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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Synechocystis sp. and UniProt Accession Q55664

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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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Synechocystis sp.
UNIPROT: Q55664
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Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
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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41 kDa antigen
-
-
-
-
aldolase
-
-
-
-
aldolase, fructose diphosphate
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-
-
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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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-
-
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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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-
-
-
Fructose diphosphate aldolase
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-
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
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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
-
-
-
r
sedoheptulose 1,7-bisphosphate
?
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
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
best divalent cation, optimal concentration: 0.2 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-ribulose 1,5-bisphosphate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.009
D-fructose 1,6-bisphosphate
0.008 - 0.047
sedoheptulose 1,7-bisphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.59
D-ribulose 1,5-bisphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.77
-
class II aldolase
8.62
-
class I aldolase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
-
class I aldolase
7 - 7.5
-
class II aldolase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
class I and class II aldolase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakahara, K.; Yamamoto, H.; Miyake, C.; Yokota, A.
Purification and characterization of class-I and class-II fructose-1,6-bisphosphate aldolases from the cyanobacterium Synechocystis sp. PCC 6803
Plant Cell Physiol.
44
326-333
2003
Synechocystis sp.
Manually annotated by BRENDA team