EC number:2.7.6.2

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.6 Diphosphotransferases
ID:2.7.6.2
Description:Thiamine diphosphokinase.
Alternative Name: Thiamine pyrophosphokinase.
Thiamine kinase.
Cath: 3.40.50.10240; 2.60.120.320;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.6.2
BRENDA Enzyme Link: BRENDA 2.7.6.2
KEGG Enzyme Link: KEGG2.7.6.2
BioCyc Enzyme Link: BioCyc 2.7.6.2
ExPASy Enzyme Link: ExPASy2.7.6.2
EC2PDB Enzyme Link: EC2PDB 2.7.6.2
ExplorEnz Enzyme Link: ExplorEnz 2.7.6.2
PRIAM enzyme-specific profiles Link: PRIAM 2.7.6.2
IntEnz Enzyme Link: IntEnz 2.7.6.2
MEDLINE Enzyme Link: MEDLINE 2.7.6.2

EC number:2.7.6.2

MSA:

2.7.6.2;
Phylogenetic Tree:

2.7.6.2;
Uniprot:
M-CSA:
RHEA:11576 ATP + thiamine = AMP + H(+) + thiamine diphosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:7]-[O;H0;+0:8]-[P;H0;+0:3](-[*:4])(=[*:5])-[*:6].[*:1]-[OH;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Partial purification and properties of thiamine pyrophosphokinase from pig brain.Peterson JW, Gubler CJ, Kuby SA1975 Aug 26239748
Pyrithiamine as a substrate for thiamine pyrophosphokinase.Liu JY, Timm DE, Hurley TD2006 Mar 1016365036
Steady-state kinetics and mutational studies of recombinant human thiamin pyrophosphokinase.Onozuka M, Nosaka K2003 Jun12953792
The crystal structure of yeast thiamin pyrophosphokinase.Baker LJ, Dorocke JA, Harris RA, Timm DE2001 Jun11435118
Molecular cloning of human thiamin pyrophosphokinase.Zhao R, Gao F, Goldman ID2001 Jan 2611342117