited
Publisher Date	1984-02-01
Access Restriction	Open
Subject Keyword	Microbiology Purification Bacteriolytic Purified Acetylmuramyl Fromstreptomyces Alanine Amidase Hexosamidase
Content Type	Text
Subject	Organic Chemistry Medicine Analytical Chemistry Molecular Biology Biochemistry Applied Microbiology and Biotechnology Biotechnology

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