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B6db references: 15219867

type Journal Article
authors Kessler D.
title Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity
journal Biochem Biophys Res Commun
sel selected
ui 15219867
year (2006)
volume 320
number 2
pages 571-7
keywords Animal
abstract NifS-like proteins activate sulfur for a variety of biosynthetic purposes. The genome of the cyanobacterium Synechocystis contains 4 nifS-related sequences of which only the slr0077 gene seems to be essential. In this report the heterologous production of the Slr0077 protein, its purification, and catalytic properties are described. Slr0077 produces alanine as well as pyruvate from cyst(e)ine as substrate; the product ratio depends on the redox conditions. Alanine is the typical product of orthodox NifS proteins, pyruvate formation is typical of the cystine lyase of Synechocystis which is the most peculiar member of the NifS protein family. The specific activities of Slr0077 for both reaction types are low as compared to the prototypic enzymes. Upon reaction with thiol-alkylating agents Slr0077 is not readily inactivated unlike NifS. The unique properties of Slr0077 add to the emerging picture that the NifS family of proteins comprises enzymes with a variety of distinct reactivities.
last changed 2018/03/22 11:37

B6db references