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Article

Thr268 in substrate binding and catalysis in P450BM-3.

Archives of biochemistry and biophysics - 1 Jan 1998

Truan G, Peterson J A

Abstract excerpt

Members of the gene superfamily of proteins called "P450" catalyze monooxygenation reactions that require an input of two electrons and a molecule of oxygen per catalytic cycle. These proteins are widely distributed among living organisms, from bacteria to human. P450BM-3, a soluble protein isolated from Bacillus megaterium, is self-sufficient, containing P450 and reductase domains on the same polypeptide....

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Source

Identifiers

PMID: 9439582
DOI: 10.1006/abbi.1997.0400

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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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Thr268 in substrate binding and catalysis in P450BM-3.PMID 9439582Read ↗

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The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant.Semantic proximity Read ↗

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Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants.Semantic proximity Read ↗

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