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Information on EC 1.1.1.251 - galactitol-1-phosphate 5-dehydrogenase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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galactitol-1-phosphate 5-dehydrogenase
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galactitol-1-phosphate + NAD+ = L-tagatose 6-phosphate + NADH + H+
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degradation of sugar alcohols
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galactitol degradation
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galactitol-1-phosphate:NAD+ oxidoreductase
The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
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galactitol-1-phosphate dehydrogenase (Escherichia coli strain EC3132 gene gatD)
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Gat1P-specific NAD-dependent dehydrogenase
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Genbank X79837-derived protein
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NAD-dependent Gat1P-dehydrogenase
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GatD
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UniProt
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UniProt
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strain EC3132
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K12 JWL194BN
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UniProt
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K12 JWL194BN
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strain EC3132
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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enzyme is involved in the galactitol metabolism
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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enzyme is involved in the galactitol metabolism
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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enzyme is involved in the galactitol metabolism
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Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
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enzyme is involved in the galactitol metabolism
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Zn2+
structure shows a pentacoordinated zinc ion in complex with a polyol
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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37422
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x * 37422, calculation from nucleotide sequence
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x * 37422, calculation from nucleotide sequence
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x * 37422, calculation from nucleotide sequence
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x * 37422, calculation from nucleotide sequence
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modeling of structure and docking analysis of substrate, Zn2+ and NAD+. Cys 37, His 58, Glu 59, Glu 142 residues form an active site pocket similar to known GPDH. A catalytic Zn2+-binding domain and a cofactor NAD+-binding domain with strong hydrogen bonding contacts with the substrate and the cofactor are identified
structures of open state with Zn2+ in the catalytic site and of the closed state in complex with the polyols Tris and glycerol, respectively. The closed state reveals no bound cofactor. The glycerol binding mode reveals a pentacoordinated zinc ion in complex with a polyol and also a strong hydrogen bond between the primary hydroxyl group and the conserved Glu144
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gat genes isolated from the wild-type isolate Escherichia coli EC3132 and cloned on a 7.8-kbp PstI DNA fragment, catD codes for EC 1.1.1.251
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Nobelmann, B.; Lengeler, J.W.
Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli
Biochim. Biophys. Acta
1262
69-72
1995
Escherichia coli, Escherichia coli EC3132
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Nobelmann, B.; Lengeler, J.W.
Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism
J. Bacteriol.
178
6790-6795
1996
Escherichia coli, Escherichia coli K12 JWL194BN
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Benavente, R.; Esteban-Torres, M.; Kohring, G.W.; Cortes-Cabrera, A.; Sanchez-Murcia, P.A.; Gago, F.; Acebron, I.; de las Rivas, B.; Munoz, R.; Mancheno, J.M.
Enantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coli
Acta Crystallogr. Sect. D
71
1540-1554
2015
Escherichia coli, Escherichia coli (P0A9S3)
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Razali, S.; Sarah Diana, P.; Shamsir, M.; Mahadi, N.; Mohd Illias, R.
Substrate and cofactor binding interaction studies of galactitol-1-phosphate 5-dehydrogenase from Peptoclostridium difficile
J. Teknol.
78
199-210
2016
Clostridioides difficile (A0A0H3N4Z0), Clostridioides difficile CD196 (A0A0H3N4Z0)
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