thiamin diphosphate kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.4.15 | ||||||||
CAS no. | 9075-79-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a thiamine-diphosphate kinase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction
Thus, the two substrates of this enzyme are ATP and thiamine diphosphate, whereas its two products are ADP and thiamine triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:thiamine-diphosphate phosphotransferase. Other names in common use include ATP:thiamin-diphosphate phosphotransferase, TDP kinase, thiamin diphosphate kinase, thiamin diphosphate phosphotransferase, thiamin pyrophosphate kinase, thiamine diphosphate kinase, and protein bound thiamin diphosphate:ATP phosphoryltransferase.
Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells. ADP consists of three important structural components: a sugar backbone attached to adenine and two phosphate groups bonded to the 5 carbon atom of ribose. The diphosphate group of ADP is attached to the 5’ carbon of the sugar backbone, while the adenine attaches to the 1’ carbon.
Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates. By constantly monitoring phosphate nucleotide levels inside the cell, ADK plays an important role in cellular energy homeostasis.
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