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ADP-D-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
based on Vmax/Km values, the enzyme is about 20fold more active toward ADP-D-ribose as compared to UDP-D-glucose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
AMP + H2O
adenosine + phosphate
ATP + H2O
ADP + phosphate
-
ATP in form of MgATP2-
-
-
?
CDP-D-glucose
CMP + glucose 1-phosphate
-
at 5% of the activity with UDP-glucose
-
-
?
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
GDP-glucose
GMP + glucose 1-phosphate
-
at 5% of the activity with UDP-glucose
-
-
?
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
NDP + H2O
NMP + phosphate
-
-
-
-
?
NMN + H2O
nicotinamide riboside + phosphate
NTP + H2O
NDP + phosphate
-
-
-
-
?
UDP-D-glucose
UMP + glucose 1-phosphate
UDP-D-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
-
-
?
UDP-galactose
UMP + galactose 1-phosphate
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
UDP-N-acetyl-D-galactosamine
UMP + N-acetyl-D-galactosamine 1-phosphate
-
-
-
?
UDP-N-acetyl-D-glucosamine
UMP + N-acetyl-D-glucosamine 1-phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
UTP in form of MgUTP2-
-
-
?
additional information
?
-
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
15% of the activity with UDP-glucose
-
-
?
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
-
20% of the activity with UDP-glucose
-
-
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
best substrate, 130% of the activity with UDP-glucose
-
-
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
-
95% of the activity with UDP-glucose
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
3% of the activity with UDP-glucose
-
-
?
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
-
2% of the activity with UDP-glucose
-
-
?
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
10% of the activity with UDP-glucose
-
-
?
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
-
10% of the activity with UDP-glucose
-
-
?
NAD+ + H2O
AMP + NMN
-
-
-
?
NAD+ + H2O
AMP + NMN
-
-
-
?
NADH + H2O
NMNH + AMP
-
-
-
?
NADH + H2O
NMNH + AMP
-
-
-
?
NMN + H2O
nicotinamide riboside + phosphate
-
-
-
?
NMN + H2O
nicotinamide riboside + phosphate
-
-
-
?
UDP-D-glucose
UMP + glucose 1-phosphate
-
-
-
-
?
UDP-D-glucose
UMP + glucose 1-phosphate
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
UshA protein, with 5'-nucleotidase and UDP-sugar hydrolase activities, is required for growth on AMP or UDP-glucose as sole sources of phosphorus
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
best substrate
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
-
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
products are uridine, phosphate and D-glucose 1-phosphate. The phosphoanhydride and the nucleoside 5'-ester linkages are hydrolyzed without detectable signs of nucleoside monophosphate as an intermediate, possibly because it is hydrolyzed as soon as it is formed without leaving the active center
-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
-
products are uridine, phosphate and D-glucose 1-phosphate. The phosphoanhydride and the nucleoside 5'-ester linkages are hydrolyzed without detectable signs of nucleoside monophosphate as an intermediate, possibly because it is hydrolyzed as soon as it is formed without leaving the active center
-
?
additional information
?
-
-
the enzyme has 5'-nucleotidase activity
-
-
?
additional information
?
-
-
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
?
additional information
?
-
the enzyme shows UDP-sugar hydrolase EC 3.6.1.45, dinucleoside-polyphosphate hydrolase, CDP-alcohol hydrolase EC 3.6.1.53, and 5'-nucleosidase activities EC 3.1.3.5, it has a variety of activities and structure-function relationships, substrate specificity, overview
-
-
?
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Garrett, A.R.; Johnson, L.A.; Beacham, I.R.
Isolation, molecular characterization and expression of the ushB gene of Salmonella typhimurium which encodes a membrane-bound UDP-sugar hydrolase
Mol. Microbiol.
3
177-186
1989
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Burns, D.M.; Beacham, I.R.
Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product
Nucleic Acids Res.
14
4325-4342
1986
Escherichia coli
brenda
Burns, D.M.; Abraham, L.J.; Beacham, I.R.
Characterization of the ush gene of Escherichia coli and its protein products
Gene
25
343-353
1983
Escherichia coli
brenda
Cowman, A.; Beacham, I.R.
Molecular cloning of the gene (ush) from Escherichia coli specifying periplasmic UDP-sugar hydrolase (5'-nucleotidase)
Gene
12
281-286
1980
Escherichia coli
brenda
Beacham, I.R.; Wilson, M.S.
Studies on the UDP-sugar hydrolases from Escherichia coli and Salmonella typhimurium
Arch. Biochem. Biophys.
218
603-608
1982
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Taylor, N.; Beacham, I.R.
Synthesis of Escherichia coli uridine diphosphate glucose hydrolase, and demonstration of an inhibitor, in Salmonella typhimurium cytoplasm
Biochem. Soc. Trans.
3
386-387
1975
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Taylor, N.S.; Beacham, I.R.
Synthesis and localization of Escherichia coli UDP-glucose hydrolase (5'-nucleotidase), and demonstration of a cytoplasmic inhibitor of this enzyme in Salmonella typhimurium
Biochim. Biophys. Acta
411
216-221
1975
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Jones, R.A.; Burns, D.M.; Carruthers, D.J.; Beacham, I.R.
Membrane localization of a UDP-sugar hydrolase, in Salmonella, is by an uncleaved N-terminal signal peptide
FEMS Microbiol. Lett.
114
299-304
1993
Salmonella sp.
brenda
Ciesla, W.P.; Bobak, D.A.
Clostridium difficile toxins A and B are cation-dependent UDP-glucose hydrolases with differing catalytic activities
J. Biol. Chem.
273
16021-16026
1998
Clostridioides difficile
brenda
Edwards, C.J.; Innes, D.J.; Burns, D.M.; Beacham, I.R.
UDP-sugar hydrolase isozymes in Salmonella enterica and Escherichia coli: silent alleles of ushA in related strains of group I Salmonella isolates, and of ushB in wild-type and K12 strains of E. coli, indicate recent and early silencing events, respectively
FEMS Microbiol. Lett.
114
293-298
1993
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Glaser, L.; Melo, A.; Paul, R.
Uridine diphosphate sugar hydrolase. Purification of enzyme and protein inhibitor
J. Biol. Chem.
242
1944-1954
1967
Escherichia coli
brenda
Decottignies, A.; Kolaczkowski, M.; Balzi, E.; Goffeau, A.
Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast
J. Biol. Chem.
269
12797-12803
1994
Saccharomyces cerevisiae
brenda
Innes, D.; Beacham, I.R.; Burns, D.M.
The role of the intracellular inhibitor of periplasmic UDP-sugar hydrolase (5'-nucleotidase) in Escherichia coli: cytoplasmic localisation of 5'-nucleotidase is conditionally lethal
J. Basic Microbiol.
41
329-337
2001
Escherichia coli
brenda
Lee, K.S.; Song, S.B.; Kim, K.E.; Kim, Y.H.; Kim, S.K.; Kho, B.H.; Ko, D.K.; Choi, Y.K.; Lee, Y.K.; Kim, C.K.; Kim, Y.C.; Lim, J.Y.; Kim, Y.; Min, K.H.; Wanner, B.L.
Cloning and characterization of the UDP-sugar hydrolase gene (ushA) of Enterobacter aerogenes IFO 12010
Biochem. Biophys. Res. Commun.
269
526-531
2000
Klebsiella aerogenes (Q9RQT7), Klebsiella aerogenes, Klebsiella aerogenes IFO 12010 (Q9RQT7)
brenda
Rittmann, D.; Sorger-Herrmann, U.; Wendisch, V.F.
Phosphate starvation-inducible gene ushA encodes a 5 nucleotidase required for growth of Corynebacterium glutamicum on media with nucleotides as the phosphorus source
Appl. Environ. Microbiol.
71
4339-4344
2005
Corynebacterium glutamicum
brenda
Innes, D.; Beacham, I.R.; Beven, C.A.; Douglas, M.; Laird, M.W.; Joly, J.C.; Burns, D.M.
The cryptic ushA gene (ushA(c)) in natural isolates of Salmonella enterica (serotype Typhimurium) has been inactivated by a single missense mutation
Microbiology
147
1887-1896
2001
Salmonella enterica
brenda
Yagi, T.; Baroja-Fernandez, E.; Yamamoto, R.; Munnoz, F.-J.; Akazawa, A.; Hong, K.S.; Pozueta-Romero, J.
Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose
Biochem. J.
370
409-415
2003
Sus scrofa, Homo sapiens (O95848), Homo sapiens
brenda
Alves-Pereira, I.; Canales, J.; Cabezas, A.; Cordero, P.M.; Costas, M.J.; Cameselle, J.C.
CDP-alcohol hydrolase, a very efficient activity of the 5-nucleotidase/UDP-sugar hydrolase encoded by the ushA gene of Yersinia intermedia and Escherichia coli
J. Bacteriol.
190
6153-6161
2008
Escherichia coli, Yersinia intermedia (A4URQ8), Yersinia intermedia, Yersinia intermedia CECT 7230 (A4URQ8)
brenda
Heyen, C.A.; Tagliabracci, V.S.; Zhai, L.; Roach, P.J.
Characterization of mouse UDP-glucose pyrophosphatase, a Nudix hydrolase encoded by the Nudt14 gene
Biochem. Biophys. Res. Commun.
390
1414-1418
2009
Mus musculus (Q9D142), Mus musculus
brenda
Wang, L.; Zhou, Y.J.; Ji, D.; Lin, X.; Liu, Y.; Zhang, Y.; Liu, W.; Zhao, Z.K.
Identification of UshA as a major enzyme for NAD degradation in Escherichia coli
Enzyme Microb. Technol.
58-59
75-79
2014
Escherichia coli (B1XCS0), Escherichia coli DH10B (B1XCS0)
brenda