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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Mus musculus

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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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Mus musculus
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
-
-
-
-
37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
aldoA
-
-
aldolase
-
-
-
-
aldolase A
-
-
aldolase, fructose diphosphate
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-
-
-
ALDP
-
-
-
-
Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
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-
-
-
FBP aldolase
-
-
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
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-
-
-
Fructose 1,6-diphosphate aldolase
-
-
-
-
Fructose 1-monophosphate aldolase
-
-
-
-
Fructose 1-phosphate aldolase
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-
-
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose diphosphate aldolase
-
-
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
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
-
-
-
-
SMALDO
-
-
-
-
zymohexase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
flexor digitorum brevis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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knockdown of fructose-1,6-bisphosphate aldolases activates AMP-activated protein kinase even in cells with abundant glucose, while the catalysis-defective D34S aldolase mutant, which still binds fructose-1,6-bisphosphate, blocks AMP-activated protein kinase activation
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALDOB_MOUSE
364
0
39507
Swiss-Prot
other Location (Reliability: 2)
ALDOC_MOUSE
363
0
39395
Swiss-Prot
other Location (Reliability: 1)
ALDOA_MOUSE
364
0
39356
Swiss-Prot
other Location (Reliability: 1)
A6ZI44_MOUSE
418
0
45120
TrEMBL
Mitochondrion (Reliability: 5)
D3Z510_MOUSE
180
0
19573
TrEMBL
other Location (Reliability: 1)
A0A0U1RPT5_MOUSE
209
0
22625
TrEMBL
Mitochondrion (Reliability: 5)
Q9CPQ9_MOUSE
364
0
39285
TrEMBL
other Location (Reliability: 1)
D3YWI1_MOUSE
236
0
25797
TrEMBL
other Location (Reliability: 1)
A0A0U1RPN8_MOUSE
190
0
20622
TrEMBL
other Location (Reliability: 1)
Q6NY00_MOUSE
364
0
39312
TrEMBL
other Location (Reliability: 1)
A6ZI47_MOUSE
364
0
39371
TrEMBL
other Location (Reliability: 1)
Q5FWB7_MOUSE
364
0
39356
TrEMBL
other Location (Reliability: 1)
Q3TJ66_MOUSE
364
0
39521
TrEMBL
other Location (Reliability: 2)
A6ZI46_MOUSE
419
0
45344
TrEMBL
Mitochondrion (Reliability: 5)
D3YV98_MOUSE
193
0
20835
TrEMBL
Mitochondrion (Reliability: 5)
Q3UER1_MOUSE
364
0
39507
TrEMBL
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D34S
-
catalysis-defective mutant enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kramerova, I.; Kudryashova, E.; Wu, B.; Ottenheijm, C.; Granzier, H.; Spencer, M.J.
Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle
Hum. Mol. Genet.
17
3271-3280
2008
Mus musculus
Manually annotated by BRENDA team
Zhang, C.S.; Hawley, S.A.; Zong, Y.; Li, M.; Wang, Z.; Gray, A.; Ma, T.; Cui, J.; Feng, J.W.; Zhu, M.; Wu, Y.Q.; Li, T.Y.; Ye, Z.; Lin, S.Y.; Yin, H.; Piao, H.L.; Hardie, D.G.; Lin, S.C.
Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK
Nature
548
112-116
2017
Homo sapiens, Mus musculus
Manually annotated by BRENDA team