The Importance of Residues in Substrate Recognition Site 3 for the Catalytic Function of CYP2D25 (Vitamin D 25-Hydroxylase)
- 9 November 2001
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 288 (4), 1059-1063
- https://doi.org/10.1006/bbrc.2001.5879
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Porcine Microsomal Vitamin D3 25-Hydroxylase (CYP2D25)Journal of Biological Chemistry, 2000
- The Importance of SRS-1 Residues in Catalytic Specificity of Human Cytochrome P450 3A4Archives of Biochemistry and Biophysics, 2000
- Current Understanding of the Molecular Actions of Vitamin DPhysiological Reviews, 1998
- Microsomal 25-hydroxylation of vitamin D2 and vitamin D3 in pig liverThe Journal of Steroid Biochemistry and Molecular Biology, 1994
- Structural determinants of cytochrome P450 2B1 specificity: evidence for five substrate recognition sitesBiochemistry, 1994
- Enhanced in vivo monooxygenase activities of mammalian P450s in engineered yeast cells producing high levels of NADPH-P450 reductase and human cytochrome b5Gene, 1993
- Purification and characterization of a vitamin D3 25-hydroxylase from pig liver microsomesBiochemical Journal, 1992
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- 25-Hydroxylation of vitamin D3 by a cytochrome P-450 from rabbit liver mitochondriaBiochemical Journal, 1988
- The Carbon Monoxide-binding Pigment of Liver MicrosomesJournal of Biological Chemistry, 1964