Titlebook: Enzymology and Molecular Biology of Carbonyl Metabolism 7; Henry Weiner,Edmund Maser,Ronald Lindahl Book 1999 The Editor(s) (if applicable

合群

Inhibition of Human Mitochondrial Aldehyde Dehydrogenase by Metabolites of Disulfiram and Structural . to .-diethyldithiocarbamate (DDC) (Cobby .., 1977) which is further metabolized as shown in Scheme 1. The general consensus is that disulfiram is too short-lived . to account for the inhibition of ALDH2 that one its metabolites is the ultimate inhibitor (Yourick & Faiman, 1991; Hart & man, 1992).

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TEN

The Big Book of Aldehyde Dehydrogenase Sequenceshare only about 25% sequence identity with class 1 and 2 ALDHs and are homodimers. However, in main-chain folding, the structures of the class 2 and 3 monomers are nearly identical (Hempel et al., 1999)

avulsion

Book 1999inth meeting. She quickly suggested that both she and Dr. Guiliana Muzio, also of Turin, help plan the meet- ing. Each of our previous eight meetings was a unique experience for the participants. The science was always outstanding and the presentations and discussions were excellent. By moving each

臭了生氣

The Big Book of Aldehyde Dehydrogenase Sequencesy closely related homotetramers and both participate in ethanol metabolism, though class 1 ALDH. can oxidize wide range of metabolites, including retinal (reviewed Lindahl, 1982; Yoshida et al., 1). Class 3 ALDH. appear at first glance to be highly divergent from the other 2 classes. Class 3 ALDH. s

CLAMP

Reaction-Chemistry-Directed Sequence Alignment of Aldehyde Dehydrogenases arrive at the consensus of invariable residues that are essential for catalysis; a conserved feature during evolution. Thus, 16 different aldehyde dehydrogenases were compared by Hempel et al., (1993)who found 23 invariable amino acid residues by alignment of sequences available at that time.

Engulf

異端邪說下

表示問

Structure and Function of Betaine Aldehyde Dehydrogenasehways. However, they are derived from separate protein families with distinct properties. Those of the vertebrate ADHs have been well characterized since long, and their different classes belong to the MDR protein family of known structures from several sources. However, the properties and multiplic

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