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Article

Rational design to improve the catalytic efficiency and stability of arginine deiminase.

International journal of biological macromolecules - 1 Jun 2024

Zhang Yijing, Zhang Tao, Li Mengli, Miao Ming

Abstract excerpt

Arginine deiminase (ADI) has garnered significant interest because of its ability to objectively eradicate cancer cells and produce L-citrulline. To meet the production demands, this study focused on enhancing the enzyme activity and thermal stability of ADI. In this study, 24 ADI mutants were obtained through computer aid site-specific mutation in the ADI of Enterobacter faecalis. Notably, the specific enzyme...

Read the complete abstract on PubMed

Topics

Hydrolases
Enzyme Stability
Hydrogen-Ion Concentration
Mutation
Kinetics
Protein Engineering
Biocatalysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Models, Molecular

Temperature

Source

Identifiers

PMID: 38705327
DOI: 10.1016/j.ijbiomac.2024.132083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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