EC 184.108.40.206 - Aspartate kinase
IntEnz Enzyme Nomenclature
23779 [IUBMB]L-aspartateL-aspartateName origin: UniProt - CHECKED (C)Formula: C4H6NO4
Charge: -1ChEBI compound status: CHECKED (C)ATPATPName origin: UniProt - CHECKED (C)Formula: C10H12N5O13P3
Charge: -4ChEBI compound status: CHECKED (C)<=>4-phospho-L-aspartate4-phospho-L-aspartateName origin: UniProt - CHECKED (C)Formula: C4H6NO7P
Charge: -2ChEBI compound status: CHECKED (C)
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 220.127.116.11 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
Conversion of aspartic acid to homoserine.Methods Enzymol. 5: 820-827 (1962).
Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies.J. Biol. Chem. 242: 4980-4986 (1967). [PMID: 6058940]
Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex.Biochemistry 11: 677-687 (1972). [PMID: 4551091]
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: 520-527 (1972). [PMID: 4562990]
[EC 18.104.22.168 created 1961]