Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli.
The nucleotide sequence of the gene cysH from Escherichia coli K12 was determined. The open reading frame was 735 nucleotides in length; it was flanked by a repetitive palindromic sequence centred 36 nucleotides upstream of cysH and a terminator-like structure located 20 nucleotides downstream. CysH encoded a polypeptide of Mr 27927 consisting of 244 amino acids. The gene product was isolated as a homodimer exhibiting phospho-adenylylsulphate reductase (PAPS reductase) activity. The active enzyme was devoid of electron transferring cofactors and contained only one cysteine per subunit. Reduction of the enzyme by dithiols resulted in a shift of the apparent molecular weight from 44,000 to 62,000 without formation of an enzyme-thioredoxin complex.
Krone
F A
FA
Biochemistry of Plants, Faculty of Biology, Ruhr University Bochum, Federal Republic of Germany.
Westphal
G
G
Schwenn
J D
JD
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D015870:Gene Expression; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016366:Open Reading Frames; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D010641:Phenotype; D012091:Repetitive Sequences, Nucleic Acid; D015183:Restriction Mapping
D010088:Oxidoreductases; C052449:3'-phosphoadenylyl-5'-phosphosulfate reductase