Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity.

doi:10.1093/protein/12.1.63

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Article

Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity.

Protein engineering - 1 Jan 1999

Yoshida H, Kojima K, Witarto A B, Sode K

Abstract excerpt

An engineered Escherichia coli PQQ glucose dehydrogenase (PQQGDH) with improved enzymatic characteristics was constructed by substituting and combining the gene-encoding protein regions responsible for EDTA tolerance, thermal stability and substrate specificity. The protein region responsible for...

Topics

Acinetobacter
Amino Acid Sequence
Circular Dichroism
Edetic Acid
Enzyme Stability
Escherichia coli
Genotype
Glucose Dehydrogenases
Kinetics
Models, Biological
Molecular Sequence Data
Phenotype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Engineering

Protein Structure, Secondary

Recombinant Fusion Proteins

Sequence Homology, Amino Acid

Substrate Specificity

Temperature

Source

Open in PubMed

Identifiers

PMID: 10065712
DOI: 10.1093/protein/12.1.63

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-10065712-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

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