PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H.
The DNA of the gene complementing a PAPS-reductase-deficient strain of Escherichia coli was sequenced. The N-terminal amino acid sequence of the purified PAPS-reductase confirmed that cys H is the structural gene for this enzyme. The open reading frame extends 732 bases and encodes for a peptide of Mr = 27927. The gene product is functionally active when supplemented with thioredoxin and immunologically related with the wild type enzyme.
Department of Biology, Ruhr University Bochum, FRG.
F A
FA
Krone
G
G
Westphal
H E
HE
Meyer
J D
JD
Schwenn
D000595:Amino Acid Sequence; D015153:Blotting, Western; D004247:DNA / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D010088:Oxidoreductases / Q000032:analysis / Q000235:genetics*; D010957:Plasmids; D011994:Recombinant Proteins / Q000032:analysis
D011994:Recombinant Proteins; D004247:DNA; D010088:Oxidoreductases; C052449:3'-phosphoadenylyl-5'-phosphosulfate reductase