The N-Terminal Membrane Domain of Yeast NADPH-Cytochrome P450 (CYP) Oxidoreductase Is Not Required for Catalytic Activity in Sterol Biosynthesis or in Reconstitution of CYP Activity-Reference-Cited by-同舟云学术

The N-Terminal Membrane Domain of Yeast NADPH-Cytochrome P450 (CYP) Oxidoreductase Is Not Required for Catalytic Activity in Sterol Biosynthesis or in Reconstitution of CYP Activity

Published:1998-02 Issue:8 Volume:273 Page:4492-4496
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Venkateswarlu K.,Lamb David C.,Kelly Diane E.,Manning Nigel J.,Kelly Steven L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase.

2. NADPH-P-450 reductase: Structural and functional comparisons of the eukaryotic and prokaryotic isoforms

3. Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase.

4. Genetically Engineered Modification of P450 Monooxygenases: Functional Analysis of the Amino-Terminal Hydrophobic Region and Hinge Region of the P450/Reductase Fused Enzyme

5. Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region.

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