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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Spinacia oleracea and UniProt Accession P16096

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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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This record set is specific for:
Spinacia oleracea
UNIPROT: P16096
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The taxonomic range for the selected organisms is: Spinacia oleracea
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 bisphosphate aldolase
-
1,6-Diphosphofructose aldolase
-
-
-
-
37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
aldolase
-
-
-
-
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
-
Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
-
-
-
-
FBP aldolase
-
-
-
-
Fru-P2A
-
-
-
-
Fructoaldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
-
-
-
-
Fructose 1,6-diphosphate aldolase
-
-
-
-
Fructose 1-monophosphate aldolase
-
-
-
-
Fructose 1-phosphate aldolase
-
-
-
-
Fructose bisphosphate aldolase
-
-
-
-
Fructose diphosphate aldolase
-
-
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Liver-type aldolase
-
-
-
-
Muscle-type aldolase
-
-
-
-
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
-
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
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
class I fructose diphosphate aldolases, Schiff-base forming, does not require a metal ion
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
1.7 - 2.3
fructose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.18
-
cytosolic enzyme
7.8
-
chloroplastic enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
ALFC_SPIOL
394
0
42468
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
determination of sedimentation velocity
143000
-
cytosolic enzyme, sucrose density gradient centrifugation
148000
-
chloroplastic enzyme, method of Martin and Ames
30000
-
4 * 30000
35000
-
4 * 35000, chloroplastic enzyme, SDS-PAGE
38000
40000
-
x * 40000, cytosolic isoenzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
chloroplastic enzyme, half-life: 3 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme does not refold into an enzymatically active conformation following denaturation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Horecker, B.L.
Fructose bisphosphate aldolase from spinach
Methods Enzymol.
42C
234-239
1975
Spinacia oleracea
-
Manually annotated by BRENDA team
Krueger, I.; Schnarrenberger, C.
Purification, subunit structure and immunological comparison of fructose-bisphosphate aldolases from spinach and corn leaves
Eur. J. Biochem.
136
101-106
1983
Spinacia oleracea, Zea mays
Manually annotated by BRENDA team
Lebherz, H.G.; Leadbetter, M.M.; Bradshaw, R.A.
Isolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase
J. Biol. Chem.
259
1011-1017
1984
Spinacia oleracea
Manually annotated by BRENDA team
Schnarrenberger, C.; Kruger, I.
Distinction between cytosol and chloroplast fructose-bisphosphate aldolases from pea, wheat, and corn leaves
Plant Physiol.
80
301-304
1986
Pisum sativum, Spinacia oleracea, Triticum aestivum, Zea mays
Manually annotated by BRENDA team
Gehring, A.G.; Ezzell, J.L.; Lebherz, H.G.
A selective reaction of fructose bisphosphate aldolase with fluorescein isothiocyanate in chicken muscle extracts
J. Mol. Recognit.
21
137-147
2008
Gallus gallus, Gallus gallus (P53449), Homarus americanus, Lithobates pipiens, Squalus acanthias, Crotalus oreganus helleri, Morone saxatilis, Triticum aestivum (C1J959), Spinacia oleracea (P16096)
Manually annotated by BRENDA team