Aspartokinase III

S Additional information <9, 15, 17, 18, 21, 24, 30, 33, 35> (<18> activity is regulated by light [28] <30> D-aspartate, L-glutamate and -alanine are inactive as substitutes for L-aspartate in the forward reaction, in the reverse reaction ADP cannot be replaced by AMP, UDP, GDP or IDP [1] <17> aspartokinase III, o-isomers of the derivatives of aspartic acid, including D-aspartate cr-benzyl ester and o-aspartate /)-hydroxamate are not substrates regardless of whether the a- or the -carboxyl group is derivatized, L-cysteine sulfinate and 2-methyl-DL-aspartate are no substrates... 

Keng, Y.-F. Viola, R.E. Specificity of aspartokinase III from Escherichia coli and an examination of important catalytic residues. Arch. Biochem. Biophys., 335, 73-81 (1996)... 

In many cases the amino acid pathway branches so that two or more amino acids are formed. Aspartate is the precursor of four other amino acids found in proteins Isoleucine, threonine, methionine, and lysine (see fig. 21.2). The first step in this overall pathway entails the conversion of aspartate to /3-aspartyl-phosphate by aspartokinase. One might imagine that all four of the amino acid end products of this pathway would act together to inhibit this enzyme. However, in E. coli a different solution has been found. In this bacterium there are three aspartokinases which appear to be parts of different multienzyme complexes leading to threonine and leucine for aspartokinase I, methionine for aspartokinase II and lysine for aspartokinase III. As might be expected threonine and isoleucine inhibit aspartokinase I,... 

E. coli The mutant aspartokinase III encoded by lysC was used to enhance L-threonine production A 30.9% increase in L-threonine production 14.4 Ogawa-Miyata et al. [57]... 

Removal of negative regulations can also enhance L-threonine production. By removing L-lysine-mediated feedback inhibition of aspartokinase III encoded by the lysC gene, L-threonine production could be increased by 30.9% (11.0-14.4 g L 1) in E. coli mutant strain [57]. 

Ogawa-Miyata Y, Kojima H, Sano K (2001) Mutation analysis of the feedback inhibition site of aspartokinase III of Escherichia coli K-12 and its use in L-threonine production. Biosci Biotech Biochem 65 1149-1154... 

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