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Dehydrogenase 3-dimensional structures

Eklund, H., et al. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 A resolution. [Pg.33]

R9. Rowland, P., Basak, A. K., Gover, S., Levy, H. R., and Adams, M. J., The 3-dimensional structure of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0-angstrom resolution. Structure 2, 1073-1087 (1994). [Pg.49]

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. [Pg.436]

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. [Pg.236]

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. [Pg.246]

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. [Pg.653]

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. [Pg.486]

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. [Pg.552]

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. [Pg.20]

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). [Pg.687]

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. [Pg.789]


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See also in sourсe #XX -- [ Pg.768 ]

See also in sourсe #XX -- [ Pg.768 ]

See also in sourсe #XX -- [ Pg.768 ]

See also in sourсe #XX -- [ Pg.768 ]




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