Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site.

doi:10.1007/BF01888363

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Article

Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site.

Journal of protein chemistry - 1 Feb 1995

Buzy A, Bracchi V, Sterjiades R, Chroboczek J, Thibault P, Gagnon J, Jouve H M, Hudry-Clergeon G

Abstract excerpt

The catalase of Proteus mirabilis PR, a peroxide-resistant (PR) mutant of Proteus mirabilis, binds strongly NADPH, which is a unique property among known bacterial catalases. The enzyme subunit consists of 484 amino acid residues for a mass of 55,647 daltons. The complete amino acid sequence was...

Topics

Amino Acid Sequence
Base Sequence
Binding Sites
Catalase
Mass Spectrometry
Methionine
Molecular Sequence Data
Molecular Weight
Mutation
NADP
Protein Processing, Post-Translational
Proteus mirabilis
Sequence Alignment
Sequence Analysis
Sequence Homology, Amino Acid

Source

Open in PubMed

Identifiers

PMID: 7786407
DOI: 10.1007/BF01888363

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7786407-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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