Substitution at residue 473 confers progesterone 21-hydroxylase activity to cytochrome P450 2C2.

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Article

Substitution at residue 473 confers progesterone 21-hydroxylase activity to cytochrome P450 2C2.

Molecular pharmacology - 1 Sept 1995

Ramarao M, Kemper B

Abstract excerpt

The carboxyl-terminal 28 amino acids of rabbit cytochrome P450 2C2 are markedly different from those of other rabbit cytochrome P450 2C family members and, substitution of the equivalent amino acids of other cytochrome P450s can confer novel steroid hydroxylase activity to P450 2C2 while the normal lauric acid hydroxylase activity is retained. To determine the basis for the novel steroid hydroxylase activity,...

Topics

Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cytochrome P-450 CYP4A
Cytochrome P-450 Enzyme System
Enzyme Stability
Glycine
Kidney
Mixed Function Oxygenases
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Proline

Sequence Homology, Amino Acid

Serine

Steroid 21-Hydroxylase

Structure-Activity Relationship

Valine

Source

Open in PubMed

Identifiers

PMID: 7565621

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7565621-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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