Alcohol dehydrogenase, molecular

Many enzymes incorporate one or more metal ions as essential parts of their structure. Different metalloenzymes make use of ions of magnesium, calcium, manganese, iron, cobalt, copper, zinc, or molybdenum. For example, the molecule of alcohol dehydrogenase (molecular mass 87000 d), which catalyzes the oxidation of ethanol to acetic acid in the human liver, contains two atoms of zinc, and the amylase in human saliva contains an atom of calcium (Ca" " ). Some enzyme molecules contain several metal atoms, which may be of different kinds. An example is cysteamine oxidase, which catalyzes the oxidation of cysteamine, HSCH2CH2NH2 this enzyme contains an atom of iron, an atom of copper, and an atom of zinc. 

Misra, K., Baneqee, A.B., Ray, S., et al., 1996. Reduction of methylglyoxal in Escherichia coli K12 by an aldehyde reductase and alcohol dehydrogenase. Molecular and Cellular Biochemistry 156,117-124. 

Adsorption processes, undesirability, 280 Alcohol dehydrogenase, molecular interfacing with nicotinamide adenine dinucleotide, 311-312,313/... 

U Ryde. Molecular dynamics simulations of alcohol dehydrogenase with a four- or five-coordinate catalytic zinc ion. Proteins 21 40-56, 1995. 

Figure 8.5 Reduction of ketone with alcohol dehydrogenase from Thermoanaerobacter species using molecular hydrogen as a hydrogen source [5a].

Dennis, E.S., Sachs, M.M., Gerlach, W.L., Finnegan, E.J. Peacock, W.J. (1985). Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize. Nucleic Acids Research, 13, 727-43. 

Llewellyn, D.J., Finnegan, E.J., Ellis, J.G., Dennis, E.S. Peacock, W.J. (1987). Structure and expression of an alcohol dehydrogenase 1 gene from Pisum sativum (cv. Greenfeast ). Journal of Molecular Biology, 195,115-23. 

Determination of molecular mass of pectic enzymes The molecular mass were determined by gel filtration in a Sepharose CL-6B column (1,8 x 88cm) equilibrated and eluted with Tris-HCl 50 mM, pH 7,5 buffer, plus 100 mM KCl. Fractions (3,3 ml) were collected at a flow rate of 10 ml/h. Molecular mass markers were tyroglobulin (660 kDa) apoferritin (440 kDa) P-amylase (200 kDa) alcohol dehydrogenase (150 kDa) bovine serum albumin (66 kDa) and carbonic anhydrase (29 kDa). Urea-SDS-PAGE (7%) was carried out according to Swank and Munkres [12]. Molecular mass markers were myosin (205 kDa) p-galactosidase (116 kDa) phosphorylase b (97 kDa) bovine serum albumin (66 kDa), ovalbumin (45 kDa) and carbonic anhydrase (29 kDa). 

Figure 3. (A) Determination of molecular mass of pectic enzymes by gel filtration in Sepharose 6B. Molecular mass markers - tyroglobulin, 2- apoferritin, 3- p-amylase, 4-alcohol dehydrogenase, 5- bovine serum albumin, 6- carbonic anhydrase. (B) SDS-PAGE of pectolytic activities. Molecular mass markers 1- myosin, 2- p-galactosidase, 3- phosphorylase b, 4- bovine serum albumin, 5- ovalbumin, 6- carbonic anhydrase.

MARTINEZ, M.C., ACHKOR, H., PERSSON, B., FERNANDEZ, M.R., SHAFQAT, J., FARRES, J., JORNVALL, H., PARES, X., Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class P and liver class I alcohol dehydrogenases, Eur. J. Biochem., 1996,241, 849-857. 

Recently, we adopted the same system for the reduction of 4-phenyl-2-butanone to (S)-4-phenyl-2-butanol using the NADH-dependent horse liver alcohol dehydrogenase (HLADH) and S-ADH from Rhodococcus sp [68] with high enantioselectivity (Fig. 17) [69]. As mediator, we applied the low-molecular... 

Catalysis. Enzymes, with more than 2000 known representatives, are the largest group of proteins in terms of numbers (see p.88). The smallest enzymes have molecular masses of 10-15 kDa. Intermediatesized enzymes, such as alcohol dehydrogenase (top left) are around 100-200 kDa, and the largest-including glutamine synthetase with its 12 monomers (top right)—can reach more than 500 kDa. 

Bruchhaus I, Tannich E (1994) Purification and molecular characterization of the NAD(+)-dependent acetaldehyde alcohol-dehydrogenase from Entamoeba histolytica. Biochem J 303 743-748... 

Hansch, C. et al. (1986) A quantitative structure-activity relationship and molecular graphics analysis of hydrophobic effects in the interactions of inhibitors with alcohol dehydrogenase. J. Med. Chem., 29 (5), 615-620. 

Horse liver alcohol dehydrogenase has a molecular weight of 80 000 and is made up of two subunits, each containing two zinc atoms. The subunits are not active in the monomeric form. 

Alcohol dehydrogenase is also obtained from yeast. Yeast alcohol dehydrogenase (YADH) was the first pyridine nucleotide-dependent dehydrogenase to be crystallized by Negelein and Wulff in 1937.1342 YADH is a tetramer of molecular weight 140000-150000. The amount of zinc determined varies,1343 but there are strong indications that the subunits of YADH and LADH have similar structures, including the presence of two zinc atoms. 

In this chapter I will focus on biochemical and molecular aspects leading to lignin production. We have studied in detail phenylalanine ammonia lyase (PAL EC 4.3.1.5), the first enzyme of the general phenylpropanoid pathway, and cinnamyl alcohol dehydrogenase (CAD EC 1.1.1.195), an enzyme specific to the branch pathway leading to lignin formation. 

Walter, M.H., Grima-Pettenati, J., Grand, C., Boudet, A.M. Lamb, C.J. (1988). Cinnamyl alcohol dehydrogenase, a molecular marker specific for lignin synthesis cDNA cloning and mRNA induction by fungal elicitor. Proceedings of the National Academy of Sciences (USA) 86, 5546-50. 

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