PMID:338862
| Citation |
Fimmel, AL and Loughlin, RE (1977) Isolation and characterization of cysK mutants of Escherichia coli K12. J. Gen. Microbiol. 103:37-43 |
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| Abstract |
cysK mutants, deficient in O-acetylserine sulphydrylase A [O-acetyl-L-serine acetate-lyase (adding hydrogen-sulphide); EC 4.2.99.8], were isolated as strains resistant to selenite or giving a black colour reaction on bismuth citrate indicator medium. All were resistant to the inhibitor I,2,4-triazole. Four independent mutants were found which possessed lowered levels of O-acetylserine sulphydrylase activity and also partially constitutive levels of NADPH-sulphite reductase [hydrogen-sulphide: NADP+ oxidoreductase; EC I.8.I.2]. Strains containing both a cysE mutation and a cysK mutation lacked the constitutive levels of NADPH-sulphite reductase showing that these levels were due to the in vivo concentration of the inducer, O-acetylserine. The cysK locus was found to be 81% cotransducible with the ptsI gene. |
| Links | |
| Keywords |
Chromosome Mapping; Chromosomes, Bacterial; Cysteine Synthase/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/isolation & purification; Mutation; Oxidoreductases/metabolism |
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