NAD-specific aromatic alcohol dehydrogenase
Glycine, serine and threonine metabolism
Metabolism of xenobiotics by cytochrome P450
The complete amino acid sequence of three alcohol dehydrogenase alleloenzymes (AdhN-11, AdhS and AdhUF) from the fruitfly Drosophila melanogaster.
Secondary-structure prediction from the sequence of Drosophila melanogaster (fruitfly) alcohol dehydrogenase.
Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein.
The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.
Mechanism of action of Drosophila melanogaster alcohol dehydrogenase.
Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability.
Kinetic interpretations of active site topologies and residue exchanges in Drosophila alcohol dehydrogenases.
Preliminary X-ray crystallographic studies on alcohol dehydrogenase from Drosophila.
Drosophila transcriptional repressor protein that binds specifically to negative control elements in fat body enhancers.
Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis.
The active site architecture of a short-chain dehydrogenase defined by site-directed mutagenesis and structure modeling.
Adding a positive charge at residue 46 of Drosophila alcohol dehydrogenase increases cofactor specificity for NADP+.
Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase.
Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis.
Structures important in mammalian 11 beta- and 17 beta-hydroxysteroid dehydrogenases.
Drosophila alcohol dehydrogenase: evaluation of Ser139 site-directed mutants.
Modeling studies of conformational changes in the substrate-binding loop in Drosophila alcohol dehydrogenase.
The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution.
Shaping of Drosophila alcohol dehydrogenase through evolution: relationship with enzyme functionality.
The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies.
The Drosophila virilis alcohol dehydrogenase catalytic residues are conserved.
Structure-function relationships in Drosophila melanogaster alcohol dehydrogenase allozymes ADH(S), ADH(F) and ADH(UF), and distantly related forms.
Enzymic and structural studies on Drosophila alcohol dehydrogenase and other short-chain dehydrogenases/reductases.
The catalytic mechanism of Drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site Lysine/Tyrosine pair and a NAD+ ribose OH switch.
Functional constraints of alcohol dehydrogenase (ADH) of tephritidae and relationships with other Dipteran species.
Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis.
Medium- and short-chain dehydrogenase/reductase gene and protein families : Structure-function relationships in short-chain alcohol dehydrogenases.
(A0) Lys156 (of 1mg5) modulates the activity (or pKa) of Tyr152 via 2'-hydroxyl group of NAD, along with the N1 atom of the nicotinamide group in NAD, whereas Ser139 modulates the pKa of hydroxyl oxygen of the substrate. (A1) Tyr152 acts as a general base to deprotonate the hydroxyl oxygen of the substrate. Meanwhile, the hydride transfer (a pro-S hydride transfer) occurs from the carbon atom with the hydroxyl group of the substrate to the C4 atom of the nicotinamide. (B) Hydride transfer from NADH to substrate (Reduction): (B0) Lys156 modulates the activity (or pKa) of Tyr152 via 2'-hydroxyl group of NAD(P)H, along with the N1 atom of the nicotinamide group in NADH, whereas Ser139 modulates the pKa of carbonyl oxygen of the substrate. (B1) Tyr152 acts as a general acid to protonate the carbonyl oxygen of the substrate. Meanwhile, the hydride transfer occurs from the C4 atom of the nicotinamide to the carbonyl carbon of the substrate. Whilst this enzyme does not utilize a zinc ion for catalysis, its counterparts (homologous enzymes) from vertebrates (such as D00018 in EzCatDB) requires zinc ion for catalysis (see [5]). The catalytic mechanism of this enzyme must be similar to those of the homologous enzymes with the catalytic triad, Ser-Tyr-Lys (S00320, S00324, S00325, S00326, S00328, S00329, S00331, S00336 in EzCatDB). According to the literature [20] and [28], the reaction proceeds as follows: (A) Hydride transfer from substrate to NAD (Dehydrogenation):