Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Escherichia coli and UniProt Accession P0AB71

for references in articles please use BRENDA:EC4.1.2.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0AB71
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
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
D-fructose-6-phosphate aldolase
-
FBP-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 aldolase
-
-
Fructose-1,6-bisphosphate triosephosphate-lyase
-
-
-
-
IgE-binding allergen
-
-
-
-
ketose 1-phosphate aldolase
-
-
-
-
Liver-type aldolase
-
-
-
-
Muscle-type aldolase
-
-
-
-
Phosphofructoaldolase
-
-
-
-
SMALDO
-
-
-
-
zymohexase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism of class II aldolase
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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 6-phosphate
D-glyceraldehyde 3-phosphate + dihydroxypropanone
show the reaction diagram
-
-
-
r
L-glyceraldehyde 3-phosphate + butanone
(2S,3S)-2,3-dihydroxy-5-oxoheptyl phosphate
show the reaction diagram
-
-
-
?
L-glyceraldehyde 3-phosphate + cyclopentane
(2S,3S)-2,3-dihydroxy-3-(2-oxocyclopentyl)propylphosphate
show the reaction diagram
-
-
-
?
L-glyceraldehyde 3-phosphate + ethanol
2-deoxy-5-O-phosphono-L-threo-pentose
show the reaction diagram
-
-
-
?
L-glyceraldehyde 3-phosphate + propanone
1,3-dideoxy-6-O-phosphono-L-threo-hex-2-ulose
show the reaction diagram
-
-
-
?
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
dihydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
i.e. (S)-N-Cbz-alaninal,substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-mannitol
-
?
dihydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
i.e. (S)-N-Cbz-alaninal, substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-glucitol
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
show the reaction diagram
-
-
-
?
hydroxyacetone + phenoxyacetaldehyde
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (2-oxoethyl)carbamate
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (3-oxopropyl)carbamate
?
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
show the reaction diagram
-
substrate only for mutant A129S/A165G
-
-
?
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
-
-
?
D-fructose 6-phosphate
D-glyceraldehyde 3-phosphate + dihydroxypropanone
show the reaction diagram
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
can partially restore activity of metal depleted enzyme
K+
-
no effect
Mn2+
-
can partially restore activity of metal depleted enzyme
Zn2+
-
the function appears to be the polarization of the C=O bound of glycerone phosphate. Each subunit of the dimer binds one Zn2+
additional information
-
metalloaldolase class II, a divalent metal ion is an integral and essential component of the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dihydroxyacetone phosphate
-
glyceraldehyde 3-phosphate
non-competitive inhibitor
2-oxo-2-[(phenylsulfonyl)amino]ethyl phosphate
-
-
2-[(methylsulfonyl)amino]-2-oxoethyl phosphate
-
-
3-phosphoglycerate
-
-
diphosphate
-
-
glyceraldehyde 3-phosphate
-
-
glycerone phosphate
-
-
Ni2+
-
cells stressed by 8 microM Ni(II) for 20 min lose 75% of their FbaA activity. In presence of 8 microM Ni(II), purified FbaA loses 80% of its activity within 2 min. Inhibition is due to Ni(II) binding to a secondary zinc binding site
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
Polyphosphate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
citrate
-
enhances activity
phosphoenolpyruvate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
sn-glycerol 3-phosphate
-
enhances D-fructose 1,6-bisphosphate-cleavage activity, fructose 1-phosphate-cleavage activity is unaffected
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 1.07
D-fructose 1,6-bisphosphate
0.02 - 2.7
D-fructose 1,6-bisphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 14.2
D-fructose 1,6-bisphosphate
0.013 - 10.5
D-fructose 1,6-bisphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 1.7
dihydroxyacetone phosphate
0.1
2-oxo-2-[(phenylsulfonyl)amino]ethyl phosphate
-
-
0.35
2-[(methylsulfonyl)amino]-2-oxoethyl phosphate
-
-
0.00001
phosphoglycolo hydroxamic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 9.3
-
pH 7.7: about 40% of maximal activity, pH 9.3: about 95% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
gel filtration
340000
-
ultracentrifugal analysis
78000
-
ultracentrifugal analysis
80000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
class II aldolase in complex with phosphoglycolohydroxamate
crystals of recombinant fructose-1,6-bisphosphate aldolase class I are obtained by the sitting-drop vapour-diffusion technique in a condition consisting of 19 mg/ml FBPA I in 0.1 M Tris pH 9.0, 10% (w/v) polyethylene glycol 8000 and diffract to 2.0 A resolution. The crystals belong to the monoclinic space group C2, with unit-cell parameters 217.7 A (a), 114.9 A (b), 183.9 A (c), 124.6° (beta)
-
sitting drop vapor diffusion method, using 0.1 M Tris pH 9.0, 10% (w/v) polyethylene glycol 8000
-
with Cd2+ in place of Zn2+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D109A
very low catalytic activity
D144A
increased Km
D288A
increased Km
D290A
increased Km
D329A
increased Km
N286A
increased Km, decreased kcat
N286D
increased Km, severely decreased kcat
A129S/A165G
-
activity is between 5- to more than 900fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives
D144A
-
residue is involved in ligating the secondary zinc atom. Mutant exhibits enhancement of enzymatic activity by added nickel
E174A
E181A
-
mutant enzyme has wild-type properties
E182A
-
decrease in kcat
K325A
-
decreased kcat
N35A
-
1.56% activity of the wild-type enzyme
Q59A
-
no significant effect on enzyme function
S61A
-
increased Km for fructose 1,6-bisphosphate
S61T
-
no effect on catalysis
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
50% loss of activity after incubation for 10 min at 50.5°C
25
-
3 d, 25% loss of activity
55
-
12 h, enzyme retains almost 100% activity
55 - 70
-
the enzyme retains almost 100% activity after incubation at 55°C for 12 h, while enzyme activity is about 10% after incubation at 70°C for 12
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, stable for up to 12 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
class II enzyme
-
HisTrap column chromatography and Superdex 75 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morse, D.E.; Horecker, B.L.
The mechanism of action of aldolases
Adv. Enzymol. Relat. Areas Mol. Biol.
31
125-181
1968
Anacystis sp., Aspergillus sp., Bacillus sp. (in: Bacteria), Brucella sp., Candida sp. (in: Saccharomycetales), Chlamydomonas sp., Clostridium sp., Corynebacterium sp., Oryctolagus cuniculus, Escherichia coli, Erwinia sp., Euglena sp., Penicillium sp., Lactobacillus sp., Mycobacterium sp., Pseudomonas sp., Saccharomyces sp., Veillonella sp.
Manually annotated by BRENDA team
Baldwin, S.A.; Perham, R.N.; Stribling, D.
Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)
Biochem. J.
169
633-641
1978
Escherichia coli, Escherichia coli Crookes
Manually annotated by BRENDA team
Baldwin, S.A.; Perham, R.N.
Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)
Biochem. J.
169
643-652
1978
Escherichia coli, Escherichia coli Crookes
Manually annotated by BRENDA team
Szwergold, B.S.; Ugurbil, K.; Brown, T.R.
Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis
Arch. Biochem. Biophys.
317
244-252
1995
Escherichia coli
Manually annotated by BRENDA team
Hall, D.R.; Leonard, G.A.; Reed, C.D.; Watt, C.I.; Berry, A.; Hunter, W.N.
The crystal structure of Escherichia coli class II fructose-1,6-bisphosphate aldolase in complex with phosphoglycolohydroxamate reveals details of mechanism and specificity
J. Mol. Biol.
287
383-394
1999
Escherichia coli (P0AB71), Escherichia coli
Manually annotated by BRENDA team
Hall, D.R.; Kemp, L.E.; Leonard, G.A.; Marshall, K.; Berry, A.; Hunter, W.N.
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase
Acta Crystallogr. Sect. D
59
611-614
2003
Escherichia coli
Manually annotated by BRENDA team
Zgiby, S.M.; Thomson, G.J.; Qamar, S.; Berry, A.
Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases
Eur. J. Biochem.
267
1858-1868
2000
Escherichia coli
Manually annotated by BRENDA team
Plater, A.R.; Zgiby, S.M.; Thomson, G.J.; Qamar, S.; Wharton, C.W.; Berry, A.
Conserved residues in the mechanism of the E. coli Class II FBP-aldolase
J. Mol. Biol.
285
843-855
1999
Escherichia coli (P0AB71), Escherichia coli
Manually annotated by BRENDA team
Zgiby, S.; Plater, A.R.; Bates, M.A.; Thomson, G.J.; Berry, A.
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli
J. Mol. Biol.
315
131-140
2002
Escherichia coli
Manually annotated by BRENDA team
Gavalda, S.; Braga, R.; Dax, C.; Vigroux, A.; Blonski, C.
N-Sulfonyl hydroxamate derivatives as inhibitors of class II fructose-1,6-diphosphate aldolase
Bioorg. Med. Chem.
15
5375-5377
2005
Oryctolagus cuniculus, Escherichia coli
Manually annotated by BRENDA team
Hao, J.; Berry, A.
A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
Protein Eng. Des. Sel.
17
689-697
2004
Edwardsiella ictaluri, Escherichia coli (P0AB71), Escherichia coli
Manually annotated by BRENDA team
Gutierrez, M.; Parella, T.; Joglar, J.; Bujons J.; Claps P.
Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation
Chem. Commun. (Camb. )
47
5762-5764
2011
Escherichia coli
Manually annotated by BRENDA team
Macomber, L.; Elsey, S.P.; Hausinger, R.P.
Fructose-1,6-bisphosphate aldolase (class II) is the primary site of nickel toxicity in Escherichia coli
Mol. Microbiol.
82
1291-1300
2011
Escherichia coli
Manually annotated by BRENDA team
Zhang, L.; Guo, Z.; Huang, J.; Liu, M.; Wang, Y.; Ji, C.
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of fructose-1,6-bisphosphate aldolase from Escherichia coli
Acta Crystallogr. Sect. F
70
1376-1379
2014
Escherichia coli
Manually annotated by BRENDA team
Roldan, R.; Sanchez-Moreno, I.; Scheidt, T.; Helaine, V.; Lemaire, M.; Parella, T.; Clapes, P.; Fessner, W.D.; Guerard-Helaine, C.
Breaking the dogma of aldolase specificity simple aliphatic ketones and aldehydes are nucleophiles for fructose-6-phosphate aldolase
Chemistry
23
5005-5009
2017
Escherichia coli (P0AB71)
Manually annotated by BRENDA team
Zhang, L.; Guo, Z.; Huang, J.; Liu, M.; Wang, Y.; Ji, C.
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of fructose-1,6-bisphosphate aldolase from Escherichia coli
Acta Crystallogr. F Struct. Biol. Commun.
70
1376-1379
2014
Escherichia coli
Manually annotated by BRENDA team