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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Pyrococcus furiosus and UniProt Accession P58314

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.13 fructose-bisphosphate aldolase
IUBMB 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.
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Pyrococcus furiosus
UNIPROT: P58314
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldolase, aldolase a, aldolase b, aldolase c, aldoa, fructose-1,6-bisphosphate aldolase, fructose-bisphosphate aldolase, aldob, fructose bisphosphate aldolase, fructose 1,6-bisphosphate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,6-Diphosphofructose aldolase
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37 kDa major allergen
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41 kDa antigen
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aldolase
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aldolase, fructose diphosphate
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ALDP
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Brain-type aldolase
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-
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CE1
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CE2
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Diphosphofructose aldolase
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FBP aldolase
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Fru-P2A
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Fructoaldolase
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Fructose 1,6-bisphosphate aldolase
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Fructose 1,6-diphosphate aldolase
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Fructose 1-monophosphate aldolase
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Fructose 1-phosphate aldolase
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Fructose bisphosphate aldolase
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Fructose diphosphate aldolase
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Fructose-1,6-bisphosphate triosephosphate-lyase
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IgE-binding allergen
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ketose 1-phosphate aldolase
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Liver-type aldolase
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Muscle-type aldolase
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Phosphofructoaldolase
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SMALDO
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zymohexase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-52-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
preferred substrate, reaction intermediate is Schiff base
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r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009
fructose 1,6-bisphosphate
50°C, pH 7
4.48
fructose 1-phosphate
50°C, pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
272000
gel filtration
31100
8 * 31100, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 31100, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siebers, B.; Brinkmann, H.; Dorr, C.; Tjaden, B.; Lilie, H.; van der Oost, J.; Verhees, C.H.
Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase
J. Biol. Chem.
276
28710-28718
2001
Pyrococcus furiosus (P58314), Pyrococcus furiosus, Thermoproteus tenax (P58315), Thermoproteus tenax
Manually annotated by BRENDA team