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
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Reaction: 4.1.2.13

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

EC Number: 4.1.2.13

Enzymes and Genes:
fructose-bisphosphate aldolase C Inferred from experiment : ALDOC ( Homo sapiens )
fructose-bisphosphate aldolase A Inferred from experiment : ALDOA ( Homo sapiens )
fructose-bisphosphate aldolase B Inferred from experiment : ALDOB ( Homo sapiens )
chloroplastic fructose-bisphosphate aldolase Inferred from experiment ( Zea mays )
cytosolic fructose-bisphosphate aldolase Inferred from experiment ( Zea mays )
chloroplastic fructose-bisphosphate aldolase Inferred from experiment ( Triticum aestivum )
cytosolic fructose-bisphosphate aldolase Inferred from experiment ( Triticum aestivum )
chloroplastic fructose-bisphosphate aldolase Inferred from experiment : FBA2 ( Spinacia oleracea )
cytosolic fructose-bisphosphate aldolase Inferred from experiment : FBA1 ( Spinacia oleracea )
chloroplastic fructose-bisphosphate aldolase Inferred from experiment ( Pisum sativum )
cytosolic fructose-bisphosphate aldolase Inferred from experiment ( Pisum sativum )

In Pathway: sucrose degradation V (sucrose α-glucosidase)

Supersedes EC number: 4.1.2.7

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

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: fructose-bisphosphate aldolase

Enzyme Commission Synonyms: aldolase, fructose-1,6-bisphosphate triosephosphate-lyase, fructose diphosphate aldolase, diphosphofructose aldolase, fructose 1,6-diphosphate aldolase, ketose 1-phosphate aldolase, phosphofructoaldolase, zymohexase, fructoaldolase, fructose 1-phosphate aldolase, fructose 1-monophosphate aldolase, 1,6-Diphosphofructose aldolase, SMALDO, D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 9.480011 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.

Citations: [Alefounder89, Horecker72]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R02568 , Rhea:30851

Relationship Links: BRENDA:EC:4.1.2.13 , ENZYME:EC:4.1.2.13 , IUBMB-ExplorEnz:EC:4.1.2.13


References

Alefounder89: Alefounder PR, Baldwin SA, Perham RN, Short NJ (1989). "Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli." Biochem J 1989;257(2);529-34. PMID: 2649077

Horecker72: Horecker, B.L, Tsolas, O, Lai, C.Y (1972). "Aldolases." In: Boyer, P.D. (Ed.), The Enzymes.

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


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 Fri Dec 19, 2014, BIOCYC14A.