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Information on EC 4.1.2.40 - tagatose-bisphosphate aldolase and Organism(s) Escherichia coli and UniProt Accession P0AB74

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.40 tagatose-bisphosphate aldolase
IUBMB 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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This record set is specific for:
Escherichia coli
UNIPROT: P0AB74
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
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, tagatose-bisphosphate aldolase, tbp aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tagatose-1,6-bisphosphate aldolase
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TBP aldolase
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aldolase, tagatose 1,6-diphosphate
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D-Tagatose 1,6-diphosphate aldolase
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D-tagatose-1,6-bisphosphate aldolase
D-Tagatose-1,6-bisphosphate aldolase (class I)
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D-Tagatose-1,6-bisphosphate aldolase (class II)
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Tagatose 1,6-bisphosphate aldolase
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Tagatose bisphosphate aldolase
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Tagatose-1,6-diphosphate aldolase
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Tagatose-bisphosphate aldolase
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TDP aldolase
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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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PATHWAY SOURCE
PATHWAYS
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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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SUBSTRATE
PRODUCT                       
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
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
additional information
?
-
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involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
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?
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
additional information
?
-
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involved in catabolism of galactitol and of N-acetyl-galactosamine and D-galactosamine
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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crystallographic data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with phosphoglycolohydroxamate
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brinkkotter, A.; Shakeri-Garakani, A.; Lengeler, J.W.
Two class II D-tagatose-bisphosphate aldolases from enteric bacteria
Arch. Microbiol.
177
410-419
2002
Escherichia coli, Klebsiella oxytoca (Q8VS16), Klebsiella pneumoniae, Salmonella enterica
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
Hall, D.R.; Bond, C.S.; Leonard, G.A.; Watt, C.I.; Berry, A.; Hunter, W.N.
Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases
J. Biol. Chem.
277
22018-22024
2002
Escherichia coli
Manually annotated by BRENDA team
Lee, J.H.; Bae, J.; Kim, D.; Choi, Y.; Im, Y.J.; Koh, S.; Kim, J.S.; Kim, M.K.; Kang, G.B.; Hong, S.I.; Lee, D.S.; Eom, S.H.
Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus
Biochem. Biophys. Res. Commun.
347
616-625
2006
Escherichia coli (P0AB74)
Manually annotated by BRENDA team
Rinas, U.; Hoffmann, F.; Betiku, E.; Estape, D.; Marten, S.
Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
J. Biotechnol.
127
244-257
2007
Escherichia coli
Manually annotated by BRENDA team