Structural determinants of glutathione transferases with azathioprine activity identified by DNA shuffling of alpha class members.

doi:10.1016/j.jmb.2007.11.034

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Structural determinants of glutathione transferases with azathioprine activity identified by DNA shuffling of alpha class members.

Journal of molecular biology - 1 Feb 2008

Kurtovic Sanela, Modén Olof, Shokeer Abeer, Mannervik Bengt

Abstract excerpt

A library of alpha class glutathione transferases (GSTs), composed of chimeric enzymes derived from human (A1-1, A2-2 and A3-3), bovine (A1-1) and rat (A2-2 and A3-3) cDNA sequences was constructed by the method of DNA shuffling. The GST variants were screened in bacterial lysates for activity with the immunosuppressive agent azathioprine, a prodrug that is transformed into its active form, 6-mercaptopurine, by...

Topics

Amino Acid Sequence
Animals
Azathioprine
Base Sequence
Binding Sites
Catalysis
Cattle
Crystallography, X-Ray
DNA Shuffling
DNA, Complementary
DNA, Recombinant

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Deoxyribonuclease I

Directed Molecular Evolution

Gene Library

Genetic Variation

Glutathione

Glutathione Transferase

Humans

Source

Open in PubMed

Identifiers

PMID: 18155239
DOI: 10.1016/j.jmb.2007.11.034

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-18155239-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural determinants of glutathione transferases with azathioprine activity identified by DNA shuffling of alpha class members.PMID 18155239Read ↗

Mutational analysis of human glutathione transferase A2-2 identifies structural elements supporting high activity with the prodrug azathioprine.Semantic proximity Read ↗

Glutathione transferases in the bioactivation of azathioprine.Semantic proximity Read ↗

Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling.Semantic proximity Read ↗

An ensemble of theta class glutathione transferases with novel catalytic properties generated by stochastic recombination of fragments of two mammalian enzymes.Semantic proximity Read ↗

The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.Semantic proximity Read ↗

Diverging catalytic capacities and selectivity profiles with haloalkane substrates of chimeric alpha class glutathione transferases.Semantic proximity Read ↗

Polymorphism of human Alpha class glutathione transferases.Semantic proximity Read ↗

Molecular evolution of Theta-class glutathione transferase for enhanced activity with the anticancer drug 1,3-bis-(2-chloroethyl)-1-nitrosourea and other alkylating agents.Semantic proximity Read ↗

Orthogonal protein purification--expanding the repertoire of GST fusion systems.Semantic proximity Read ↗

Functionally diverging molecular quasi-species evolve by crossing two enzymes.Semantic proximity Read ↗

Glutathione transferases with novel active sites isolated by phage display from a library of random mutants.Semantic proximity Read ↗

Identification of Residues in Glutathione Transferase Capable of Driving Functional Diversification in EvolutionSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.