hGuanylatekinase, His-Tag
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SKU: P2020-107 trenzyme
Description
The transformation process of cellular guanosine monophosphate kinase (GMP) into guanosine monophosphate kinase (GDP) is performing due to human guanylate kinase which catalyses the phosphorylation reaction. Moreover, human guanylate kinase is known to have a similar structure to the A57R protein. In addition to phosphorylation catalysis, the enzyme plays a crucial role in the breakdown and synthesis of purines. Purine metabolism is present in a broad range of different organisms.
Overview
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Product Name: hGuanylatekinase, His-Tag
- Catalog No.: P2020-107
- RefSeq Links: UniProt: Q16774
- Synonyms: guanosine monophosphate kinase; GMK; GMPK; Guanylate kinase; GUK1; hGMPK; human Guanylate kinase; GMP Kinase
Sequence Information
- Species: Homo sapiens, human
- Tags: His-Tag, N-terminal
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Sequence without tags (AA 1-198):
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
Product Information
- Expression Host: human, HEK293
- Formulation: PBS, pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 95% as determined by SDS-PAGE
Background Information
Human Guanylate kinase is the only known enzyme which catalyzes the ATP-dependent phosphorylation of cellular guanosine monophosphate (GMP) into guanosine diphosphate (GDP). Process is crucial for GMP and cyclic guanosine monophosphate (cGMP) recycling, essential for cellular viability and proliferation. It occurs in low eukaryotes, prokaryotes as well as in vertebrates. Human Guanylate kinase is a monomeric protein that is highly conserved and made up of approximately 200 amino acids. This enzyme belongs to the family of transferases with a phosphate group as phosphotransferases. The hGuanylatekinase is essential for producing the nucleotide building blocks of DNA, RNA. That enzyme is indispendable in metabolic activation of antiviral prodrugs. The hGuanylatekinase structure consists of three particular domains that are dynamic: LID, GMP-binding, and CORE domain.
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