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Information on EC 4.1.2.40 - tagatose-bisphosphate aldolase
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EC Tree
4.1.2.40 tagatose-bisphosphate aldolaseIUBMB Comments
Enzyme activity is stimulated by certain divalent cations. It is involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.
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Word Map
- 4.1.2.40
- streptococcus
- aldolases
- pyogenes
- 6-phosphate
- lactis
- lactococcus
-
phosphotransferase
- phosphoglycolohydroxamate
-
fbpas
-
phosphoenolpyruvate-dependent
-
diastereoisomers
- galactitol
- speb
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
lacd.1, tagatose-1,6-bisphosphate aldolase, tagatose-1,6-diphosphate aldolase, d-tagatose-1,6-bisphosphate aldolase, tagatose 1,6-bisphosphate aldolase, tdp aldolase, tagatose-bisphosphate aldolase, tbp aldolase, tagatose bisphosphate aldolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldolase, tagatose 1,6-diphosphate
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-
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D-Tagatose 1,6-diphosphate aldolase
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-
-
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D-tagatose-1,6-bisphosphate aldolase
D-Tagatose-1,6-bisphosphate aldolase (class I)
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-
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D-Tagatose-1,6-bisphosphate aldolase (class II)
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-
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LacD.1
Tagatose 1,6-bisphosphate aldolase
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Tagatose bisphosphate aldolase
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tagatose-1,6-bisphosphate aldolase
Tagatose-1,6-diphosphate aldolase
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Tagatose-bisphosphate aldolase
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-
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TBP aldolase
TDP aldolase
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D-tagatose-1,6-bisphosphate aldolase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
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D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
mechanism
-
D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
kinetics
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
reversal of an aldol condensation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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.
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CAS REGISTRY NUMBER
COMMENTARY
39433-95-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-tagatose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Fructose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Psicose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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no activity
-
-
?
D-Psicose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Sorbose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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no activity
-
-
?
D-Sorbose 1,6-diphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-tagatose 1,6-diphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-tagatose 1,6-diphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
enzyme functions in catabolism of galactitol, inducible enzyme
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
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-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
r
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
in the reverse reaction only the diphosphates of tagatose and fructose are detected
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?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
-
in the reverse reaction the 1,6-diphosphates of all four D-2-oxohexoses are formed
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-
?
D-Tagatose-1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde 3-phosphate
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-
-
-
?
additional information
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
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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
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
-
no activity with D-fructose 1-phosphate or L-sorbose 1-phosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Tagatose-1,6-bisphosphate
?
-
enzyme functions in catabolism of galactitol, inducible enzyme
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
induced by growth on either lactose or galactose
-
-
?
D-Tagatose-1,6-bisphosphate
?
-
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
?
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
additional information
?
-
-
involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Distinct time-resolved roles for two catabolite-sensing pathways during Streptococcus pyogenes infection.
Soft Tissue Infections
CcpA and LacD.1 Affect Temporal Regulation of S. pyogenes Virulence Genes.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.293
D-fructose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
0.498
D-fructose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
1.993
D-fructose 1,6-diphosphate
-
isoform LacD.2, pH 7.5, temperature not specified in the publication
0.183
D-tagatose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
0.199
D-tagatose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
0.92
D-tagatose 1,6-diphosphate
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isoform LacD.2, pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.41
D-fructose 1,6-diphosphate
-
isoform LacD.2, pH 7.5, temperature not specified in the publication
6.35
D-fructose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
12.6
D-fructose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
14.6
D-tagatose 1,6-diphosphate
-
isoform LacD.2, pH 7.5, temperature not specified in the publication
18.3
D-tagatose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
24.3
D-tagatose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
D-fructose 1,6-diphosphate
-
isoform LacD.2, pH 7.5, temperature not specified in the publication
12.8
D-fructose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
42.9
D-fructose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
16
D-tagatose 1,6-diphosphate
-
isoform LacD.2, pH 7.5, temperature not specified in the publication
100
D-tagatose 1,6-diphosphate
-
mutant isoform LacD.1, C-terminal half replaced with 162 amino acid residues from the C-terminus of LacD.2, pH 7.5, temperature not specified in the publication
122
D-tagatose 1,6-diphosphate
-
isoform LacD.1, pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.3
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with tagatose 1,6-diphosphate or fructose 1,6-diphosphate as substrate
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pH RANGE
ORGANISM
UNIPROT
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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (6549 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
K204A
-
mutation results in more than 98% decrease in aldolase activity
additional information
additional information
-
construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1
additional information
-
construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1
-
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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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography, HiTrap-Q column chromatography, and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, R.L.; Markwell, J.P.
D-Tagatose-1,6-bisphosphate aldolase (class II) from Klebsiella pneumoniae
Methods Enzymol.
90
232-234
1982
Klebsiella pneumoniae
brenda
Anderson, R.L.; Bissett, D.L.
D-Tagatose-1,6-bisphosphate aldolase (class I) from Staphylococcus aureus
Methods Enzymol.
90
228-232
1982
Staphylococcus aureus