ライフサイエンスコーパス: aspartokinase

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1 phorylation was inhibited in the presence of aspartokinase.

2 activity; thus, FKBP12 is not essential for aspartokinase activity.

3 Aspartokinase also binds FKBP12 in vitro, and drugs that

4 g the yeast two-hybrid system, we identified aspartokinase, an enzyme that catalyzes an intermediate

5 hanneling of beta-aspartyl phosphate between aspartokinase and aspartate semialdehyde dehydrogenase i

6 eriments indicated that purified recombinant aspartokinase and EI(Ntr) interact directly with each ot

7 dentified, including the ryanodine receptor, aspartokinase, and the type II TGF-beta receptor; howeve

8 ce to a specific region of the mycobacterium aspartokinase (ask) gene when utilized in combinations w

9 terminal nickel-binding domain forms an ACT (aspartokinase, chorismate mutase, and TyrA) fold and con

10 activity is abolished if the C-terminal ACT (aspartokinase, chorismate, and TyrA) domain is licensed

11 and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants

12 feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to prod

13 Aspartokinase, encoded by lysC, catalyzes the phosphoryl

14 regulates the hom-thrCB operon and the thrD aspartokinase gene.

15 Aspartokinase-homoserine dehydrogenase I (AK-HDH I) from

16 The bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichi

17 atalyze consecutive metabolic reactions, the aspartokinase I domain was fused to the enzyme that cata

18 with an artificially produced monofunctional aspartokinase I, or with a fusion construct of AK I-ASAD

19 The more stable aspartokinase III is further stabilized against thermal

20 whether these experiments are conducted with aspartokinase III, a naturally occurring monofunctional

21 so created between the native monofunctional aspartokinase III, an allosteric enzyme regulated by lys

22 d suggest an unusual regulatory function for aspartokinase in regulating the phosphorylation state of

23 The activity of aspartokinase is regulated by feedback inhibition by pro

24 omplemented the lysC mutant, suggesting that aspartokinase normally affects Enzyme I(Ntr) in a manner

25 rmediate beta-aspartyl phosphate between the aspartokinase of this bifunctional enzyme and aspartate

26 auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not

27 te kinase is predicted to be a member of the aspartokinase superfamily.

28 Aspartokinase, the first enzyme in this pathway, is enco

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