EC 4.1.2.13 - Fructose-bisphosphate aldolase

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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
Systematic name:
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)

Reaction

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
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004332
CAS Registry Number: 9024-52-6
UniProtKB/Swiss-Prot: (185) [show] [UniProt]

References

  1. Horecker, B.L., Tsolas, O. and Lai, C.Y.
    Aldolases.
    In: Boyer, P.D. (Ed.) The Enzymes, 3rd ed. vol. 7, Academic Press, New York, 1972, 213-258
  2. Alefounder, P.R., Baldwin, S.A., Perham, R.N., Short, N.J.
    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)]