PMVK Protein, Human (His)

PMVK proteins play a key role in cellular metabolism by catalyzing the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate, leading to the production of mevalonate diphosphate and ADP. This enzymatic activity represents a key step in the mevalonate-mediated biosynthesis of isopentenyl diphosphate, a precursor for the synthesis of various polyisoprene metabolites. PMVK Protein, Human (His) is the recombinant human-derived PMVK protein, expressed by E. coli , with N-6*His labeled tag. The total length of PMVK Protein, Human (His) is 192 a.a., with molecular weight of ~26.0 kDa.

The PMVK (Phosphomevalonate kinase) protein is an enzyme that catalyzes a pivotal step in the mevalonate pathway, which is crucial for the biosynthesis of isopentenyl diphosphate and various polyisoprenoid metabolites. Specifically, PMVK facilitates the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate, generating mevalonate diphosphate and ADP. This enzymatic activity is essential for the production of isoprenoids, which serve as precursors for essential cellular components such as sterols, dolichols, and ubiquinones. The mevalonate pathway, in which PMVK participates, plays a central role in diverse biological processes, including cholesterol synthesis and regulation of cell membrane integrity. Understanding the functions of PMVK provides insights into the regulation of isoprenoid metabolism and its implications for various cellular functions.

Human

E. coli

N-6*His

Q15126 (M1-L192)

10654  [NCBI]

MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIEFIRSRL

Approximately 26.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.