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Information on EC 2.7.1.177 - L-threonine kinase for references in articles please use BRENDA:EC2.7.1.177
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IUBMB Comments The enzyme is involved in the de novo synthesis of adenosylcobalamin. It is specific for ATP and free L-threonine. In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
The expected taxonomic range for this enzyme is: Salmonella enterica
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ATP + L-threonine = ADP + O-phospho-L-threonine
ATP + L-threonine = ADP + O-phospho-L-threonine
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ATP + L-threonine = ADP + O-phospho-L-threonine
steady-state ordered BiBI mechanism
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ATP:L-threonine O3-phosphotransferase
The enzyme is involved in the de novo synthesis of adenosylcobalamin. It is specific for ATP and free L-threonine. In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
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ATP + L-threonine
ADP + O-phospho-L-threonine
additional information
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ATP + L-threonine
ADP + O-phospho-L-threonine
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ATP + L-threonine
ADP + O-phospho-L-threonine
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ATP + L-threonine
ADP + O-phospho-L-threonine
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product indentified by 31P NMR spectroscopy
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additional information
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the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
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additional information
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the activity with CTP, GTP, or UTP is 6, 11, 3% of the activity with ATP, respectively
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ATP + L-threonine
ADP + O-phospho-L-threonine
ATP + L-threonine
ADP + O-phospho-L-threonine
Q9XDM4
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ATP + L-threonine
ADP + O-phospho-L-threonine
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0.127 - 4.698
L-threonine
0.0547
ATP
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Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication
0.0547
ATP
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wild-type, pH 7.4, temperature not specified in the publication
0.068
ATP
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mutant D135N, pH 7.4, temperature not specified in the publication
0.069
ATP
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calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication
0.074
ATP
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mutant S255A, pH 7.4, temperature not specified in the publication
0.076
ATP
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mutant S253A, pH 7.4, temperature not specified in the publication
0.087
ATP
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mutant T134A, pH 7.4, temperature not specified in the publication
0.098
ATP
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mutant T101A, pH 7.4, temperature not specified in the publication
0.117
ATP
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mutant E24Q, pH 7.4, temperature not specified in the publication
0.141
ATP
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mutant D103N, pH 7.4, temperature not specified in the publication
0.163
ATP
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mutant D103A, pH 7.4, temperature not specified in the publication
1.264
ATP
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mutant E132Q, pH 7.4, temperature not specified in the publication
1.374
ATP
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mutant S99A, pH 7.4, temperature not specified in the publication
1.979
ATP
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mutant E132A, pH 7.4, temperature not specified in the publication
0.127
L-threonine
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calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication
0.142
L-threonine
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mutant T134A, pH 7.4, temperature not specified in the publication
0.144
L-threonine
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mutant E132Q, pH 7.4, temperature not specified in the publication
0.146
L-threonine
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Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication
0.146
L-threonine
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wild-type, pH 7.4, temperature not specified in the publication
0.176
L-threonine
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mutant S99A, pH 7.4, temperature not specified in the publication
0.184
L-threonine
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mutant D103N, pH 7.4, temperature not specified in the publication
0.198
L-threonine
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mutant E132A, pH 7.4, temperature not specified in the publication
0.22
L-threonine
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mutant T101A, pH 7.4, temperature not specified in the publication
0.258
L-threonine
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mutant D103A, pH 7.4, temperature not specified in the publication
0.273
L-threonine
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mutant D135N, pH 7.4, temperature not specified in the publication
0.464
L-threonine
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mutant E24Q, pH 7.4, temperature not specified in the publication
3.708
L-threonine
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mutant S255A, pH 7.4, temperature not specified in the publication
4.698
L-threonine
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mutant S253A, pH 7.4, temperature not specified in the publication
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0.016 - 0.0427
L-threonine
0.0173
ATP
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mutant D135N, pH 7.4, temperature not specified in the publication
0.0187
ATP
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mutant E24Q, pH 7.4, temperature not specified in the publication
0.0205
ATP
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mutant E132A, pH 7.4, temperature not specified in the publication
0.0227
ATP
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mutant S255A, pH 7.4, temperature not specified in the publication
0.026
ATP
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mutant S253A, pH 7.4, temperature not specified in the publication
0.0272
ATP
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mutant E132Q, pH 7.4, temperature not specified in the publication
0.0313
ATP
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mutant D103A, pH 7.4, temperature not specified in the publication
0.0338
ATP
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mutant D103N, pH 7.4, temperature not specified in the publication; mutant S99A, pH 7.4, temperature not specified in the publication
0.0342
ATP
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mutant T134A, pH 7.4, temperature not specified in the publication
0.0355
ATP
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mutant T101A, pH 7.4, temperature not specified in the publication
0.408
ATP
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wild-type, pH 7.4, temperature not specified in the publication
0.016
L-threonine
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mutant D135N, pH 7.4, temperature not specified in the publication
0.0188
L-threonine
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mutant E24Q, pH 7.4, temperature not specified in the publication
0.0193
L-threonine
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mutant E132A, pH 7.4, temperature not specified in the publication
0.0238
L-threonine
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mutant S255A, pH 7.4, temperature not specified in the publication
0.0258
L-threonine
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mutant E132Q, pH 7.4, temperature not specified in the publication
0.0287
L-threonine
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mutant S253A, pH 7.4, temperature not specified in the publication
0.0322
L-threonine
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mutant D103A, pH 7.4, temperature not specified in the publication
0.0325
L-threonine
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mutant S99A, pH 7.4, temperature not specified in the publication
0.0353
L-threonine
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mutant T134A, pH 7.4, temperature not specified in the publication
0.0358
L-threonine
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mutant D103N, pH 7.4, temperature not specified in the publication
0.037
L-threonine
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mutant T101A, pH 7.4, temperature not specified in the publication
0.0427
L-threonine
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wild-type, pH 7.4, temperature not specified in the publication
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0.000061 - 0.00292
L-threonine
0.000104
ATP
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mutant E132A, pH 7.4, temperature not specified in the publication
0.00022
ATP
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mutant E132Q, pH 7.4, temperature not specified in the publication
0.000247
ATP
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mutant S99A, pH 7.4, temperature not specified in the publication
0.00159
ATP
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mutant E24Q, pH 7.4, temperature not specified in the publication
0.00193
ATP
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mutant D103A, pH 7.4, temperature not specified in the publication
0.0024
ATP
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mutant D103N, pH 7.4, temperature not specified in the publication
0.00257
ATP
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mutant D135N, pH 7.4, temperature not specified in the publication
0.00308
ATP
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mutant S255A, pH 7.4, temperature not specified in the publication
0.00342
ATP
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mutant S253A, pH 7.4, temperature not specified in the publication
0.00363
ATP
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mutant T101A, pH 7.4, temperature not specified in the publication
0.00393
ATP
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mutant T134A, pH 7.4, temperature not specified in the publication
0.00755
ATP
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wild-type, pH 7.4, temperature not specified in the publication
0.000061
L-threonine
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mutant S253A, pH 7.4, temperature not specified in the publication
0.0000643
L-threonine
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mutant S255A, pH 7.4, temperature not specified in the publication
0.000407
L-threonine
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mutant E24Q, pH 7.4, temperature not specified in the publication
0.000587
L-threonine
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mutant D135N, pH 7.4, temperature not specified in the publication
0.00098
L-threonine
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mutant E132A, pH 7.4, temperature not specified in the publication
0.00125
L-threonine
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mutant D103A, pH 7.4, temperature not specified in the publication
0.00168
L-threonine
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mutant T101A, pH 7.4, temperature not specified in the publication
0.0018
L-threonine
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mutant E132Q, pH 7.4, temperature not specified in the publication
0.00185
L-threonine
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mutant S99A, pH 7.4, temperature not specified in the publication
0.00195
L-threonine
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mutant D103N, pH 7.4, temperature not specified in the publication
0.00248
L-threonine
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mutant T134A, pH 7.4, temperature not specified in the publication
0.00292
L-threonine
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wild-type, pH 7.4, temperature not specified in the publication
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no activity in Streptomyces coelicolor
the protein CouR3, encoded by gene couR3, exhibits an ATPase activity similar to its close orthologue, the threonine kinase PduX, but it does not show a threonine kinase activity
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brenda
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UniProt
brenda
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metabolism
involved in the biosynthesis of adenosylcobalamin
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32787
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x * 32787, calculated from sequence, x * 35000, SDS-PAGE
35000
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x * 32787, calculated from sequence, x * 35000, SDS-PAGE
35000
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x * 35000, SDS-PAGE
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?
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x * 32787, calculated from sequence, x * 35000, SDS-PAGE
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D103N
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similar growth rate compared to wild-type
D135A
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no activity, decrease in helical structure
D135N
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similar growth rate compared to wild-type
E132A
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similar growth rate compared to wild-type
E132Q
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similar growth rate compared to wild-type
E24A
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no activity, decrease in helical structure
E24Q
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similar growth rate compared to wild-type
S253A
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low growth rate, reduced affinity for L-threonine
S255A
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low growth rate, reduced affinity for L-threonine
S99A
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similar growth rate compared to wild-type
T101A
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similar growth rate compared to wild-type
T134A
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similar growth rate compared to wild-type
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nickel-nitrilotriacetate column
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Fan, C.; Bobik, T.A.
The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis
J. Biol. Chem.
283
11322-11329
2008
Salmonella enterica (Q9XDM4), Salmonella enterica
brenda
Fan, C.; Fromm, H.J.; Bobik, T.A.
Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica
J. Biol. Chem.
284
20240-20248
2009
Salmonella enterica (Q9XDM4), Salmonella enterica
brenda
Novotna, J.; Gust, B.; Kulik, A.; Spizek, J.; Heide, L.
Five gene products are required for assembly of the central pyrrole moiety of coumermycin A1
J. Ind. Microbiol. Biotechnol.
40
915-925
2013
no activity in Streptomyces coelicolor
brenda
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2.7.1.177 L-threonine kinase
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