Dehydrogenases structural relationships

M. G. Rossman A. Liljas C. I. Branden L. J. Banaszak, Evolutionary and Structural Relationship among Dehydrogenases. 

M Arthur, C Molinas, S Dutka-Malen, P Courvalin. Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases. Gene 103(1) 133—134, 1991. 

NAD analogues. Faraday Discuss Chem Soc 74 257-265 Rossman MG, Liljas A, Branden C-I, Banaszak LJ (1975) Evolutionary and structural relationships among dehydrogenases. In Boyer PD (ed) The enzyme. Vol 11 Academic Press, New York, pp61-102 Sakurai T, Kuzuhara H, Emoto S (1979) The crystal structure and the absolute configuration of a chiral vitamin B analogue, (-)-14-... 

Evolutionary and structural relationships among dehydrogenases, 3 i The Enzymes , P.D. Boyer, ed., Academic Press, London, LL 61. 

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. 

Fig. 18. Chain trace (centre) of a subunit of dogfish muscle lactate dehydrogenase. Diagrammatic representations (corners) show constituent parts of the structure, and their relationship to the bound coenzyme. From the work of Rossmann and colleagues [79],...

Do more detailed similarities of structure and mechanism accompany the broad relationships of Branden s topological analysis [72] Functionally equivalent groups around the substrate are illustrated in Fig. 35 for lactate dehydrogenase, glyceralde-... 

X-Ray data are also useful for molecular modeling of the biological potency. Thus, the X-ray data of benzazocine 12 were manipulated in connection with its inhibitory effect on 17/3-hydroxysteroid dehydrogenase type 3 to support structure-activity relationship considerations <2006BML1532>. 

In this section on mechanism and in the section to follow on structure, the comparisons will show that the relationship between lipoamide dehydrogenase and glutathione reductase is more marked than is the relationship of either to thioredoxin reductase. Thus, in catalysis, lipoamide dehydrogenase and glutathione reductase cycle between the oxidized state and a spectrally characteristic state in which the enzyme has accepted two electrons and these are shared between the FAD and the active center disulfide. This intermediate does not seem to be operative in thioredoxin reductase, and in this enzyme the FAD and disulfide interact in a different way. The oxidized forms of these enzsrmes can then be represented as... 

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