Protein Family Models

Mevalonate diphosphate decarboxylase (EC:4.1.1.33) catalyzes the ATP dependent decarboxylation of mevalonate 5-diphosphate (MVAPP) to form isopentenyl 5-diphosphate. The reaction is required for production of polyisoprenoids and sterols from acetyl-CoA. This entry represents the C-terminal domain of the mevalonate 5-diphosphate decarboxylase enzyme which is a member of the GHMP kinase superfamily. [1]. 11698677. Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK;. Proc Natl Acad Sci U S A. 2001;98:12896-12901. [2]. 17583736. Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity. Byres E, Alphey MS, Smith TK, Hunter WN;. J Mol Biol. 2007;371:540-553. [3]. 18823933. Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure. Voynova NE, Fu Z, Battaile KP, Herdendorf TJ, Kim JJ, Miziorko HM;. Arch Biochem Biophys. 2008;480:58-67. (from Pfam)

Date:

2024-10-16

This entry represents the N-terminal domain of Diphosphomevalonate decarboxylases [1-5] whoch catalyse the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Members of this entry function in the mevalonate pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis. Paper describing PDB structure 1fi4. [1]. 11698677. Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK;. Proc Natl Acad Sci U S A. 2001;98:12896-12901. Paper describing PDB structure 2hk2. [2]. 17583736. Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity. Byres E, Alphey MS, Smith TK, Hunter WN;. J Mol Biol. 2007;371:540-553. Paper describing PDB structure 3d4j. [3]. 18823933. Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure. Voynova NE, Fu Z, Battaile KP, Herdendorf TJ, Kim JJ, Miziorko HM;. Arch Biochem Biophys. 2008;480:58-67. Paper describing PDB structure 3qt5. [4]. 21561869. Crystal structures of Staphylococcus epidermidis mevalonate diphosphate decarboxylase bound to inhibitory analogs reveal new insight into substrate binding and catalysis. Barta ML, Skaff DA, McWhorter WJ, Herdendorf TJ, Miziorko HM, Geisbrecht BV;. J Biol Chem. 2011;286:23900-23910. Paper describing PDB structure 4dpw. [5]. 22734632. Structu. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family includes homoserine kinases, galactokinases and mevalonate kinases. (from Pfam)

Date:

2024-08-14

diphosphomevalonate/mevalonate 3,5-bisphosphate decarboxylase family protein similar to diphosphomevalonate decarboxylase (DMD) that catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP), and mevalonate 3,5-bisphosphate decarboxylase (MBD) that catalyzes the ATP-independent decarboxylation of (R)-mevalonate 3,5-bisphosphate to isopentenyl phosphate

Date:

2021-09-24

This enzyme catalyzes the last step in the synthesis of isopentenyl diphosphate (IPP) in the mevalonate pathway. Alternate names: mevalonate diphosphate decarboxylase; pyrophosphomevalonate decarboxylase

Gene:

mvaD

Date:

2024-05-30