Replacing the carboxy-terminal 28 residues of rabbit liver P-450 (laurate (omega-1)-hydroxylase) with those of P-450 (testosterone 16 alpha-hydroxylase) produces a new stereospecific hydroxylase activity.

doi:10.1016/0006-291x(90)92051-z

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Article

Replacing the carboxy-terminal 28 residues of rabbit liver P-450 (laurate (omega-1)-hydroxylase) with those of P-450 (testosterone 16 alpha-hydroxylase) produces a new stereospecific hydroxylase activity.

Biochemical and biophysical research communications - 16 Mar 1990

Uno T, Yokota H, Imai Y

Abstract excerpt

cDNA for chimeric P-450 consisting of the amino-terminal 462 residues of P-450 (laurate (omega-1)-hydroxylase) and the remaining 28 residues of P-450 (testosterone 16 alpha-hydroxylase) was constructed and expressed in yeast cells. The resulting chimera could catalyze laurate (omega-1)-hydroxylat...

Topics

Amino Acid Sequence
Animals
Aryl Hydrocarbon Hydroxylases
Chimera
Cytochrome P-450 CYP4A
Cytochrome P-450 Enzyme System
DNA
Microsomes, Liver
Mixed Function Oxygenases
Mutation
Plasmids
Rabbits
Restriction Mapping
Saccharomyces cerevisiae

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Open in PubMed

Identifiers

PMID: 2182013
DOI: 10.1016/0006-291x(90)92051-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2182013-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Sequence Homology, Nucleic Acid

Steroid 16-alpha-Hydroxylase

Steroid Hydroxylases

Substrate Specificity