| Version |
2.5 |
| Creation Date |
2005-11-16 15:48:42 |
| Update Date |
2009-05-05 20:58:41 |
| Accession Number |
HMDB01343 |
| Secondary Accession Numbers |
Not Available |
| Common Name |
Mevalonic acid-5P |
| Description |
5-Phosphomevalonate is a metabolic intermediate in the mevalonate pathway, catalyzed by the enzyme mevalonate kinase from Mevalonate. (wikipedia) |
| Synonyms |
- (R)-5-phosphomevalonate
- (R)-5-phosphomevalonic acid
- (R)-5-phosphomevaloonate
- (R)-5-phosphomevaloonic acid
- (R)-mevalonic acid 5-phosphate
- 5-phosphomevalonate
- mevalonate-5-p
- mevalonate-5-phosphate
- mevalonate-5P
- mevalonate-p
- p-mevalonate
|
| Chemical IUPAC Name |
3-hydroxy-3-methyl-5-phosphonooxy-pentanoic acid |
| Chemical Formula |
C6H13O7P |
| Chemical Structure |
 |
| Chemical Taxonomy |
| Kingdom |
|
| Super Class |
|
| Class |
|
| Sub Class |
- Short chain acyl phosphates
|
| Family |
|
| Species |
- tertiary alcohol
- carboxylic acid
- phosphoric acid ester
|
| Biofunction |
| — |
| Application |
| — |
| Source |
|
|
| Average Molecular Weight |
228.137 |
| Monoisotopic Molecular Weight |
228.039886 |
| Isomeric SMILES |
C[C@@](O)(CCOP(O)(O)=O)CC(O)=O |
| Canonical SMILES |
CC(O)(CCOP(O)(O)=O)CC(O)=O |
| KEGG Compound ID |
C01107  |
| BioCyc ID |
CPD-499  |
| BiGG ID |
36819  |
| Wikipedia Link |
5-phosphomevalonate  |
| NuGOwiki Link |
HMDB01343  |
| Metagene Link |
HMDB01343  |
| METLIN ID |
6177  |
| PubChem Compound |
439400  |
| PubChem Substance |
8144823  |
| ChEBI ID |
17436  |
| CAS Registry Number |
73566-35-5 |
| InChI Identifier |
InChI=1/C6H13O7P/c1-6(9,4-5(7)8)2-3-13-14(10,11)12/h9H,2-4H2,1H3,(H,7,8)(H2,10,11,12)/t6-/m1/s1 |
| Synthesis Reference |
Not Available |
| Melting Point (Experimental) |
Not Available |
| Experimental Water Solubility |
Not Available
Source: PhysProp
|
| Predicted Water Solubility |
19.9 mg/mL [Predicted by ALOGPS]
Calculated using ALOGPS
|
| Physiological Charge |
-3 |
| State |
Solid |
| Experimental LogP/Hydrophobicity |
Not Available
Source: PhysProp
|
| Predicted LogP/Hydrophobicity |
-2.18 [Predicted by ALOGPS]; -2.1 [Predicted by PubChem via XLOGP]
Calculated using ALOGPS
|
| Material Safety Data Sheet (MSDS) |
Not Available |
| MOL File |
Show |
| SDF File |
Show |
| PDB File |
Show |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
Not Available |
| Experimental 1H NMR Spectrum |
Not Available |
| Experimental 13C NMR Spectrum |
Not Available |
| Experimental 13C HSQC Spectrum |
Not Available |
| Predicted 1H NMR Spectrum |
Show Image Show Peaklist
|
| Predicted 13C NMR Spectrum |
Show Image Show Peaklist
|
| Mass Spectrum |
Not Available |
| Simplified TOCSY Spectrum |
Not Available |
| BMRB Spectrum |
Not Available |
| Cellular Location |
- Cytoplasm (Predicted from LogP)
- peroxisome
|
| Biofluid Location |
Not Available |
| Tissue Location |
| Tissue |
References |
| Heart |
— |
| Kidney |
— |
| Liver |
— |
| Pancreas |
— |
| Skeletal Muscle |
— |
|
| Concentrations (Normal) |
Not Available |
| Concentrations (Abnormal) |
Not Available |
| Associated Disorders |
Not Available |
| OMIM ID |
Not Available |
| Pathways |
|
| General References |
- Popjak G, Boehm G, Parker TS, Edmond J, Edwards PA, Fogelman AM: Determination of mevalonate in blood plasma in man and rat. Mevalonate "tolerance" tests in man. J Lipid Res. 1979 Aug;20(6):716-28. [PubMed
]
- Campos N, Rodriguez-Concepcion M, Sauret-Gueto S, Gallego F, Lois LM, Boronat A: Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyl diphosphate from mevalonate: a novel system for the genetic analysis of the 2-C-methyl-d-erythritol 4-phosphate pathway for isoprenoid biosynthesis. Biochem J. 2001 Jan 1;353(Pt 1):59-67. [PubMed
]
- Houten SM, Waterham HR: Nonorthologous gene displacement of phosphomevalonate kinase. Mol Genet Metab. 2001 Mar;72(3):273-6. [PubMed
]
- Wikipedia

|
| Metabolic Enzymes |
- Phosphomevalonate kinase
- Mevalonate kinase
- cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
|
|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6305 |
| Enzyme 1 Name |
Phosphomevalonate kinase |
| Enzyme 1 Synonyms |
- PMKase
|
| Enzyme 1 Gene Name |
PMVK |
| Enzyme 1 Protein Sequence |
>Phosphomevalonate kinase
MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQ
RLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFRE
AYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQ
LENLIEFIRSRL
|
| Enzyme 1 Number of Residues |
192 |
| Enzyme 1 Molecular Weight |
21995 |
| Enzyme 1 Theoretical pI |
5.41 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- kinase activity
- phosphomevalonate kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolism
- cellular metabolism
- cholesterol biosynthesis
- cholesterol metabolism
- metabolism
- physiological process
- sterol metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
ATP + (R)-5-phosphomevalonate = ADP + (R)-5- diphosphomevalonate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1294782  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q15126  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PMVK_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>579 bp
ATGGCCCCGCTGGGAGGCGCCCCGCGGCTGGTACTGCTGTTCAGCGGCAAGAGGAAATCC
GGGAAGGACTTCGTGACCGAGGCGCTGCAGAGCAGACTTGGAGCTGATGTCTGTGCTGTC
CTCCGGCTCTCTGGTCCACTCAAGGAACAGTATGCTCAGGAGCATGGCTTGAACTTCCAG
AGACTCCTGGACACCAGCACCTACAAGGAGGCCTTTCGGAAGGACATGATCCGCTGGGGA
GAGGAGAAACGCCAGGCTGACCCAGGCTTCTTTTGCAGGAAGATTGTGGAGGGCATCTCC
CAGCCCATCTGGCTGGTGAGTGACACACGGAGAGTGTCTGACATCCAGTGGTTTCGGGAG
GCCTATGGGGCCGTGACGCAGACGGTCCGCGTTGTAGCGTTGGAGCAGAGCCGACAGCAG
CGGGGCTGGGTGTTCACGCCAGGGGTGGACGATGCTGAGTCAGAATGTGGCCTGGACAAC
TTCGGGGACTTTGACTGGGTCATCGAGAACCATGGAGTTGAACAGCGCCTGGAGGAGCAG
TTGGAGAACCTGATAGAATTTATCCGCTCCAGACTTTAG
|
| Enzyme 1 GenBank Gene ID |
L77213  |
| Enzyme 1 GeneCard ID |
PMVK  |
| Enzyme 1 GenAtlas ID |
PMVK  |
| Enzyme 1 HGNC ID |
HGNC:9141  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p13-q23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Chambliss KL, Slaughter CA, Schreiner R, Hoffmann GF, Gibson KM: Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. J Biol Chem. 1996 Jul 19;271(29):17330-4. [PubMed
]
- Olivier LM, Chambliss KL, Gibson KM, Krisans SK: Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting. J Lipid Res. 1999 Apr;40(4):672-9. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6342 |
| Enzyme 2 Name |
Mevalonate kinase |
| Enzyme 2 Synonyms |
- MK
|
| Enzyme 2 Gene Name |
MVK |
| Enzyme 2 Protein Sequence |
>Mevalonate kinase
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKR
AWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSIC
RKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKE
DLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVP
RNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDM
NQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQAL
TSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
|
| Enzyme 2 Number of Residues |
396 |
| Enzyme 2 Molecular Weight |
42451 |
| Enzyme 2 Theoretical pI |
6.43 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- mevalonate kinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- cellular metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- phosphate metabolism
- phosphorus metabolism
- phosphorylation
- physiological process
- primary metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
May be a regulatory site in cholesterol biosynthetic pathway |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
187561  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q03426  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
KIME_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1191 bp
ATGTTGTCAGAAGTCCTACTGGTGTCTGCTCCGGGGAAAGTCATCCTTCATGGAGAACAT
GCCGTGGTACATGGCAAGGTAGCACTGGCTGTATCCTTGAACTTGAGAACATTCCTCCGG
CTTCAACCCCACAGCAATGGGAAAGTGGACCTCAGCTTACCCAACATTGGTATCAAGCGG
GCCTGGGATGTGGCCAGGCTTCAGTCACTGGACACAAGCTTTCTGGAGCAAGGTGATGTC
ACAACACCCACCTCAGAGCAAGTGGAGAAGCTAAAGGAGGTTGCAGGCTTGCCTGACGAC
TGTGCTGTCACCGAGCGCCTGGCTGTGCTGGCCTTTCTTTACTTATACCTGTCCATCTGC
CGGAAGCAGAGGGCCCTGCCGAGCCTGGATATCGTAGTGTGGTCGGAGCTGCCCCCCGGG
GCGGGCTTGGGCTCCAGCGCCGCCTACTCGGTGTGTCTGGCAGCAGCCCTCCTGACTGTG
TGCGAGGAGATCCCAAACCCGCTGAAGGACGGGGATTGCGTCAACAGGTGGACCAAGGAG
GATTTGGAGCTAATTAACAAGTGGGCCTTCCAAGGGGAGAGAATGATTCACGGGAACCCC
TCCGGAGTGGACAATGCTGTCAGCACCTGGGGAGGAGCCCTCCGATACCATCAAGGGAAG
ATTTCATCCTTAAAGAGGTCGCCAGCTCTCCAGATCCTGCTGACCAACACCAAAGTCCCT
CGCAATACCAGGGCCCTTGTGGCTGGCGTCAGAAACAGGCTGCTCAAGTTCCCAGAGATC
GTGGCCCCCCTCCTGACCTCAATAGATGCCATCTCCCTGGAGTGTGAGCGCGTGCTGGGA
GAGATGGGGGAAGCCCCAGCCCCGGAGCAGTACCTCGTGCTGGAAGAGCTCATTGACATG
AACCAGCACCATCTGAATGCCCTCGGCGTGGGCCACGCCTCTCTGGACCAGCTCTGCCAG
GTGACCAGGGCCCGCGGACTTCACAGCAAGCTGACTGGCGCAGGCGGTGGTGGCTGTGGC
ATCACACTCCTCAAGCCAGGGCTGGAGCAGCCAGAAGTGGAGGCCACGAAGCAGGCCCTG
ACCAGCTGTGGCTTTGACTGCTTGGAAACCAGCATCGGTGCCCCCGGCGTCTCCATCCAC
TCAGCCACCTCCCTGGACAGCCGAGTCCAGCAAGCCCTGGATGGCCTCTGA
|
| Enzyme 2 GenBank Gene ID |
M88468  |
| Enzyme 2 GeneCard ID |
MVK  |
| Enzyme 2 GenAtlas ID |
MVK  |
| Enzyme 2 HGNC ID |
HGNC:7530  |
| Enzyme 2 Chromosome Location |
12 |
| Enzyme 2 Locus |
12q24 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Schafer BL, Bishop RW, Kratunis VJ, Kalinowski SS, Mosley ST, Gibson KM, Tanaka RD: Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria. J Biol Chem. 1992 Jul 5;267(19):13229-38. [PubMed
]
- Graef E, Caselmann WH, Wells J, Koshy R: Insertional activation of mevalonate kinase by hepatitis B virus DNA in a human hepatoma cell line. Oncogene. 1994 Jan;9(1):81-7. [PubMed
]
- Houten SM, Koster J, Romeijn GJ, Frenkel J, Di Rocco M, Caruso U, Landrieu P, Kelley RI, Kuis W, Poll-The BT, Gibson KM, Wanders RJ, Waterham HR: Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome. Eur J Hum Genet. 2001 Apr;9(4):253-9. [PubMed
]
- Hinson DD, Ross RM, Krisans S, Shaw JL, Kozich V, Rolland MO, Divry P, Mancini J, Hoffmann GF, Gibson KM: Identification of a mutation cluster in mevalonate kinase deficiency, including a new mutation in a patient of Mennonite ancestry. Am J Hum Genet. 1999 Aug;65(2):327-35. [PubMed
]
- Houten SM, Romeijn GJ, Koster J, Gray RG, Darbyshire P, Smit GP, de Klerk JB, Duran M, Gibson KM, Wanders RJ, Waterham HR: Identification and characterization of three novel missense mutations in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of isoprene biosynthesis. Hum Mol Genet. 1999 Aug;8(8):1523-8. [PubMed
]
- Houten SM, Kuis W, Duran M, de Koning TJ, van Royen-Kerkhof A, Romeijn GJ, Frenkel J, Dorland L, de Barse MM, Huijbers WA, Rijkers GT, Waterham HR, Wanders RJ, Poll-The BT: Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat Genet. 1999 Jun;22(2):175-7. [PubMed
]
- Drenth JP, Cuisset L, Grateau G, Vasseur C, van de Velde-Visser SD, de Jong JG, Beckmann JS, van der Meer JW, Delpech M: Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group. Nat Genet. 1999 Jun;22(2):178-81. [PubMed
]
- Cuisset L, Drenth JP, Simon A, Vincent MF, van der Velde Visser S, van der Meer JW, Grateau G, Delpech M: Molecular analysis of MVK mutations and enzymatic activity in hyper-IgD and periodic fever syndrome. Eur J Hum Genet. 2001 Apr;9(4):260-6. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
16528 |
| Enzyme 3 Name |
cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c) |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
MVK |
| Enzyme 3 Protein Sequence |
>cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKR
AWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSIC
RKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKE
DLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVP
RNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDM
NQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQAL
TSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
|
| Enzyme 3 Number of Residues |
396 |
| Enzyme 3 Molecular Weight |
42451 |
| Enzyme 3 Theoretical pI |
6.43 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- mevalonate kinase activity
- nucleotide binding
- phosphotransferase activity, alcohol group as acceptor
- purine nucleotide binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular lipid metabolism
- cellular metabolism
- isoprenoid biosynthesis
- isoprenoid metabolism
- lipid metabolism
- metabolism
- phosphate metabolism
- phosphorus metabolism
- phosphorylation
- physiological process
- primary metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 3 General Function |
Lipid transport and metabolism |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
B2RDU6  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
B2RDU6_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
AK315678  |
| Enzyme 3 GeneCard ID |
B2RDU6  |
| Enzyme 3 GenAtlas ID |
Not Available |
| Enzyme 3 HGNC ID |
Not Available |
| Enzyme 3 Chromosome Location |
12 |
| Enzyme 3 Locus |
12q24 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |