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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P14540

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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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Saccharomyces cerevisiae
UNIPROT: P14540
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
class II aldolase
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class II fructose bisphosphate aldolase
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fructose bis-phosphate 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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-
-
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41 kDa antigen
-
-
-
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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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CE2
-
-
-
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Diphosphofructose aldolase
-
-
-
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FBP aldolase
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-
-
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Fru-P2A
-
-
-
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Fructoaldolase
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-
-
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Fructose 1,6-bisphosphate aldolase
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-
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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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-
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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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-
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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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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
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
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
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucitol 1,6-bisphosphate
competitive inhibitor, better inhibitor
D-mannitol 1,6-bisphosphate
competitive inhibitor
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
phosphoglycolo hydroxamic acid
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PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycolo-amidoxime
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PGA, i.e. 2-amino-2-(hydroxyimino)ethyl phosphate
phosphoglycolo-hydrazide
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PGHz, i.e. 2-hydrazino-2-oxoethyl phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
D-fructose 1,6-bisphosphate
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0.45
D-fructose-1,6-bisphosphate
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0.055
D-fructose 1,6-bisphosphate
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
D-glucitol 1,6-bisphosphate
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0.4
D-mannitol 1,6-bisphosphate
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0.00001
phosphoglycolo hydroxamic acid
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-
0.0023
phosphoglycolo-amidoxime
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-
0.00034
phosphoglycolo-hydrazide
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the overproduction of fructose bisphosphate aldolase Fba1 enables overcoming of a severe growth defect caused by a missense mutation rpc128-1007 in a gene encoding the C128 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fba1 is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. Overproduction of an inactive aldolase mutant still suppresses the rpc128-1007 phenotype, and Fba1 interacts with the RNA polymerase III complex and plays a role in control of tRNA transcription
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
inhibitors of class II Fba can be potential drugs against microorganisms
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fonvielle, M.; Weber, P.; Dabkowska, K.; Therisod, M.
New highly selective inhibitors of class II fructose-1,6-bisphosphate aldolases
Bioorg. Med. Chem. Lett.
14
2923-2926
2004
Bacillus subtilis, Saccharomyces cerevisiae, Oryctolagus cuniculus
Manually annotated by BRENDA team
Mabiala-Bassiloua, C.G.; Zwolinska, M.; Therisod, H.; Sygusch, J.; Therisod, M.
Separate synthesis and evaluation of D-glucitol 1,6-bisphosphate and mannitol bis-phosphate, as competitive inhibitors of fructose bis-phosphate aldolases
Bioorg. Med. Chem. Lett.
18
1735-1737
2008
Oryctolagus cuniculus (P00883), Saccharomyces cerevisiae (P14540), Helicobacter pylori (P56109)
Manually annotated by BRENDA team
Fonvielle, M.; Coincon, M.; Daher, R.; Desbenoit, N.; Kosieradzka, K.; Barilone, N.; Gicquel, B.; Sygusch, J.; Jackson, M.; Therisod, M.
Synthesis and biochemical evaluation of selective inhibitors of class II fructose bisphosphate aldolases: towards new synthetic antibiotics
Chemistry
14
8521-8529
2008
Oryctolagus cuniculus (P00883), Saccharomyces cerevisiae (P14540), Helicobacter pylori (P56109), Mycobacterium tuberculosis (P9WQA3), Mycobacterium tuberculosis H37Rv (P9WQA3)
Manually annotated by BRENDA team
Ciesla, M.; Mierzejewska, J.; Adamczyk, M.; Farrants, A.K.; Boguta, M.
Fructose bisphosphate aldolase is involved in the control of RNA polymerase III-directed transcription
Biochim. Biophys. Acta
1843
1103-1110
2014
Saccharomyces cerevisiae
Manually annotated by BRENDA team