z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here