Information on EC 4.1.2.40 - tagatose-bisphosphate aldolase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.2.40
-
RECOMMENDED NAME
GeneOntology No.
tagatose-bisphosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
reversal of an aldol condensation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactosamine and N-acetyl-D-galactosamine degradation
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degradation of sugar alcohols
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galactitol degradation
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Galactose metabolism
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lactose and galactose degradation I
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Metabolic pathways
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metabolism of disaccharids
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N-acetyl-D-galactosamine degradation
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SYSTEMATIC NAME
IUBMB Comments
D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Enzyme activity is stimulated by certain divalent cations. It is involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
39433-95-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two enzymes
UniProt
Manually annotated by BRENDA team
strain C10
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-
Manually annotated by BRENDA team
strain E8
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-
Manually annotated by BRENDA team
two enzymes
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-
Manually annotated by BRENDA team
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S5ELN7
UniProt
Manually annotated by BRENDA team
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-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-Psicose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-Sorbose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-tagatose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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-
-
?
D-tagatose 1,6-diphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CdSO4
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activates
CoCl2
-
activates
KCl
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activates
MnCl2
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activates
NaCl
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activates
NH4Cl
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activates
additional information
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no divalent metal ion required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.293 - 2.5
D-fructose 1,6-diphosphate
0.183 - 1.5
D-tagatose 1,6-diphosphate
0.25
fructose 1,6-diphosphate
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0.1
tagatose 1,6-diphosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.41 - 12.6
D-fructose 1,6-diphosphate
14.6 - 24.3
D-tagatose 1,6-diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1 - 42.9
D-fructose 1,6-diphosphate
16 - 122
D-tagatose 1,6-diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
S5ELN7
isoforms LacD.1 and LacD2
7 - 7.3
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with tagatose 1,6-diphosphate or fructose 1,6-diphosphate as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 7.6
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85% of maximal activity at pH 6.6 and at pH 7.6, with tagatose 1,6-diphosphate or fructose 1,6-diphosphate as substrate
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
S5ELN7
gel filtration, isoform LacD.1
70000
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gel filtration
71000
S5ELN7
gel filtration, isoform LacD.2
157000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 36476, calculation from nucleotide sequence
monomer
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1 * 37000
tetramer
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crystallographic data
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with phosphoglycolohydroxamate
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sitting drop vapor diffusion method; sitting drop vapor diffusion method, using
native enzyme and native enzyme in complex with dihydroxyacetone-P, by the hanging drop method. Native free TBP aldolase crystallized in the P212121 space group with four protomers in the asymmetric unit and diffracted to 1.87 A resolution. Folding of the polypeptide chain of TBP aldolase corresponds to a (alpha/beta)8 or TIM barrel fold. The liganded crystal structure is isomorphous with the crystal structure of the native aldolase and diffracted to 1.92 A resolution
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recombinant, orthorhombic crystals suitable for structural analysis are obtained by the hanging-drop vapour-diffusion method for the native enzyme and the selenomethionine derivative. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 63.7, b = 108.1, c = 238.7 A for the native form and a = 64.1, b = 108.3, c = 239.8 A for the selenomethionine derivative. The asymmetric unit contains four protomers
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
native protein crystals can be stored for several months without degradation, crystals of the selenomethionine enzyme are degraded within a few weeks
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM sodium phosphate buffer, pH 7.5, 10% v/v glycerol, stable for 3 months
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-20°C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by anion-exchange chromatography and gel filtration, to homogeneity
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nickel affinity column chromatography, HiTrap-Q column chromatography, and Superdex 200 gel filtration
nickel affinity resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli Rosetta2(DE3) cells
plasmid pKK-223-3 with T7 IPTG-inducible promoter and coding for the lacD2 gene product tagatose-1-6-biphosphate aldolase 2 transformed and overexpressed using the Escherichia coli JM109 strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L165E
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L165E/L275S
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L275S
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
K124A
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strongly reduced aldolase activity
K204A
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mutation results in more than 98% decrease in aldolase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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