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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Leishmania mexicana and UniProt Accession Q9U5N6

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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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Leishmania mexicana
UNIPROT: Q9U5N6
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The taxonomic range for the selected organisms is: Leishmania mexicana
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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-
-
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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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-
-
-
aldolase, fructose diphosphate
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-
-
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ALDP
-
-
-
-
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
-
-
-
-
Fructose 1,6-bisphosphate aldolase
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-
-
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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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-
-
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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
-
-
-
-
zymohexase
-
-
-
-
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
-
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
NATURAL SUBSTRATE
NATURAL 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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Agaricic acid
50% inhibition at 0.03 mM
D-hexitol-1,6-bisphosphate
-
D-mannitol-1,6-bisphosphate
competitive inhibitor
suramin
50% inhibition at 0.025 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049
D-fructose 1,6-bisphosphate
pH 7.6
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.2
D-fructose 1,6-bisphosphate
pH 7.6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9U5N6_LEIME
371
0
40837
TrEMBL
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour diffusion method using 15% polyethylene glycol 5000 MME in 20 mM sodium phosphate pH 4.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G312A
mutation does not perturb ligand binding in the active site
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel chelating affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
de Walque, S.; Opperdoes, F.R.; Michels, P.A.M.
Cloning and characterization of Leishmania mexicana fructose-1,6-bisphosphate aldolase
Mol. Biochem. Parasitol.
103
279-283
1999
Leishmania mexicana (Q9U5N6), Leishmania mexicana
Manually annotated by BRENDA team
Lafrance-Vanasse, J.; Sygusch, J.
Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases
Biochemistry
46
9533-9540
2007
Leishmania mexicana (Q9U5N6), Leishmania mexicana
Manually annotated by BRENDA team