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Thermophiles glyceraldehyde-3-phosphate

V. Rehaver and R. Jaenicke, Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyper-thermophilic eubaderium Thermotoga maritima, J. Biol. Chem. 1992, 267, 10999-11006. [Pg.59]

Pyrococcus endeavori (unpublished results ), hydrogenases from Methanococcus jannaschii and the extreme thermophile Methanococcus igneus, a-glucosidase from P. furiosus, glyceraldehyde-3-phosphate dehydrogenase from Thermotoga... [Pg.327]

The importance of the ionic bonds in the thermostabilization was emphasized by Perutz (1978). From differences in rate of denaturation in mesophilic and thermophilic molecules, Perutz (1978) has evaluated the extrastabilization energy to be no more than 2 kcal/mole in ferredoxin and 5-10 kcal/mole in glyceraldehyde-3-phosphate dehydrogenase. Proteins from thermophilic organisms offer a very good example, allowing one to... [Pg.323]

See other pages where Thermophiles glyceraldehyde-3-phosphate is mentioned: [Pg.235]    [Pg.351]    [Pg.775]    [Pg.324]    [Pg.5]    [Pg.13]    [Pg.16]    [Pg.213]    [Pg.775]    [Pg.329]    [Pg.452]    [Pg.473]    [Pg.61]    [Pg.72]    [Pg.175]    [Pg.114]    [Pg.115]    [Pg.323]   


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Glyceraldehyd

Glyceraldehyde 3-phosphate

Thermophiles

Thermophilic

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