Titlebook: Cytochrome P450; John B. Schenkman,Helmut Greim Book 1993 Springer-Verlag Berlin Heidelberg 1993 biosynthesis.cytochrome P450.enzyme.enzym

obtuse

https://doi.org/10.1007/978-3-662-38443-5y acids, drugs, and xenobiotics. The catalytic diversity required to bind and oxidize the many substrates of this monooxygenase system is possible due to the expression of multiple isozymes, many of which have overlapping substrate specificities. Relatively little is known about the topologies of th

平躺

Annual Review of Gerontology and Geriatricsiplicity is to a major extent responsible for the extremely broad substrate specificity of the hepatic microsomal monooxygenase system, although many individual cytochromes P450 catalyze the metabolism of a number of substrates and frequently display overlapping substrate specificities (. et al. 198

Foolproof

https://doi.org/10.1007/978-3-662-11155-0tematic attempts to explore substrate and inhibitor specificity of individual cytochrome P450 species have been occasional. An improved understanding of the specificity of individual cytochrome P450 enzymes, however, is desirable for several reasons. First, animal species differ from each other and

胆汁

https://doi.org/10.1007/978-3-662-11152-9 proteins possess a non-covalently bound heme (protoporphyrin IX) and segment of 26 amino acids surrounding a cysteine that is highly conserved. This cysteine donates the thiolate fifth ligand to the heme iron. The amino acid environment surrounding the heme results in a typical cytochrome P450 Sore

小木槌

暂停,间歇

Cytochrome P450978-3-642-77763-9Series ISSN 0171-2004 Series E-ISSN 1865-0325

易弯曲

Depression in Late Life: An Updateated oxygen, representing oxygen metabolites, mainly reduction products of oxygen, released from the cytochrome P-450 enzyme system. Reactive oxygen formed during the metabolic reaction of the cytochrome P-450 enzyme at the active site of the heme moiety will not be discussed here; the reader is referred to other chapters in this book.

obligation

Synapse

arthroscopy

Metabolic Reactions: Role of Cytochrome P-450 in the Formation of Reactive Oxygen Speciesated oxygen, representing oxygen metabolites, mainly reduction products of oxygen, released from the cytochrome P-450 enzyme system. Reactive oxygen formed during the metabolic reaction of the cytochrome P-450 enzyme at the active site of the heme moiety will not be discussed here; the reader is referred to other chapters in this book.