Sphingomyelinase C from Streptomyces sp. A9107: Unusual primary structure for bacterial sphingomyelinase C

descriptionPublicationkeyboard_double_arrow_right Article 01 Oct 2012 English Publisher:Elsevier BVJournal:Journal of Bioscience and Bioengineering, volume 114, pages 398-401 (issn: 1389-1723,

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Authors: Takayuki, Sogabe; Hiroko, Ota; Miyuki, Iwasaki; Shin-ichi, Sakasegawa; Tomohiro, Tamura;

doi: 10.1016/j.jbiosc.2012.05.005

pmid: 22664344

Sphingomyelinase C from Streptomyces sp. A9107: Unusual primary structure for bacterial sphingomyelinase C

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Abstract

A sphingomyelinase C (SMase) was identified in the culture supernatant of Streptomyces sp. A9107 (S-SMase). Although S-SMase seems to be a typical bacterial SMase, the primary structure of S-SMase was unusual for known bacterial SMase. The gene was functionally overexpressed in the culture medium of recombinant Rhodococcus erythropolis.

Related Organizations

Hokkaido Bunkyo University
Japan
Hokkaido University
Japan
National Institute of Advanced Industrial Science and Technology
Japan

Keywords

Industrial Microbiology, Sphingomyelin Phosphodiesterase, Molecular Sequence Data, Amino Acid Sequence, Sequence Alignment, Streptomyces, Substrate Specificity

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