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 class I Inferred from experiment : fbaB ( Escherichia coli K-12 substr. MG1655 )
fructose bisphosphate aldolase class II Inferred from experiment : fbaA ( Escherichia coli K-12 substr. MG1655 )
fructose-bisphosphate aldolase B Inferred from experiment : ALDOB ( Homo sapiens )
fructose-bisphosphate aldolase A Inferred from experiment : ALDOA ( Homo sapiens )
fructose-bisphosphate aldolase C Inferred from experiment : ALDOC ( Homo sapiens )
fructose-1,6-bisphosphate aldolase Inferred from experiment : aroA' ( Methanocaldococcus jannaschii )
6-deoxy-5-ketofructose 1-phosphate synthase Inferred from experiment : MJ1585 ( Methanocaldococcus jannaschii )
fructose bisphosphate aldolase Inferred from experiment : fba ( Enterococcus faecalis )
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 )
cytosolic fructose-1,6-bisphosphate aldolase Inferred from experiment ( Vigna radiata radiata )
fructose-1,6-bisphosphate aldolase Inferred from experiment : fba ( Pyrococcus furiosus )
fructose-1,6-biphosphate aldolase Inferred from experiment ( Pisum sativum )
fructose-1,6-phosphate aldolase Inferred from experiment ( Zea mays )
cytosolic fructose-1,6-biphosphate aldolase Inferred from experiment ( Ricinus communis )
fructose-bisphosphate aldolase Inferred from experiment : fba ( Mycoplasma pneumoniae M129 )
fructose-bisphosphate aldolase Inferred from experiment ( Thermotoga maritima )
fructose-bisphosphate aldolase Inferred from experiment : fbaB ( Synechocystis sp. PCC 6803 )
fructose-bisphosphate aldolase Inferred from experiment : fbaA ( Synechocystis sp. PCC 6803 )

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

Supersedes EC number: 4.1.2.7

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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): 8.226501 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: [Alefounder89a, 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

Alefounder89a: 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, biocyc14.