EC 4.1.2.13 - Fructose-bisphosphate aldolase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 4.1.2.13
Names
Accepted name:
fructose-bisphosphate aldolase
Other
names:
1,6-diphosphofructose aldolase
SMALDO
aldolase
diphosphofructose aldolase
fructoaldolase
fructose 1,6-diphosphate aldolase
fructose 1-monophosphate aldolase
fructose 1-phosphate aldolase
fructose diphosphate aldolase
fructose-1,6-bisphosphate triosephosphate-lyase
ketose 1-phosphate aldolase
phosphofructoaldolase
zymohexase
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
SMALDO
aldolase
diphosphofructose aldolase
fructoaldolase
fructose 1,6-diphosphate aldolase
fructose 1-monophosphate aldolase
fructose 1-phosphate aldolase
fructose diphosphate aldolase
fructose-1,6-bisphosphate triosephosphate-lyase
ketose 1-phosphate aldolase
phosphofructoaldolase
zymohexase
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
Systematic name:
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Reaction
- D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Cofactor
Comments:
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.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
DIAGRAM
,
DIAGRAM
,
DIAGRAM
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
NIST 74
,
UniPathway
Protein domains and families:
PROSITE:PDOC00143
,
PROSITE:PDOC00523
Gene Ontology:
GO:0004332
CAS Registry Number:
9024-52-6
References
-
Aldolases.In: Boyer, P.D. (Ed.) The Enzymes , 3rd ed. vol. 7 , Academic Press , New York , 1972 , 213-258
-
Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli.Biochem. J. 257 : 529-534 (1989). [PMID: 2649077]
[EC 4.1.2.13 created 1965, modified 1999 (EC 4.1.2.7 created 1961, incorporated 1972)]