Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax.
Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax.
复制标题
来自极端嗜热古细菌 Thermoproteus tenax 的两种 D-甘油醛-3-磷酸脱氢酶的表征。
DOI：
10.1111/j.1432-1033.1987.tb13703.x
复制
发表时间：
1987
期刊：
影响因子：
--
通讯作者：
F. Lottspeich
中科院分区：
文献类型：
--
作者：
R. Hensel;Silvia Laumann;J. Lang;Herrmann Heumann;F. Lottspeich
Thermoproteus tenax具有两种不同的甘油醛-3-磷酸脱氢酶，一种特异于NADP+，另一种特异于NAD+。NADP（H）相对于NAD+竞争性地抑制NAD+特异性酶，而NAD（H）实际上不与NADP+特异性酶相互作用。这两种酶分别代表亚基分子量为39 kDa（NADP+特异性酶）和49 kDa（NAD+特异性酶）的同源四聚体。如部分测序所示，NADP+特异性酶显示出与来自真细菌和真核生物的已知甘油醛-3-磷酸脱氢酶的显著同源性。所述酶是热稳定的，NADP+特异性酶在100 ° C下具有35分钟的半衰期，NAD+特异性酶在100 ° C下具有大于或等于20分钟的半衰期，这取决于蛋白质浓度。这两种酶在60-70 ℃时均显示构象和功能变化。
Thermoproteus tenax possesses two different glyceraldehyde-3-phosphate dehydrogenases, one specific for NADP+ and the other for NAD+. NADP(H) inhibits the NAD+-specific enzyme competetively with respect to NAD+ whereas NAD(H) virtually does not interact with the NADP+-specific enzyme. Both enzymes represent homomeric tetramers with subunit molecular masses of 39 kDa (NADP+-specific enzyme) and 49 kDa (NAD+-specific enzyme), respectively. The NADP+-specific enzyme shows significant homology to the known glyceraldehyde-3-phosphate dehydrogenases from eubacteria and eukaryotes as indicated by partial sequencing. The enzymes are thermostable, the NADP+-specific enzyme with a half-life of 35 min at 100 degrees C, the NAD+-specific enzyme with a half-line of greater than or equal to 20 min at 100 degrees C, depending on the protein concentration. Both enzymes show conformational and functional changes at 60-70 degrees C.
两个不连锁的黑腹果蝇甘油醛-3-磷酸脱氢酶基因的结构。
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Tso,JY;Sun,XH;Wu,R
通讯作者：
Wu,R