Carbonyl Reductases and Pluripotent HydroxysteroidDehydrogenases of the Short-Chain Dehydrogenase/ReductaseSuperfamily:Structural Aspects of Oligomerization in 3alpha-HydroxysteroidDehydrogenase /Carbonyl Reductase from Comamonas testosteroni:New Approaches for efficient Protein Design

Carbonyl reduction of aldehydes, ketones and quinones to their corresponding hydroxy de-rivatives plays an important role in the phase-I metabolism of many endogenous (biogenic aldehydes, steroids, prostaglandins, reactive lipid peroxidation products) and xenobiotic (pharmacologic drugs, carcinogens...

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Bibliographische Detailangaben
1. Verfasser: Hoffmann-Geim, Frank
Beteiligte: Buckel, Wolfgang (Prof. Dr.) (BetreuerIn (Doktorarbeit))
Format: Dissertation
Sprache:Deutsch
Veröffentlicht: Philipps-Universität Marburg 2009
Biologie
Schlagworte:
SDR
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Zusammenfassung:Carbonyl reduction of aldehydes, ketones and quinones to their corresponding hydroxy de-rivatives plays an important role in the phase-I metabolism of many endogenous (biogenic aldehydes, steroids, prostaglandins, reactive lipid peroxidation products) and xenobiotic (pharmacologic drugs, carcinogens, toxicants) compounds. Carbonyl-reducing enzymes are grouped into two large protein superfamilies, the aldo-keto reductases (AKR) and the short-chain dehydrogenases/reductases (SDR). Whereas aldehyde reductase and aldose reductase are AKRs, several forms of carbonyl reductase belong to the SDRs. In addition, there exist a variety of pluripotent hydroxysteroid dehydrogenases (HSDs) of both superfamilies which specifically catalyze the oxidoreduction at different positions of the steroid nucleus, and which also catalyze rather non-specifically the reductive metabolism of a great number of non-steroidal carbonyl compounds. The present review summarizes recent findings on car-bonyl reductases and pluripotent HSDs of the SDR protein superfamily.
ISBN:978-3-8366-3391-8
DOI:https://doi.org/10.17192/z2009.0563