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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Gallus gallus and UniProt Accession P53449

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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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Gallus gallus
UNIPROT: P53449
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The taxonomic range for the selected organisms is: Gallus gallus
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
Fructose bisphosphate aldolase
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1,6-Diphosphofructose aldolase
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-
-
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37 kDa major allergen
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-
-
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41 kDa antigen
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-
-
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aldolase
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-
-
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aldolase, fructose diphosphate
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-
-
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ALDP
-
-
-
-
Brain-type aldolase
-
-
-
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CE1
-
-
-
-
CE2
-
-
-
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Diphosphofructose aldolase
-
-
-
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FBP aldolase
-
-
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
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Fructose 1,6-bisphosphate aldolase
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-
-
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Fructose 1,6-diphosphate aldolase
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-
-
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Fructose 1-monophosphate aldolase
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-
-
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Fructose 1-phosphate aldolase
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-
-
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Fructose bisphosphate aldolase
Fructose diphosphate aldolase
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-
-
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Fructose-1,6-bisphosphate triosephosphate-lyase
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-
-
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IgE-binding allergen
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-
-
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ketose 1-phosphate aldolase
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-
-
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Liver-type aldolase
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-
-
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Muscle-type aldolase
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-
-
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Phosphofructoaldolase
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-
-
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SMALDO
-
-
-
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zymohexase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
in class I fructose diphosphate aldolases a Schiff base intermediate is formed between glycerone phosphate or fructose 1,6-diphosphate and an epsilon-amino group of a Lys residue at the active site of the enzyme
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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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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strong allosteric inhibition. I0.5: 0.00023 mM
Fluorescein 5'-isothiocyanate
results in a minimal loss of enzyme activity
glycerone phosphate
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inhibition in presence of glycerone phosphate and NaBH4
NaBH4
-
-
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45.9
D-fructose 1,6-bisphosphate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8.8
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pH 6.8: about 45% of maximal activity, pH 8.8: about 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALDOC_CHICK
137
0
14438
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
structure and amino acid composition
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schettino, C.M.; Lima, D.F.; Leyton, J.F.; ElDorry, H.A.; Bacila, M.
Studies on the structure of aldolase A from chicken muscle
Biochim. Biophys. Acta
667
411-420
1981
Gallus gallus
Manually annotated by BRENDA team
Dziewulska-Szwajkowska, D.; Zmojdzian, M.; Dobryszycki, P.; Kochman, M.; Dzugaj, A.
The interaction of FBPase with aldolase: a kinetic and fluorescence investigation on chicken muscle enzymes
Comp. Biochem. Physiol. B
137
115-129
2004
Gallus gallus
Manually annotated by BRENDA team
Gehring, A.G.; Ezzell, J.L.; Lebherz, H.G.
A selective reaction of fructose bisphosphate aldolase with fluorescein isothiocyanate in chicken muscle extracts
J. Mol. Recognit.
21
137-147
2008
Gallus gallus, Gallus gallus (P53449), Homarus americanus, Lithobates pipiens, Squalus acanthias, Crotalus oreganus helleri, Morone saxatilis, Triticum aestivum (C1J959), Spinacia oleracea (P16096)
Manually annotated by BRENDA team