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MetaCyc Reaction: 4.1.2.13

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 4.1.2.13

Enzymes and Genes:

Enterococcus faecalis: fructose bisphosphate aldolaseInferred from experiment: fba
Escherichia coli K-12 substr. MG1655:
Homo sapiens:
Methanocaldococcus jannaschii:
Mycoplasma pneumoniae M129: fructose-bisphosphate aldolaseInferred from experiment: fba
Pisum sativum:
Pyrococcus furiosus: fructose-1,6-bisphosphate aldolaseInferred from experiment: fba
Ricinus communis: cytosolic fructose-1,6-biphosphate aldolaseInferred from experiment
Spinacia oleracea:
Synechocystis sp. PCC 6803:
Thermotoga maritima: fructose-bisphosphate aldolaseInferred from experiment
Triticum aestivum:
Vigna radiata radiata: cytosolic fructose-1,6-bisphosphate aldolaseInferred from experiment
Zea mays:

In Pathway: glycolysis IV (plant cytosol), formaldehyde assimilation II (RuMP Cycle), formaldehyde assimilation III (dihydroxyacetone cycle), Calvin-Benson-Bassham cycle, gluconeogenesis III, glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis V (Pyrococcus), sucrose biosynthesis I (from photosynthesis), 1,3-propanediol biosynthesis (engineered), glycolysis I (from glucose 6-phosphate), gluconeogenesis I, gluconeogenesis II (Methanobacterium thermoautotrophicum)

Supersedes EC number: 4.1.2.7

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

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): 8.226501Inferred 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]

Unification Links: KEGG:R01068, Rhea:14729

Relationship Links: BRENDA:EC:4.1.2.13, ENZYME:EC:4.1.2.13, IUBMB-ExplorEnz:EC:4.1.2.13, UniProt:RELATED-TO:O04975, UniProt:RELATED-TO:O22486, UniProt:RELATED-TO:O51401, UniProt:RELATED-TO:O65581, UniProt:RELATED-TO:P00883, UniProt:RELATED-TO:P00884, UniProt:RELATED-TO:P04075, UniProt:RELATED-TO:P05062, UniProt:RELATED-TO:P05063, UniProt:RELATED-TO:P05064, UniProt:RELATED-TO:P05065, UniProt:RELATED-TO:P07341, UniProt:RELATED-TO:P07752, UniProt:RELATED-TO:P07764, UniProt:RELATED-TO:P08440, UniProt:RELATED-TO:P09117, UniProt:RELATED-TO:P09972, UniProt:RELATED-TO:P0AB71, UniProt:RELATED-TO:P13243, UniProt:RELATED-TO:P14223, UniProt:RELATED-TO:P14540, UniProt:RELATED-TO:P16096, UniProt:RELATED-TO:P17784, UniProt:RELATED-TO:P19537, UniProt:RELATED-TO:P22197, UniProt:RELATED-TO:P27995, UniProt:RELATED-TO:P29356, UniProt:RELATED-TO:P36580, UniProt:RELATED-TO:P44429, UniProt:RELATED-TO:P46256, UniProt:RELATED-TO:P46257, UniProt:RELATED-TO:P47269, UniProt:RELATED-TO:P50923, UniProt:RELATED-TO:P52210, UniProt:RELATED-TO:P53444, UniProt:RELATED-TO:P53447, UniProt:RELATED-TO:P53818, UniProt:RELATED-TO:P75089, UniProt:RELATED-TO:P93565, UniProt:RELATED-TO:Q7LZE8, UniProt:RELATED-TO:Q7LZE9, UniProt:RELATED-TO:Q7M2K6, UniProt:RELATED-TO:Q7M4Z4, UniProt:RELATED-TO:Q7M4Z5, UniProt:RELATED-TO:Q9CED4, UniProt:RELATED-TO:Q9JW15, UniProt:RELATED-TO:Q9SVJ6, UniProt:RELATED-TO:Q9URB4, UniProt:RELATED-TO:Q01516, UniProt:RELATED-TO:Q01517, UniProt:RELATED-TO:Q07159, UniProt:RELATED-TO:Q40677, UniProt:RELATED-TO:Q42476, UniProt:RELATED-TO:Q42690, UniProt:RELATED-TO:Q59100, UniProt:RELATED-TO:Q59101, UniProt:RELATED-TO:Q91384


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 Pathway Tools version 19.5 (software by SRI International) on Sat Apr 30, 2016, biocyc11.