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Article

Glu327 is part of a catalytic triad in rat liver fructose-2,6-bisphosphatase.

The Journal of biological chemistry - 5 Apr 1992

Lin K, Li L, Correia J J, Pilkis S J

Abstract excerpt

The fructose-2,6-bisphosphatase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase has been shown to be structurally and functionally homologous to phosphoglycerate mutase. Both enzymes catalyze their reactions via phosphoenzyme intermediates which utilize an active site histidine as a nucleophilic phosphoacceptor and another histidine as a proton donor to the leaving group. Glu327 in the...

Topics

Animals
Catalysis
Chromatography, Gel
Circular Dichroism
DNA
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Glutamine
Kinetics
Liver
Mutagenesis, Site-Directed
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphofructokinase-2

Phosphoric Monoester Hydrolases

Rats

Source

Identifiers

PMID: 1313012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1313012-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Glu327 is part of a catalytic triad in rat liver fructose-2,6-bisphosphatase.PMID 1313012Read ↗

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