We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 1.1.1.251 - galactitol-1-phosphate 5-dehydrogenase for references in articles please use BRENDA:EC1.1.1.251
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments The enzyme from the bacterium Escherichia coli is involved in a galactitol degradation pathway. It contains two zinc atoms per subunit.
The enzyme appears in viruses and cellular organisms
Synonyms
galactitol-1-phosphate dehydrogenase (Escherichia coli strain EC3132 gene gatD), Gat1P-specific NAD-dependent dehydrogenase, GatD, Genbank X79837-derived protein, GPDH, NAD-dependent Gat1P-dehydrogenase,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
galactitol-1-phosphate dehydrogenase (Escherichia coli strain EC3132 gene gatD)
-
-
-
-
Gat1P-specific NAD-dependent dehydrogenase
-
-
-
-
Genbank X79837-derived protein
-
-
-
-
NAD-dependent Gat1P-dehydrogenase
-
-
-
-
GatD
A0A0H3N4Z0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
galactitol 1-phosphate + NAD+ = D-tagatose 6-phosphate + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
enzyme is involved in the galactitol metabolism
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
enzyme is involved in the galactitol metabolism
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
enzyme is involved in the galactitol metabolism
-
-
-
Galactitol-1-phosphate + NAD+
L-Tagatose 6-phosphate + NADH
-
enzyme is involved in the galactitol metabolism
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
structure shows a pentacoordinated zinc ion in complex with a polyol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
A0A0H3N4Z0
UniProt
brenda
-
A0A0H3N4Z0
UniProt
brenda
-
-
-
brenda
K12 JWL194BN
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
K12 JWL194BN
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37422
-
x * 37422, calculation from nucleotide sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 37422, calculation from nucleotide sequence
?
-
x * 37422, calculation from nucleotide sequence
-
?
-
x * 37422, calculation from nucleotide sequence
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
A0A0H3N4Z0
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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)
brenda
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)
-
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.1.1.251 galactitol-1-phosphate 5-dehydrogenase
more
top
Information
