Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
Thiamin pyrophosphokinase, vitamin B1 binding domain
Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyses the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis [1]. [1]. 11435118. The crystal structure of yeast thiamin pyrophosphokinase. Baker LJ, Dorocke JA, Harris RA, Timm DE;. Structure 2001;9:539-546. (from Pfam)
Thiamin pyrophosphokinase, catalytic domain
thiamine pyrophosphokinase
thiamine pyrophosphokinase catalyzes the phosphorylation of thiamine to thiamine pyrophosphate
thiamine diphosphokinase
This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on