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Clustering Method in QMMM Modeling of the HLADH Binding

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2013-05-01 · Horse Liver Alcohol Dehydrogenase (HLADH) is a zinc-containing enzyme, successfully used in biocatalysis [20], [21], [22]. Native HLADH is found in two isoforms, E and S, which leads in vivo to the formation of a dimeric enzyme of mixed composition (EE, ES and SS) [23]. The enantiomer selectivity of HLADH with respect to the racemic -ketone substrates (), (), (), and has been examined, showing that the enzyme exhibits a remarkable selectivity which is opposite to that indicated by the microbial -ketone rule for and . HLADH-NADH-PhCHO Jia Luo and Thomas C. Bruice* Contribution from the Department of Chemistry and Biochemistry, UniVersity of California at Santa Barbara, Santa Barbara, California 93106 ReceiVed April 16, 2001 Abstract: Molecular dynamics simulations of the oxidation of benzyl alcohol by horse liver alcohol dehydrogenase (HLADH) have been Human dihydrolipoamide dehydrogenase (hLADH, hE3) deficiency (OMIM# 246900) is an often prematurely lethal genetic disease usually caused by inactive or partially inactive hE3 variants.

Fractions exhibiting high levels of enzyme activity (43 to 47 min) were collected and desalted using a Centriprep YM-30 filter unit. We report the crystal structures of the human (dihydro)lipoamide dehydrogenase (hLADH, hE3) and its disease-causing homodimer interface mutant D444V-hE3 at 2.27 and 1.84 Å resolution, respectively. The wild type structure is a unique uncomplexed, unliganded hE3 structure with the true canonical sequence 2013-05-01 The initial step in reactions catalyzed by NAD(P)H-dependent alcohol dehydrogenases (ADHs) is the binding of the cofactor to the active site.

Biocatalysed redox reactions in aqueous and organic media

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K212O0161-0180.pdf

7 The kinetic parameters of 1,4-BD (Fig. S1 †) as well as EtOH and i PrOH were determined (Table S1 †) showing that HLADH exhibits a reasonable apparent K M value of 23 mM towards 1,4-BD In the HLADH molecule, the position of the active site is well known: the enzyme subunits are divided into two different domains (the coenzyme binding domain and the catalytic domain). These domains are separated by a crevice that contains a wide and deep pocket which is the binding site for the substrate and the nicotinamide moiety of the coenzyme [ [ 24 ] ]. 2000-09-01 HLADH, in order to understand the essential factors in- volved in the productive binding between coenzyme and apo-enzyme [17-20]. In this paper we present the results of detailed kinetic studies on HLADH with PEG-NAD ÷ as coenzyme, and an extension of our modelling studies hLADH pathogenic mutants [13,17].

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This procedure has allowed the formation of valuable (S)‐lactones in good to excellent conversions and enantiomeric excess. 1991-10-01 2012-04-28 2010-01-01 The RMSF of HLADH at water contents below 10 % (v/v) indicate a rigid enzymatic structure relative to that in the purely aqueous system. This behavior is followed by an increase in enzymatic flexibility at 10 % ( v / v ) water; however, the RMSFs of mixtures of glyceline/water (12.5 to 20 % v / v ) are still much lower than that of the average RMSF of HLADH in water. HLADH was selected as the best biocatalyst, in terms of specific activity and kinetic parameters. Moreover, HLADH catalyzed oxidation of Cbz-ethanolamine was performed and the direct formation of the acid, Cbz-glycine, was observed.

The following three states have been studied: HLADH·PhCH2OH·NAD+ (MD1), HLADH·PhCH2O-·NAD+ (MD2), and HLADH·PhCHO·NADH (MD3). In our preliminary report on HLADH reaction under pressure [32], kinetic parameters and thermodynamic activation volumes of HLADH oxidation of ethanol with the coenzyme NAD + as oxidizing agent In the HLADH molecule, the position of the active site is well known: the enzyme subunits are divided into two different domains (the coenzyme binding domain and the catalytic domain). These domains are separated by a crevice that contains a wide and deep pocket which is the binding site for the substrate and the nicotinamide moiety of the coenzyme [ [ 24 ] ]. 2013-05-01 · Horse Liver Alcohol Dehydrogenase (HLADH) is a zinc-containing enzyme, successfully used in biocatalysis [20], [21], [22].
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The resulting cross-correlation map allowed the identiﬁcation of the correlated and anticorrelated motions, which involve the entire protein. Anticor- Furthermore, the effect of the silicon atom on the HLADH-catalysed reaction was examined in comparison with the corresponding carbon compounds. HLADH HLADH isoenzyme S. 말의 간에서 분리된 알코올 탈수소효소(Horse liver alcohol dehydrogenase ：H L A D H )는 효소(apoen- zy m e ).

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The product had an isolated yield of 89.7% or 15.3 g L -1. The predicted range of possible polyamine products by this method is broad since many amino alcohols are putative substrates for HLADH. Examples 1 and 2 in the following table were carried out by a batchwise procedure, ie. the enzyme HLADH and cyclohexanone were added to the catholyte only after the indirect electrochemical hydrogenation of NAD ♁ to NADH, and the cyclohexanol was then determined. HLADH was selected as the best biocatalyst, in terms of specific activity and kinetic parameters. Moreover, HLADH catalyzed oxidation of Cbz-ethanolamine was performed and the direct formation of the acid, Cbz-glycine, was observed.