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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Thermoproteus tenax and UniProt Accession P58315

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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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Thermoproteus tenax
UNIPROT: P58315
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The taxonomic range for the selected organisms is: Thermoproteus tenax
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-1,6-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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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
-
-
-
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Brain-type aldolase
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-
-
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CE1
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-
-
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CE2
-
-
-
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Diphosphofructose aldolase
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-
-
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FBP aldolase
Fru-P2A
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-
-
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Fructoaldolase
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-
-
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Fructose 1,6-bisphosphate aldolase
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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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Fructose bisphosphate aldolase
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Fructose diphosphate aldolase
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fructose-1,6-bisphosphate aldolase
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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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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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-
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SMALDO
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-
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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
-
-
?
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
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-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036
fructose 1,6-bisphosphate
50°C, pH 7
0.71
fructose 1-phosphate
50°C, pH 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
241000
gel filtration
28700
8 * 28700, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 28700, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of Y146F covalently bound to the carbinolamine intermediate of the substrate fructose 1,6-bisphosphate and noncovalently bound to the cyclic form of the substrate. The structures are determined at a resolution of 1.9 A and refined to crystallographic R factors of 0.148 and 0.149, respectively. The crystal structure of the W144E/Y146F double-mutant substrate complex represents the first example where the cyclic form of beta-fructose 1,6-bisphosphate is noncovalently bound to FBPA I
the crystal structure of the archaeal FBPA revealed that the protein fold is that of a parallel (betaalpha)8 barrel
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y146F
catalytically deficient mutant
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
Lorentzen, E.; Siebers, B.; Hensel, R.; Pohl, E.
Structure, function and evolution of the Archaeal class I fructose-1,6-bisphosphate aldolase
Biochem. Soc. Trans.
32
259-263
2004
Thermoproteus tenax
Manually annotated by BRENDA team
Lorentzen, E.; Siebers, B.; Hensel, R.; Pohl, E.
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates
Biochemistry
44
4222-4229
2005
Thermoproteus tenax (P58315), Thermoproteus tenax
Manually annotated by BRENDA team
Tittmann, K.
Sweet siblings with different faces the mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data
Bioorg. Chem.
57
263-280
2014
Thermoproteus tenax
Manually annotated by BRENDA team