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Article

Role of a mutated residue at the entrance of the substrate access channel in cytochrome p450 engineered for vitamin D(3) hydroxylation activity.

Biochemistry - 4 Oct 2011

Fukunishi Hiroaki, Yagi Hirotaka, Kamijo Ken'ichi, Shimada Jiro

Abstract excerpt

The cytochrome P450 enzyme engineered for enhancement of vitamin D(3) (VD(3)) hydroxylation activity, Vdh-K1, includes four mutations (T70R, V156L, E216M, and E384R) compared to the wild-type enzyme. Plausible roles for V156L, E216M, and E384R have been suggested by crystal structure analysis (Protein Data Bank 3A50 ), but the role of T70R, which is located at the entrance of the substrate access channel,...

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PMID: 21877691
DOI: 10.1021/bi2006493

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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