
Isolation of a gene encoding cysteine synthase from Flavobacterium K 3–15
Author(s) -
Müller Rolf,
Kuttler Elke,
Lanz Christa,
Drewke Christel,
Schmidt Karsten
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08065.x
Subject(s) - cysteine , biochemistry , gene , biology , amino acid , gene product , enzyme , serine , peptide sequence , microbiology and biotechnology , gene expression
The cysteine synthase gene ( cysK ) from Flavobacterium K 3–15 was cloned and sequenced. The gene exhibits 30–50% identity to known cysteine synthases on both the DNA and the amino acid levels. The pyridoxal phosphate binding site of the enzyme is part of a conserved motif comprising seven amino acids (SIKDRIA). The lys31 residue of the flavobacterial enzyme is conserved in all known cysteine synthases. The cysK gene from Flavobacterium K 3–15 was heterologously expressed and the gene product identified by immunoblotting and determination of the enzyme activity.