Diphosphomevalonate decarboxylase

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Diphosphomevalonate decarboxylase
Diphosphomevalonate decarboxylase
Ribbon / surface model of the dimer according to PDB  3D4J

Existing structural data : 3D4J

Properties of human protein
Mass / length primary structure 399 amino acids
Secondary to quaternary structure Homodimer
Identifier
Gene name MVD
External IDs
Enzyme classification
EC, category 4.1.1.33 ,  lyase
Response type Decarboxylation
Substrate ATP + diphosphomevalonate
Products ADP + isopentenyl diphosphate + P i + CO 2
Occurrence
Parent taxon Creature
Orthologue
human House mouse
Entrez 4597 192156
Ensemble ENSG00000167508 ENSMUSG00000006517
UniProt P53602 Q99JF5
Refseq (mRNA) NM_002461 NM_13865
Refseq (protein) NP_002452 NP_619597
Gene locus Chr 16: 88.65 - 88.66 Mb Chr 8: 122.43 - 122.44 Mb
PubMed search 4597 192156

The pyrophosphomevalonate decarboxylase (MDDase) is the enzyme , which in most living things, the conversion of Diphosphomevalonat to isopentenyl diphosphate catalyzed . In eukaryotes this reaction is part of the biosynthesis of isoprenoids , especially in animals part of the cholesterol biosynthesis. In humans, MDDase is expressed in the heart , lungs , liver , muscles , brain , pancreas , kidneys and placenta and, in contrast to enzymes located upstream in the synthesis path, is not localized in the peroxisomes but in the cytosol .

Catalyzed reaction

Diphosphomevalonate+ ATP ⇒ IPP+ ADP + P i + CO 2

5-Diphospho- R mevalonate is converted to isopentenyl diphosphate (IPP).

Individual evidence

  1. ↑ Homologues at OMA
  2. ↑ UniProt P53602
  3. ↑ Hogenboom S, Tuyp JJ, Espeel M, Koster J, Wanders RJ, Waterham HR: Human mevalonate pyrophosphate decarboxylase is localized in the cytosol . In: Mol. Genet. Metab. . 81, No. 3, March 2004, pp. 216-24. doi : 10.1016 / j.ymgme.2003.12.001 . PMID 14972328 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Cholesterol Biosynthesis  - Learning and Teaching Materials