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Dehydrogenases binding

Klingbeil, M.M., Walker, D.J., Arnette, R., Sidawy, E., Hayton, K, Komuniecki, P.R. and Komuniecki, R. (1996) Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum. Journal of Biological Chemistry 271, 5451-5457. [Pg.289]

Will the 6-phosphogluconate dehydrogenase bind to the CM-cellulose in the same buffer pH range used with the DEAE-cellulose Explain. In what pH range would you expect the dehydrogenase to bind to CM-cellulose Explain. [Pg.132]

Cedergren-Zeppezauer, E., Samama, J. P., Eklund, H. (1982) Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase binding... [Pg.1413]

Figure 2 Schematic representation of the reactions cataiyzed by the pyruvate dehydrogenase compiex. The Ei subunit (pyruvate dehydrogenase) binds thiamine diphosphate (TDP) the E2 subunit (dihydroiipoyi transacetyiase) contains iipoamide the E3 subunit (dihydroiipoyi dehydrogenase) binds fiavin adenine dinucieotide (FAD). Figure 2 Schematic representation of the reactions cataiyzed by the pyruvate dehydrogenase compiex. The Ei subunit (pyruvate dehydrogenase) binds thiamine diphosphate (TDP) the E2 subunit (dihydroiipoyi transacetyiase) contains iipoamide the E3 subunit (dihydroiipoyi dehydrogenase) binds fiavin adenine dinucieotide (FAD).
Cedergren-Zeppezauer E, Samama J-P, Eklund H (1982) Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase Binding of 1,4,5,6-tetrahydronicotin-amide adenine dinucleotide and trans-4-(N,N-dimethylamino)cinnam-aldehyde to the enzyme. Biochemistry 21 4895-4908 Cherest M, Felkin H, Prudent N (1968) Tortional strain involving partial bonds. The stereochemistry of the lithium aluminium hydride reduction of some simple open-chain ketones. Tetrahedron Lett 2199-2204... [Pg.95]

The dehydrogenation of L- and D-3-hydroxyacyl-CoAs is catalyzed by L- and D-3-hydroxyacyl-CoA dehydrogenases, respectively. These enzymes display strict substrate stereochemical specificity, but they both produce 3-ketoacyl-CoAs. The L-3-hydroxyacyl-CoA dehydrogenase binds its coenzyme NAD and its substrate to a cleft between its... [Pg.137]


See other pages where Dehydrogenases binding is mentioned: [Pg.78]    [Pg.497]    [Pg.771]    [Pg.798]    [Pg.110]    [Pg.52]    [Pg.511]    [Pg.6273]    [Pg.497]    [Pg.771]    [Pg.798]    [Pg.110]    [Pg.6272]    [Pg.386]    [Pg.7177]    [Pg.137]    [Pg.115]    [Pg.502]   
See also in sourсe #XX -- [ Pg.1010 , Pg.1016 ]

See also in sourсe #XX -- [ Pg.5 , Pg.1010 , Pg.1016 ]




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Adenine lactate dehydrogenase coenzyme bind

Alcohol dehydrogenase binding

Alcohol dehydrogenase, zinc binding

Coenzyme binding domain liver alcohol dehydrogenase

Dehydrogenases NAD binding structure

Dehydrogenases binding domains

Dehydrogenases initial measurements and binding

Dehydrogenases mononucleotide binding unit

Lactate dehydrogenase binding site

Lactate dehydrogenase coenzyme binding

Liver alcohol dehydrogenase NADH binding

Nucleotide binding domain dehydrogenase

Nucleotide binding domain glyceraldehyde phosphate dehydrogenase

Structure of Dehydrogenase and Substrate Binding

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