2.7.4.16: thiamine-phosphate kinase
This is an abbreviated version!
For detailed information about thiamine-phosphate kinase, go to the full flat file.
Word Map on EC 2.7.4.16
-
2.7.4.16
-
pyrophosphate
-
tpp
-
pyrophosphorylation
-
2.7.6.2
-
transketolase
-
pyrithiamine
-
cocarboxylase
- 2.7.4.16
- pyrophosphate
- tpp
-
pyrophosphorylation
-
2.7.6.2
- transketolase
- pyrithiamine
-
cocarboxylase
Reaction
Synonyms
ATP:thiamin-phosphate phosphotransferase, kinase, thiamin monophosphate (phosphorylating), More, thiamin monophosphatase, thiamin monophosphate kinase, thiamin monophosphokinase, thiamin phosphate kinase, thiamin pyrophosphokinase, thiamin-monophosphate kinase, thiamin-phosphate kinase, thiamine monophosphate kinase, thiamine monophosphokinase, ThiL, TP kinase
ECTree
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Reference
Reference on EC 2.7.4.16 - thiamine-phosphate kinase
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Nishino, H.
Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase
J. Biochem.
72
1093-1100
1972
Escherichia coli
Webb, E.; Downs, D.
Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium
J. Biol. Chem.
272
15702-15707
1997
Salmonella enterica subsp. enterica serovar Typhimurium (P55881), Salmonella enterica subsp. enterica serovar Typhimurium
Melnick, J.S.; Sprinz, K.I.; Reddick, J.J.; Kinsland, C.; Begley, T.P.
An efficient enzymatic synthesis of thiamin pyrophosphate
Bioorg. Med. Chem. Lett.
13
4139-4141
2003
Escherichia coli
McCulloch, K.M.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
Structural studies of thiamin monophosphate kinase in complex with substrates and products
Biochemistry
47
3810-3821
2008
Aquifex aeolicus (O67883), Aquifex aeolicus
Hayashi, M.; Nosaka, K.
Characterization of thiamin phosphate kinase in the hyperthermophilic archaeon Pyrobaculum calidifontis
J. Nutr. Sci. Vitaminol.
61
369-374
2015
Pyrobaculum calidifontis (A3MTW6), Pyrobaculum calidifontis, Pyrobaculum calidifontis JCM 11548 (A3MTW6)
Kim, H.J.; Lee, H.; Lee, Y.; Choi, I.; Ko, Y.; Lee, S.; Jang, S.
The ThiL enzyme is a valid antibacterial target essential for both thiamine biosynthesis and salvage pathways in Pseudomonas aeruginosa
J. Biol. Chem.
295
10081-10091
2020
Pseudomonas aeruginosa
Sullivan, A.H.; Dranow, D.M.; Horanyi, P.S.; Lorimer, D.D.; Edwards, T.E.; Abendroth, J.
Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products
Sci. Rep.
9
4392
2019
Acinetobacter baumannii (A0A0D5YC82), Acinetobacter baumannii, Acinetobacter baumannii AB5075-UW (A0A0D5YC82)
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