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1 phorylation was inhibited in the presence of aspartokinase.
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 e-l-alanine ligase, uncharacterized protein, aspartokinase, chaperone protein DnaK, IGP synthase cycl
10 terminal nickel-binding domain forms an ACT (aspartokinase, chorismate mutase, and TyrA) fold and con
11 activity is abolished if the C-terminal ACT (aspartokinase, chorismate, and TyrA) domain is licensed
12 and active site residues, disrupt the FKBP12-aspartokinase complex in vivo and in vitro.fpr1 mutants
13 feedback inhibition, possibly by catalyzing aspartokinase conformational changes in response to prod
18 atalyze consecutive metabolic reactions, the aspartokinase I domain was fused to the enzyme that cata
19 with an artificially produced monofunctional aspartokinase I, or with a fusion construct of AK I-ASAD
21 whether these experiments are conducted with aspartokinase III, a naturally occurring monofunctional
22 so created between the native monofunctional aspartokinase III, an allosteric enzyme regulated by lys
23 d suggest an unusual regulatory function for aspartokinase in regulating the phosphorylation state of
25 omplemented the lysC mutant, suggesting that aspartokinase normally affects Enzyme I(Ntr) in a manner
26 rmediate beta-aspartyl phosphate between the aspartokinase of this bifunctional enzyme and aspartate
27 auxotrophs, and express wild-type levels of aspartokinase protein and activity; thus, FKBP12 is not