The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: aspartate kinase
Reaction: ATP + L-aspartate = ADP + 4-phospho-L-aspartate
For diagram of lysine biosynthesis (early stages), click here
Other name(s): aspartokinase; AK; β-aspartokinase; aspartic kinase
Systematic name: ATP:L-aspartate 4-phosphotransferase
Comments: The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-50-4
1.  Black, S. Conversion of aspartic acid to homoserine. Methods Enzymol. 5 (1962) 820–827.
2.  Paulus, H. and Gray, E. Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies. J. Biol. Chem. 242 (1967) 4980–4986. [PMID: 6058940]
3.  Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex. Biochemistry 11 (1972) 677–687. [PMID: 4551091]
4.  Véron, M., Falcoz-Kelly, F. and Cohen, G.N. 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 (1972) 520–527. [DOI] [PMID: 4562990]
5.  Chassagnole, C., Rais, B., Quentin, E., Fell, D. A. and Mazat, J.-P. An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. Biochem. J. 356 (2001) 415–423. [PMID: 11368768]
6.  Curien, G., Ravanel, S., Robert, M. and Dumas, R. Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. J. Biol. Chem. 280 (2005) 41178–41183. [PMID: 16216875]
[EC created 1961]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald