PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H

FEBS Lett. 1990 Jan 15;260(1):6-9. doi: 10.1016/0014-5793(90)80052-k.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Blotting, Western
  • DNA / analysis*
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Gene Expression Regulation, Enzymologic*
  • Genes, Bacterial*
  • Molecular Sequence Data
  • Mutation
  • Oxidoreductases / analysis
  • Oxidoreductases / genetics*
  • Plasmids
  • Recombinant Proteins / analysis

Substances

  • Recombinant Proteins
  • DNA
  • Oxidoreductases
  • 3'-phosphoadenylyl-5'-phosphosulfate reductase

Associated data

  • GENBANK/Y07525