Accession Number:

ADA429664

Title:

3-Hydroxylaminophenol Mutase From Ralstonia eutropha JMP134 Catalyzes a Bamberger Rearrangement

Descriptive Note:

Journal article

Corporate Author:

AIR FORCE RESEARCH LAB TYNDALL AFB FL

Report Date:

1999-03-01

Pagination or Media Count:

8.0

Abstract:

3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 is involved in the degradative pathway of 3-nitrophenol, in which it catalyzes the conversion of 3-hydroxylaminophenol to aminohydroquinone. To show that the reaction was really catalyzed by a single enzyme without the release of intermediates, the corresponding protein was purified to apparent homogeneity from an extract of cells grown on 3-nitrophenol as the nitrogen source and succinate as the carbon and energy source. 3-Hydroxylaminophenol mutase appears to be a relatively hydrophobic but soluble and colorless protein consisting of a single 62-kDa polypeptide. The pI was determined to be at pH 4.5. In a database search, the NH2-terminal amino acid sequence of the undigested protein and of two internal sequences of 3-hydroxylaminophenol mutase were found to be most similar to those of glutamine synthetases from different species. The enzyme requires no oxygen or added cofactors for its reaction, which suggests an enzymatic mechanism analogous to the acid-catalyzed Bamberger rearrangement.

Subject Categories:

  • Biochemistry
  • Microbiology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE