Category:Complex:aspartate kinase I
About
Comments (originally from EcoCyc[1][2]) This reaction, the phosphorylation of aspartate, is the first step in the biosynthesis of 4 different amino acids, namely lysine, methionine and threonine (through homoserine), and isoleucine (which is synthesized from threonine). In E. coli there are three isozymes that catalyze this step, namely aspartate kinase I, II and III. Each of the kinases is controlled by one of the end products of the different pathways (threonine, methionine and lysine, respectively). Two of the three enzymes (aspartate kinase I and II) are multifunctional proteins, also catalyzing the reaction of homoserine dehydrogenase [3][4].
References
- ↑ EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Thèze, J et al. (1974) Mapping of the structural genes of the three aspartokinases and of the two homoserine dehydrogenases of Escherichia coli K-12. J. Bacteriol. 117 133-43 PubMed
- ↑ Véron, M et al. (1972) The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. Eur. J. Biochem. 28 520-7 PubMed
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