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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 1.1.1.298

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

EC Number: 1.1.1.298

Enzymes and Genes:
3-hydroxy acid dehydrogenase Inferred from experiment : ydfG
predicted malonic semialdehyde reductase Inferred from experiment : rutE

In Pathway: uracil degradation III

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

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: 3-hydroxypropionate dehydrogenase (NADP+)

Enzyme Commission Synonyms: 3-hydroxypropanoate dehydrogenase (NADP+), 3-hydroxypropionate:NADP+ oxidoreductase

Enzyme Commission Summary:
Catalyses the reduction of malonate semialdehyde to 3-hydroxypropionate, a key step in the 3-hydroxypropionate and the 3-hydroxypropionate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [Strauss93, Berg07]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [Hugler02]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.1.1.298 , ENZYME:EC:1.1.1.298 , IUBMB-ExplorEnz:EC:1.1.1.298


References

Berg07: Berg IA, Kockelkorn D, Buckel W, Fuchs G (2007). "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea." Science 318(5857);1782-6. PMID: 18079405

Hugler02: Hugler M, Menendez C, Schagger H, Fuchs G (2002). "Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO(2) fixation." J Bacteriol 184(9);2404-10. PMID: 11948153

Strauss93: Strauss G, Fuchs G (1993). "Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle." Eur J Biochem 215(3);633-43. PMID: 8354269


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 Mon Dec 22, 2014, BIOCYC13A.