Purification and characterization of O-acetylserine sulfhydrylase of Corynebacterium glutamicum

9Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

We highly purified O-acetylserine sulfhydrylase from the glutamate-producing bacterium Corynebacterium glutamicum. The molecular mass of the purified enzyme was 34,500 as determined by SDS-polyacrylamide gel electrophoresis, and 70,800 as determined by gel filtration chromatography. It had an apparent Km of 7.0 mM for O-acetylserine and a Vmax of 435 μmol min-1 (mg·protein)-1. This is the first report of the cysteine biosynthetic enzyme of C. glutamicum in purified form.

Cite

CITATION STYLE

APA

Wada, M., Awano, N., Yamazawa, H., Takagi, H., & Nakamori, S. (2004). Purification and characterization of O-acetylserine sulfhydrylase of Corynebacterium glutamicum. Bioscience, Biotechnology and Biochemistry, 68(7), 1581–1583. https://doi.org/10.1271/bbb.68.1581

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free