Three-dimensional structures dehydrogenase

Eklund, H., et al. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 A resolution. 

Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD. Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci 2001 10 697-706. 

Lim, L.W., Shamala, N., Mathews, F.S., Steenkamp, D.J., Hamlin, R., and Xuong, N.H. 1986. Three-dimensional structure of the iron-sulfur flavoprotein trimethylam-ine dehydrogenase at 2.4-A resolution. The Journal of Biological Chemistry 261 15140-15146. 

Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M. Three-dimensional structure of rat liver -hydroxysteroid/dihydrodiol dehydrogenase a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 1994 91 2517-2521. 

Thorpe, C. Kim, J.J. (1995) Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9, 718-725. Short, clear description of the three-dimensional structure and catalytic mechanism of these enzymes. 

C. Vinals, X. De Bolle, E. Depiereux, and E. Feytmans, Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure, Proteins 1995, 21, 307-318. 

K Imada, M Sato, N Tanaka, YKatsube, Y Matsuura, T Oshima. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. J Mol Biol 222 725-738, 1991. 

The crystal structures of the E. coli DHFR-methotrexate binary complex (Bolin et al., 1982), of the Lactobacillus casei (DHFR-NADPH-methotrexate ternary complex (Filman et al., 1982), of the human DHFR-folate binary complex (Oefner et al., 1988), and of the mouse (DHFR-NADPH-trimethoprim tertiary complex (Stammers et al., 1987) have been resolved at a resolution of 2 A or better. The crystal structures of the mouse DHFR-NADPH-methotrexate (Stammers et al., 1987) and the avian DHFR—phenyltriazine (Volz et al., 1982) complexes were determined at resolutions of 2.5 and 2.9 A, respectively. Recently, the crystal structure of the E. coli DHFR—NADP + binary and DHFR-NADP+-folate tertiary complexes were resolved at resolutions of 2.4 and 2.5 A, respectively (Bystroff et al., 1990). DHFR is therefore the first dehydrogenase system for which so many structures of different complexes have been resolved. Despite less than 30% homology between the amino acid sequences of the E. coli and the L. casei enzymes, the two backbone structures are similar. When the coordinates of 142 a-carbon atoms (out of 159) of E. coli DHFR are matched to equivalent carbons of the L. casei enzyme, the root-mean-square deviation is only 1.07 A (Bolin et al., 1982). Not only are the three-dimensional structures of DHFRs from different sources similar, but, as we shall see later, the overall kinetic schemes for E. coli (Fierke et al., 1987), L. casei (Andrews et al., 1989), and mouse (Thillet et al., 1990) DHFRs have been determined and are also similar. That the structural properties of DHFRs from different sources are very similar, in spite of the considerable differences in their sequences, suggests that in the absence, so far, of structural information for ADHFR it is possible to assume, at least as a first approximation, that the a-carbon chain of the halophilic enzyme will not deviate considerably from those of the nonhalophilic ones. 

Eklund, H., Nordstrom, B., Zeppezauer, E., Soderlund, G., Ohlsson, L, Boiwe, T., Soderberg, B. 0., Tapia, O.. and Brands. C.-I. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 A resolution. J. Molec. Biol. 102, 27-59 (1976). 

The three-dimensional structure of the medium chain acyl-CoA dehydrogenases with bound substrates and inhibitors is known. A conserved glutamate side chain is positioned to pull the pro-R proton from the a carbon to create the initial enolate anion. 

Three-dimensional structures. The TPQ-con-taining amine oxidase from E. coU is a dimer of 727-residue subunits with one molecule of TPQ at position 402 in each subunit. 7458 Methylamine dehydrogenase is also a large dimeric protein of two large 46.7-kDa subunits and two small 15.5-kDa subunits. Each large subunit contains a TTQ cofactor Reduced TTQ is reoxidized by the 12.5-kDa blue copper protein amicyanin. Crystal structures have been determined for complexes of methylamine dehydrogenase with amicyanin and of these two proteins with a third protein, a small bacterial cytochrome... 

Labeyrie et al. (41) isolated a trypsin fragment of 11 kDa from S. cerevisiae flavocytochrome 62 that contained heme but was devoid of flavin and had no lactate dehydrogenase activity. The fragment, which was referred to as cytochrome 62 core, was found to have spectral properties very like those of microsomal cytochrome 65 (41). This similarity with cytochrome 65 is borne out by comparisons of amino acid sequence (42-44). The sequence similarity extends to related heme domains of sulfite oxidase (45, 46) and assimilatory nitrate reductase (47). The existence of a protein family with a common cytochrome 65 fold was suggested by Guiard and Lederer (48) and this is supported by the close similarity between the three-dimensional structures of microsomal cytochrome 65 (49) and the cytochrome domain of flavocytochrome 62 (23-25). 

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