Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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Escherichia coli K-12 substr. MG1655 Reaction: 2.7.2.4

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.2.4

Enzymes and Genes:
aspartate kinase III Inferred from experiment : lysC
aspartate kinase Inferred from experiment : metL
aspartate kinase Inferred from experiment : thrA

In Pathway: homoserine biosynthesis , lysine biosynthesis I

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: aspartate kinase

Enzyme Commission Synonyms: aspartokinase, AK, β-aspartokinase, aspartic kinase

Enzyme Commission Summary:
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 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.

Citations: [Veron72, Starnes72, Paulus67]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.7.2.4 , ENZYME:EC:2.7.2.4 , IUBMB-ExplorEnz:EC:2.7.2.4


References

Paulus67: Paulus H, Gray E (1967). "Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies." J Biol Chem 242(21);4980-6. PMID: 6058940

Starnes72: Starnes WL, Munk P, Maul SB, Cunningham GN, Cox DJ, Shive W (1972). "Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex." Biochemistry 11(5);677-87. PMID: 4551091

Veron72: Veron M, Falcoz-Kelly F, Cohen GN (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 1972;28(4);520-7. PMID: 4562990


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, biocyc14.