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Glyceraldehyde-3-phosphate dehydrogenase crystal structure

The relatively unhindered domain motion in immunoglobulins may be contrasted with that observed in some enzymes, in which the domain motion occurs upon substrate binding during the catalytic cycle. The phenomenon has been established by crystal structure analysis of the different forms of yeast hexokinase [11], liver alcohol dehydrogenase [12] and citrate synthase [13], and appears to occur also in glyceraldehyde-3-phosphate-dehydrogenase. [Pg.11]


See other pages where Glyceraldehyde-3-phosphate dehydrogenase crystal structure is mentioned: [Pg.27]    [Pg.151]    [Pg.39]    [Pg.28]    [Pg.198]    [Pg.452]    [Pg.472]    [Pg.573]   
See also in sourсe #XX -- [ Pg.374 ]




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Dehydrogenase phosphate

Dehydrogenases glyceraldehyde-3-phosphate dehydrogenase

Dehydrogenases structure

Glyceraldehyd

Glyceraldehyd dehydrogenase

Glyceraldehyde 3-phosphate

Glyceraldehyde dehydrogenase

Glyceraldehyde phosphate dehydrogenase

Glyceraldehyde phosphate dehydrogenases

Glyceraldehyde-3-phosphate dehydrogenase structure

Phosphate crystallization

Phosphates structure

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