|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 220.127.116.11
Enzymes and Genes:
|Homo sapiens :|
|Pisum sativum :|
|Spinacia oleracea :|
|Triticum aestivum :|
|Zea mays :|
In Pathway: sucrose degradation V (sucrose α-glucosidase)
Supersedes EC number: 18.104.22.168
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 [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.
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
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