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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Drosophila melanogaster
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4.1.2.13 fructose-bisphosphate aldolaseIUBMB 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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Word Map
- 4.1.2.13
- creatine
-
phosphofructokinase
- enolase
- hexokinase
- isozyme
- isoenzymes
- dihydroxyacetone
- glucose-6-phosphate
- erythrocyte
- phosphoglycerate
- aminotransferase
- albumin
- transaminase
- malate
- intolerance
- gapdh
- hereditary
- muscular
-
phosphokinase
- glycogen
- pentose
- myopathy
- plasmodium
-
gluconeogenesis
-
schiff
- falciparum
- transketolase
- phosphoglucomutase
-
purkinje
- dermatomyositis
- mutase
-
phosphoglucose
-
entner-doudoroff
- dhap
- myositis
- 6-phosphogluconate
-
gluconeogenic
-
calvin
- myoglobin
- myalgia
- fructose-1,6-bisphosphatase
- tpi
- rhabdomyolysis
- polymyositis
- fbpase
- fructokinase
- medicine
-
electromyography
- glycosomal
-
parasagittal
-
glutamic-oxalacetic
- molecular biology
- drug development
- diagnostics
- food industry
- agriculture
- synthesis
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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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-
-
-
aldolase
-
-
-
-
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
-
Brain-type aldolase
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-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
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-
-
-
FBP aldolase
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-
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
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
-
-
-
-
Fructose diphosphate aldolase
-
-
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
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-
-
-
IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Liver-type aldolase
-
-
-
-
Muscle-type aldolase
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-
-
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Phosphofructoaldolase
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-
-
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SMALDO
-
-
-
-
zymohexase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9024-52-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALF_DROME
361
0
39047
Swiss-Prot
other Location (Reliability: 1)
F3YDA0_DROME
394
0
42700
TrEMBL
other Location (Reliability: 4)
Q9VBF5_DROME
364
0
40252
TrEMBL
other Location (Reliability: 1)
A4V3G1_DROME
363
0
39561
TrEMBL
other Location (Reliability: 1)
C8VV14_DROME
361
0
39047
TrEMBL
other Location (Reliability: 1)
B6IDI2_DROME
353
0
39021
TrEMBL
other Location (Reliability: 1)
F3YDB5_DROME
363
0
39619
TrEMBL
other Location (Reliability: 1)
F3YDE2_DROME
363
0
39589
TrEMBL
other Location (Reliability: 1)
Q86NZ4_DROME
77
0
8408
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brenner-Holzach, O.
Properties of fructose 1,6-diphosphate aldolase from Drosophila melanogaster
Arch. Biochem. Biophys.
194
321-327
1979
Drosophila melanogaster
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