Dehydrogenase, from liver

Fig. 14. pH dependence of the pKo values of complexes of alcohol dehydrogenase from liver with (a) NADH, (b) dihydronicotinamide-benzimidazole dinucleotide... 

According to investigations by Theorell 54), the oxidation of alcohol by alcohol dehydrogenase from liver involves a binary complex of dehydrogenase -h diphosphopyridine nucleotide (DPN), while with yeast dehydrogenase the complex is ternary and includes the alcohol. Vennesland and Westheimer 55) have established, using deuteroethanol with yeast alcohol dehydrogenase, that the reaction is... 

The inhibition of succinate dehydrogenase from liver flukes in vitro by 25 substituted 2,6-dihydroxybenzanilides has been correlated with the Hansch parameter , suggesting that the distribution of the compound between lipid and aqueous phase and not electronic or steric factors within the series is responsible for the activity.113,114... 

Citric dehydrogenase, from liver, muscle and vegetable extracts, converts citric acid into acetone dicarboxylic acid, which by a second decarboxylation gives rise to acetoacetic acid. 

Acetoin dehydrogenase [from beef liver acetoin NAD oxidoreductase] [9028-49-3] Mr 76000, [EC 1.1.1.5]. Purified via the acetone cake then Ca-phosphate gel filtration (unabsorbed), lyophilised and then fractionated through a DEAE-22 cellulose column. The Km for diacetyl in 40pM and for... 

FIGURE 24.13 The subunit structure of medium chain acyl-CoA dehydrogenase from pig liver mitochondria. Note the location of the bound FAD (red). (Adapted from Kim, J-T., and Wiz, J., 1988. Structure of the medium-chain acyl-CoA clchyclro-genase from pig liver mitochonciria at 3-A resolution. Proceedings of the National Academy of Sciences, USA 85 6671-668. )... 

Lu Z-H, R Zhang, RB Diasio (1992) Purification and characterization of dihydropyrimidine dehydrogenase from human liver. J Biol Chem 267 17102-17109A. 

Of the mammalian enzymes, the sulphite oxidase of bovine liver has only recently been discovered to contain molybdenum (15). The better known molybdenum enzymes, xanthine oxidase from cows milk (31) and aldehyde oxidase from rabbit liver (16) are closely related to one another as they are to the xanthine dehydrogenases from chicken liver (17) and from bacteria (18). 

Xanthine dehydrogenase from chicken liver reacts readily with NAD as acceptor (77) while that from Micrococcus lactilyticus is inactive towards this, reacting instead with ferredoxin (18). Both enzymes react only slowly with oxygen. It seems reasonable to assume, however, that for each member of this group of enzymes, reducing substrates all react via molybdenum, as in milk xanthine oxidase. Presumably, different... 

Y. Shibusawa, T. Fujiwara, H. Shindo and Y. Ito, Purification of alcohol dehydrogenase from bovine liver crude extract by dye-ligand affinity counter current chromatography. J. Chromatogr.B, 799 (2004) 239-244. 

G. B. Strambini, Singular oxygen effects on the room-temperature phosphorescence of alcohol dehydrogenase from horse liver, Biophys. J. 43, 127-130 (1983). 

N. Barboy and J. Feitelson, Quenching of tryptophan phosphorescence in alcohol dehydrogenase from horse liver and its temperature dependence, Photochem. Photobiol. 41, 9-13 (1985). 

Cytoplasmic and mitochondrial aldehyde dehydrogenases (from beef liver) have also been inactivated by the hydrate 21 [21]. 

Activation with alcohol dehydrogenase from yeast ° Activation with alcohol dehydrogenase from horse liver... 

UDP-GlcUA By oxidation of UDP-Glc with UDP-Glc dehydrogenase from bovine liver or guinea pig liver... 

The NAD+-dependent alcohol dehydrogenase from horse liver contains one catalytically essential zinc ion at each of its two active sites. An essential feature of the enzymic catalysis appears to involve direct coordination of the enzyme-bound zinc by the carbonyl and hydroxyl groups of the aldehyde and alcohol substrates. Polarization of the carbonyl group by the metal ion should assist nucleophilic attack by hydride ion. A number of studies have confirmed this view. Zinc(II) catalyzes the reduction of l,10-phenanthroline-2-carbaldehyde by lV-propyl-l,4-dihy-dronicotinamide in acetonitrile,526 and provides an interesting model reaction for alcohol dehydrogenase (Scheme 45). The model reaction proceeds by direct hydrogen transfer and is absolutely dependent on the presence of zinc(II). The zinc(II) ion also catalyzes the reduction of 2- and 4-pyridinecarbaldehyde by Et4N BH4-.526 The zinc complex of the 2-aldehyde is reduced at least 7 x 105 times faster than the free aldehyde, whereas the zinc complex of the 4-aldehyde is reduced only 102 times faster than the free aldehyde. A direct interaction of zinc(II) with the carbonyl function is clearly required for marked catalytic effects to be observed. 

Alcohol dehydrogenase-catalyzed reduction of ketones is a convenient method for the production of chiral alcohols. HLAD, the most thoroughly studied enzyme, has a broad substrate specificity and accommodates a variety of substrates (Table 11). It efficiently reduces all simple four- to nine-membered cyclic ketones and also symmetrical and racemic cis- and trans-decalindiones (167). Asymmetric reduction of aliphatic acyclic ketones (C-4-C-10) (103,104) can be efficiently achieved by alcohol dehydrogenase isolated from Thermoanaerobium brockii (TBADH) (168). The enzyme is remarkably stable at temperatures up to 85°C and exhibits high tolerance toward organic solvents. Alcohol dehydrogenases from horse liver and T. brockii... 

Hempel J, Kaiser R, Jdmvall H. Mitochondrial aldehyde dehydrogenase from human liver primary structure, differences in relation to the cytosolic enzyme and functional correlations. Eur J Biochem 1985 153 13-28. 

Retrieve the amino acid sequences of liver alcohol dehydrogenase from six organisms to perform phylogenetic analysis. Compare phylogenetic results from Fitch-Margoliash methods without (Fitch) versus with (Kisch) molecular clock using the Dayhoff PAM 001 matrix. 

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