Lowering the pH optimum of D-xylose isomerase: the effect of mutations of the negatively charged residues.

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Article

Lowering the pH optimum of D-xylose isomerase: the effect of mutations of the negatively charged residues.

Molecules and cells - 31 Aug 1998

Cha J, Batt C A

Abstract excerpt

Streptomyces rubiginosus D-xylose isomerase catalyzes the reversible isomerization of D-glucose to D-fructose. The isomerization reaction is maximized in the alkaline region of pH 8.5-8.8. The amino acid residues around two active site histidines (His-54 and His-220) and on the surface of the enz...

Topics

Aldose-Ketose Isomerases
Amino Acid Sequence
Binding Sites
DNA Mutational Analysis
Enzyme Stability
Histidine
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Research Design
Sequence Alignment
Sequence Homology, Amino Acid
Streptomyces
Temperature

Source

Open in PubMed

Identifiers

PMID: 9749522

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9749522-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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