Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.

doi:10.1096/fj.11-191254

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Article

Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Mar 2012

Bansal Saurabh, Srivastava Ankit, Mukherjee Goutam, Pandey Ramendra, Verma Anita Kamra, Mishra Prashant, Kundu Bishwajit

Abstract excerpt

Thermophilic l-asparaginases display high stability and activity at elevated temperatures. However, they are of limited use in leukemia therapy because of their low substrate affinity and reduced activity under physiological conditions. In an attempt to combine stability with activity at physiological conditions, 3 active-site mutants of Pyrococcus furiosus l-asparaginase (PfA) were developed. The mutants,...

Topics

Amino Acid Sequence
Antineoplastic Agents
Archaeal Proteins
Asparaginase
Catalytic Domain
Cell Line, Tumor
Cell Survival
Circular Dichroism
Dose-Response Relationship, Drug

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Enzyme Stability

HL-60 Cells

Hot Temperature

Humans

K562 Cells

Kinetics

Models, Molecular

Molecular Dynamics Simulation

Molecular Sequence Data

Source

Open in PubMed

Identifiers

PMID: 22166247
DOI: 10.1096/fj.11-191254

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-22166247-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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