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
4.1.2.40
-
RECOMMENDED NAME
GeneOntology No.
tagatose-bisphosphate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-tagatose 1,6-bisphosphate = 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
kinetics
-
D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
reversal of an aldol condensation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
D-galactosamine and N-acetyl-D-galactosamine degradation
-
galactitol degradation
-
Galactose metabolism
-
lactose and galactose degradation I
-
Metabolic pathways
-
N-acetyl-D-galactosamine degradation
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldolase, tagatose 1,6-diphosphate
-
-
-
-
D-Tagatose 1,6-diphosphate aldolase
-
-
-
-
D-tagatose-1,6-bisphosphate aldolase
-
-
-
-
D-tagatose-1,6-bisphosphate aldolase
-
-
D-Tagatose-1,6-bisphosphate aldolase (class I)
-
-
-
-
D-Tagatose-1,6-bisphosphate aldolase (class II)
-
-
-
-
LacD
Q5HE13
a class I tagatose-1,6-bisphosphate aldolase
Tagatose 1,6-bisphosphate aldolase
-
-
-
-
Tagatose bisphosphate aldolase
-
-
-
-
tagatose-1,6-biphosphate aldolase 2
-
-
tagatose-1,6-bisphosphate aldolase
-
-
tagatose-1,6-bisphosphate aldolase
Q5HE13
-
tagatose-1,6-bisphosphate aldolase
-
-
Tagatose-1,6-diphosphate aldolase
-
-
-
-
Tagatose-bisphosphate aldolase
-
-
-
-
TBP aldolase
-
-
TBP aldolase
Q5HE13
-
TBP aldolase
-
-
TDP aldolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
39433-95-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
two enzymes
-
-
Manually annotated by BRENDA team
two enzymes
UniProt
Manually annotated by BRENDA team
two enzymes
-
-
Manually annotated by BRENDA team
strain C10
-
-
Manually annotated by BRENDA team
subsp. lactis MG1820
-
-
Manually annotated by BRENDA team
Lactococcus lactis C10
strain C10
-
-
Manually annotated by BRENDA team
Lactococcus lactis subsp. cremoris E8
strain E8
-
-
Manually annotated by BRENDA team
two enzymes
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Lactococcus lactis, Lactococcus lactis subsp. cremoris, Lactococcus lactis C10, Lactococcus lactis subsp. cremoris E8
-
-
-
-
-
D-Psicose 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
-
no activity
-
-
-
D-Sorbose 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
-
no activity
-
-
-
D-tagatose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q5HE13
-
-
-
?
D-Tagatose-1,6-bisphosphate
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
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
P0AB74
-
-
-
?
D-Tagatose-1,6-bisphosphate
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
-
-
-
-
-
D-Tagatose-1,6-bisphosphate
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
-
-
-
?
D-Tagatose-1,6-bisphosphate
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
Q8VS16
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
r, in the reverse reaction only the diphosphates of tagatose and fructose are detected
-
-
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
in the reverse reaction the 1,6-diphosphates of all four D-2-oxohexoses are formed
-
-
-
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Lactococcus lactis C10, Lactococcus lactis subsp. cremoris E8
-
-
-
-
-
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
-
induced by growth on either lactose or galactose
-
-
-
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
-
enzyme functions in catabolism of galactitol, inducible enzyme
-
-
-
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
Lactococcus lactis C10, Lactococcus lactis subsp. cremoris E8
-
induced by growth on either lactose or galactose
-
-
-
additional information
?
-
-
no activity with D-fructose 1-phosphate or L-sorbose 1-phosphate
-
-
-
additional information
?
-
-
no activity with D-fructose 1-phosphate or L-sorbose 1-phosphate
-
-
-
additional information
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
Q8VS16
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
-
induced by growth on either lactose or galactose
-
-
-
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
-
enzyme functions in catabolism of galactitol, inducible enzyme
-
-
-
D-Tagatose-1,6-bisphosphate
?
show the reaction diagram
Lactococcus lactis C10, Lactococcus lactis subsp. cremoris E8
-
induced by growth on either lactose or galactose
-
-
-
additional information
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
Q8VS16
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CdSO4
-
activates
CoCl2
-
activates
KCl
-
activates
NaCl
-
activates
NH4Cl
-
activates
MnCl2
-
activates
additional information
-
no divalent metal ion required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
no inhibition
NaBH4
-
no inhibition
NaBH4
-
substrate-dependent inactivation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.5
-
D-fructose 1,6-diphosphate
-
-
0.4
-
D-tagatose 1,6-diphosphate
-
-
1.5
-
D-tagatose 1,6-diphosphate
-
-
0.25
-
fructose 1,6-diphosphate
-
-
0.1
-
tagatose 1,6-diphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.3
-
with tagatose 1,6-diphosphate or fructose 1,6-diphosphate as substrate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.6
7.6
-
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
-
-
gel filtration
157000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 36476, calculation from nucleotide sequence
dimer
-
gel filtration
dimer
Q5HE13
x-ray crystallography
monomer
-
1 * 37000
tetramer
-
crystallographic data
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with phosphoglycolohydroxamate
-
sitting drop vapor diffusion method; sitting drop vapor diffusion method, using
Q5HE13
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
-
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
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native protein crystals can be stored for several months without degradation, crystals of the selenomethionine enzyme are degraded within a few weeks
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, 20 mM sodium phosphate buffer, pH 7.5, 10% v/v glycerol, stable for 3 months
-
-20°C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nickel affinity column chromatography, HiTrap-Q column chromatography, and Superdex 200 gel filtration
Q5HE13
by anion-exchange chromatography and gel filtration, to homogeneity
-
nickel affinity resin column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli Rosetta2(DE3) cells
Q5HE13
expressed in Escherichia coli BL21(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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L165E
Q5HE13
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L165E/L275S
Q5HE13
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
L275S
Q5HE13
the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate
K124A
-
strongly reduced aldolase activity
K204A
-
mutation results in more than 98% decrease in aldolase activity
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
use in measuring intracellular tagatose 1,6-diphosphate
analysis
Lactococcus lactis subsp. cremoris E8
-
use in measuring intracellular tagatose 1,6-diphosphate
-