Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 4.1.3.41

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

EC Number: 4.1.3.41

Enzymes and Genes:
D 3-hydroxyaspartate aldolase Inferred from experiment : dhaa ( Paracoccus denitrificans IFO 13301 )

Reaction Locations: cytosol

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: 3-hydroxy-D-aspartate aldolase

Enzyme Commission Synonyms: D-3-hydroxyaspartate aldolase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 3.1899872 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans IFO 13301, is strictly D-specific as to the α-position of the substrate, but accepts both the threo and erythro forms at the β-position. The erythro form is a far better substrate (about 100 fold). The enzyme can also accept D-allothreonine, D-threonine, D-erythro-3-phenylserine and D-threo-3-phenylserine. Different from EC 4.1.3.14, L-erythro-3-hydroxyaspartate aldolase. Requires a divalent cation, such as Mg2+, Mn2+ or Co2+.

Citations: [Liu03a]

Gene-Reaction Schematic: ?

Unification Links: Rhea:27934

Relationship Links: BRENDA:EC:4.1.3.41 , ENZYME:EC:4.1.3.41 , IUBMB-ExplorEnz:EC:4.1.3.41

Credits:
Created 14-Oct-2010 by Caspi R , SRI International


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Liu03a: Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S (2003). "A novel enzyme, D-3-hydroxyaspartate aldolase from Paracoccus denitrificans IFO 13301: purification, characterization, and gene cloning." Appl Microbiol Biotechnol 62(1);53-60. PMID: 12835921


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.