mevalonate kinase

Target not currently curated in GtoImmuPdb

Target id: 640

Nomenclature: mevalonate kinase

Family: Lanosterol biosynthesis pathway

Gene and Protein Information
Previous and Unofficial Names
Database Links
Selected 3D Structures
Enzyme Reaction
Substrates and Reaction Kinetics
Cofactors
Inhibitors
Immuno Process Associations
Tissue Distribution
Clinically-Relevant Mutations and Pathophysiology
General Comments
References
Contributors
How to cite this page

Gene and Protein Information
Species	TM	AA	Chromosomal Location	Gene Symbol	Gene Name	Reference
Human	-	396	12q24.11	MVK	mevalonate kinase	8
Mouse	-	395	5 55.99 cM	Mvk	mevalonate kinase
Rat	-	395	12q16	Mvk	mevalonate kinase

Previous and Unofficial Names
ATP:mevalonate 5-phosphotransferase \| mevalonate 5-phosphotransferase \| mevalonate phosphokinase \| mevalonic acid kinase \| mevalonic kinase \| MVA kinase \| LRBP \| MK \| LH receptor mRNA-binding protein

Previous and Unofficial Names

Database Links
Alphafold	Q03426 (Hs), Q9R008 (Mm), P17256 (Rn)
BRENDA	2.7.1.36
CATH/Gene3D	3.30.230.10, 3.30.70.890
ChEMBL Target	CHEMBL4274 (Rn)
Ensembl Gene	ENSG00000110921 (Hs), ENSMUSG00000041939 (Mm), ENSRNOG00000049604 (Rn)
Entrez Gene	4598 (Hs), 17855 (Mm), 81727 (Rn)
Human Protein Atlas	ENSG00000110921 (Hs)
KEGG Enzyme	2.7.1.36
KEGG Gene	hsa:4598 (Hs), mmu:17855 (Mm), rno:81727 (Rn)
OMIM	251170 (Hs)
Orphanet	ORPHA123588 (Hs)
Pharos	Q03426 (Hs)
RefSeq Nucleotide	NM_001114185 (Hs), NM_000431 (Hs), NM_023556 (Mm), NM_031063 (Rn)
RefSeq Protein	NP_001107657 (Hs), NP_000422 (Hs), NP_076045 (Mm), NP_112325 (Rn)
UniProtKB	Q03426 (Hs), Q9R008 (Mm), P17256 (Rn)
Wikipedia	MVK (Hs)

Selected 3D Structures

Image of receptor 3D structure from RCSB PDB

Description:	Crystal structure of rat mevalonate kinase in complex with feedback inhibitor farnesyl diphosphate
PDB Id:	2R42
Ligand:	farnesyl diphosphate
Resolution:	2.4Å
Species:	Rat
References:	7

Enzyme Reaction

EC Number: 2.7.1.36	ATP + (R)-mevalonate -> ADP + (R)-5-phosphomevalonate

Substrates and Reaction Kinetics

Substrate	Sp.	Property	Value	Units	Standard property	Standard value	Assay description	Assay conditions	Comments	Reference
ATP	Rn	K_cat	21.9	s-1			wild type purified enzyme; in vitro assay	pH 7.5, 34°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5 mM MgCl2, 4 mM ATP, 3 mM (RS)-mevalonic acid	3
ATP	Hs	K_m	7.4x10^-5	M	pK_m	4.1	wild type enzyme, in vitro assay	pH 7.0, 30°C		20
ATP	Hs	K_m	1.784x10^-4	M	pK_m	3.7	recombinant human MVK expressed in E coli; spectrophotometric assay	pH 7.5, 30°C	Concentration of substrates and cofactors: 10 mM MgCl2, 0.2 mM NADH, saturating concentration of (R,S)-mevalonic acid. Concentration of ATP varied between 0.02-6.0 mM.	7
ATP	Hs	K_m	4.4x10^-4	M	pK_m	3.4	recombinant enzyme expressed in E coli, purified by affinity chromatography; in vitro assay- spectrophotometric assay	pH 7.0	Concentration of substrates and cofactors: 6mM MgCl2, 0.2mM NADH, 2mM (R,S)-mevalonate. Concentration of ATP varied between 0.16-5mM.	9
ATP	Rn	K_m	9.5x10^-4	M	pK_m	3.0	wild type purified enzyme; in vitro assay	pH 7.5, 34°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5mM MgCl2, 3 mM (RS)-mevalonate. Concentration of ATP varied between 0.05-1mM	3
ATP	Rn	K_m	9.53x10^-4	M	pK_m	3.0	recombinant overexpression in E coli and purification, in vitro assay	pH 7.5, 25°C	Concentration of substrates and cofactors: 0.16 mM NADH, 4 mM ATP, 3 mM (RS)-mevalonate, 5 mM MgCl2	1
ATP	Rn	K_m	9.53x10^-4	M	pK_m	3.0	wild type purified enzyme; in vitro assay	pH 7.2, 25°C	Concentration of substrates and cofactors; 3mM (RS)-mevalonate, 0.16mM NADH. Concentration of ATP was varied between 0.1 to 10mM	2
ATP	Rn	K_m	1.24x10^-3	M	pK_m	2.9	recombinant enzyme, expression and purification in E coli; in vitro assay	pH 7.0, 30°C		21
ATP	Rn	K_m	1.75x10^-3	M	pK_m	2.8	wild type purified enzyme, in vitro assay	pH 7.0, 25°C	Concentration of substrates and cofactors: 0.5mM NADH, 10mM MgCl2, 1mM (R,S)-mevalonate. Concentrations of ATP varied between 0.1-2mM	24
(RS)-mevalonate	Hs	K_m	2.4x10^-5	M	pK_m	4.6	recombinant enzyme, in vitro assay	pH 7.0, 30°C		20
(RS)-mevalonate	Rn	K_m	3.5x10^-5	M	pK_m	4.5	recombinant enzyme, overexpression in E coli and purification, in vitro assay	pH 7.0, 25°C	Concentration of substrates and cofactors: 0.16 mM NADH, 4 mM ATP, 3 mM (RS)-mevalonate, 5 mM MgCl2	1
(RS)-mevalonate	Rn	K_m	3.5x10^-5	M	pK_m	4.5	purified wild type enzyme; in vitro assay	pH 7.5, 34°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5mM MgCl2, 4 mM ATP. Concentration of (RS)-mevalonate varied between 0.03-5mM	3
(RS)-mevalonate	Rn	K_m	3.5x10^-5	M	pK_m	4.5	purified wild type enzyme; in vitro assay	pH 7.2, 25°C	Concentrations of substrates and cofactors: 4mM ATP, 0.16mM NADH, concentration of (RS)-mevalonate varied between 0.01 to 10 mM	2
(RS)-mevalonate	Hs	K_m	4.08x10^-5	M	pK_m	4.4	recombinant human MVK expressed in E coli; spectrophotometric assay	pH 7.5, 30°C	Concentration of substrates and cofactors: 10 mM MgCl2, 0.2 mM NADH, 6mM ATP, concentration of (R,S)-mevalonic acid varied between 0.017- 3.5 mM	7
(RS)-mevalonate	Hs	K_m	1.5x10^-4	M	pK_m	3.8	recombinant enzyme expressed in E coli, purified by affinity chromatography; in vitro assay- spectrophotometric assay	pH 7.0	Concentration of substrates and cofactors: 6mM MgCl2, 0.2mM NADH, 5mM ATP. Concentration of (R,S)-mevalonate varied.	9
(RS)-mevalonate	Rn	K_m	2.71x10^-4	M	pK_m	3.6	wild type purified enzyme, in vitro assay	pH 7.0, 25°C	Concentration of substrates and cofactors: 2mM ATP, 0.5mM NADH, 10mM MgCl2. Concentration of (R,S)-mevalonate varied between 30-400µM	24
(RS)-mevalonate	Rn	K_m	2.88x10^-4	M	pK_m	3.5	recombinant expression and purification in E coli; in vitro assay	pH 7.0, 30°C		21
ATP	Hs	V_max	37	µmol/min/mg			wild type enzyme, in vitro assay	pH 7.0, 30°C		20
ATP	Rn	V_max	38.7	µmol/min/mg			wild type purified enzyme; in vitro assay	pH 7.5, 34°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5 mM MgCl2, 4 mM ATP, 3 mM (RS)-mevalonic acid	3
(RS)-mevalonate	Hs	V_max	13.6	µmol/min/mg			0.3-0.5µg of purified recombinant enzyme; in vitro assay	pH 7.0	Concentration of substrates and cofactors: 6mM MgCl2, 0.2mM NADH, 5mM ATP. Concentration of (R,S)-mevalonate varied.	9
(RS)-mevalonate	Hs	V_max	28	µmol/min/mg			recombinant human MVK expressed in E coli; spectrophotometric assay	pH 7.5, 30°	Concentration of substrates and cofactors: 10 mM MgCl2, 0.2 mM NADH, 6mM ATP, concentration of (R,S)-mevalonic acid varied between 0.017- 3.5 mM	7
(RS)-mevalonate	Rn	V_max	29.4	µmol/min/mg			Wild type partially purified, in vitro assay, 1.7µg of purified enzyme	pH 7.0, 25°C	Concentration of substrates and cofactors: 2mM ATP, 0.5mM NADH, 10mM MgCl2. Concentration of (R,S)-mevalonate varied between 30-400µM	24
(RS)-mevalonate	Rn	V_max	30.2	µmol/min/mg			recombinant expression and purification in E coli; in vitro assay	pH 7.0, 30°C		21
(RS)-mevalonate	Hs	V_max	37	µmol/min/mg			recombinant enzyme, in vitro assay	pH 7.0, 30°C		20
(RS)-mevalonate	Rn	V_max	38.7	µmol/min/mg			purified wild type enzyme; in vitro assay	pH 7.5, 34°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5 mM MgCl2, 4 mM ATP, 3 mM (RS)-mevalonic acid	3
(RS)-mevalonate	Rn	V_max	38.7	µmol/min/mg			recombinant enzyme, overexpression in E coli and purification, in vitro assay	pH 7.0, 25°C	Concentration of substrates and cofactors: 0.16 mM NADH, 4 mM ATP, 3 mM (RS)-mevalonate, 5 mM MgCl2	1
(RS)-mevalonate	Rn	V_max	38.7	µmol/min/mg			purified wild type enzyme; in vitro assay	pH 7.2, 25°C	Concentration of substrates and cofactors: 0.16 mM NADH, 5 mM MgCl2, 4 mM ATP, 3 mM (RS)-mevalonic acid	2

Cofactors

Cofactor	Species	Comments	Reference
Mg²⁺	Human	The reaction catalysed by mevalonate kinase requires a divalent cation. Use of magnesium as a cofactor has also been characterised in rats.	7,11,22

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Inhibitors

Key to terms and symbols

View all chemical structures

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Ligand		Sp.	Action	Value	Parameter	Reference
farnesyl thiodiphosphate		Hs	Inhibition	7.5	pK_i	26
⤷	pK_i 7.5 (K_i 2.9x10^-8 M) [26] Description: Spectrophotometric in vitro assay Conditions: 30°C, pH 7.5. ATP concentration varied from 0.02-5mM, mevalonate concentration varied from 0.02 to 0.6mM
trans,trans-farnesyl diphosphate		Hs	Feedback inhibition	7.0 – 7.5	pK_i	7,9
⤷	pK_i 7.5 (K_i 3.4x10^-8 M) [7] Description: recombinant wild type enzyme expressed in E coli, in vitro spectrophotometric assay Conditions: 30°C, pH 7.5; 0.5-11µM (R,S)-mevalonic acid, 6mM ATP pK_i 7.0 (K_i 1.01x10^-7 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Concentration of mevalonate fixed and saturating; ATP varied between 0.16-5mM
geranylgeranyl diphosphate		Hs	Feedback inhibition	7.2	pK_i	9
⤷	pK_i 7.2 (K_i 5.9x10^-8 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Saturating concentrations of substrates, 0.16-5mM ATP
geranyl diphosphate		Hs	Feedback inhibition	6.9	pK_i	9
⤷	pK_i 6.9 (K_i 1.16x10^-7 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C, saturating concentrations of substrates, 0.16-5mM ATP
farnesyl thiodiphosphate		Rn	Inhibition	6.3	pK_i	26
⤷	pK_i 6.3 (K_i 4.73x10^-7 M) [26] Description: Spectrophotometric in vitro assay Conditions: 30°C, pH 7.5. ATP concentration varied from 0.02-5mM, mevalonate concentration varied from 0.02 to 0.6mM
trans,trans-farnesyl diphosphate		Rn	Feedback inhibition	5.6 – 6.5	pK_i	24,26
⤷	pK_i 6.5 (K_i 3.48x10^-7 M) [26] Description: spectrophotometric in vitro assay Conditions: Substrate concentrations: ATP concentration varied from 0.02-5mM, mevalonate concentration vaired from 0.02 to 0.6mM pK_i 5.6 (K_i 2.5x10^-6 M) [24] Description: in vitro, spectrophotometric assay Conditions: pH 7.0, 25°C. Concentration of FPP varied (2µM and 6µM). MgATP^2- concentration varied between 0.2-2mM.
isopentenyl diphosphate		Hs	Feedback inhibition	4.8	pK_i	9
⤷	pK_i 4.8 (K_i 1.6x10^-5 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Saturating concentrations of substrates, 0.16-5mM ATP
dimethylallyl diphosphate		Hs	Competitive	4.7	pK_i	9
⤷	pK_i 4.7 (K_i 2x10^-5 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Saturating concentrations of substrates, 0.16-5mM ATP
farnesol		Hs	Competitive	4.1	pK_i	9
⤷	pK_i 4.1 (K_i 7.2x10^-5 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Saturating concentrations of substrates, 0.16-5mM ATP
dolichol phosphate		Hs	Competitive	4.1	pK_i	9
⤷	pK_i 4.1 (K_i 8.3x10^-5 M) [9] Description: recombinant enzyme expressed in E coli cells. Spectrophotometric assay Conditions: pH 7.0, 25°C. Saturating concentrations of substrates, 0.16-5mM ATP
geranyl diphosphate		Rn	Feedback inhibition	5.3	pIC₅₀	22
⤷	pIC₅₀ 5.3 (IC₅₀ 5x10^-6 M) [22] Description: in vitro assay, enzyme expressed in E coli, purified Conditions: pH 7.0-8.0, 30 ºC. Substrate concentrations: 4mM ATP, 3mM RS-mevalonate, 0.16mM NADH
(RS)-5-diphosphomevalonate		Rn	Feedback inhibition	3.7	pIC₅₀	22
⤷	pIC₅₀ 3.7 (IC₅₀ 1.8x10^-4 M) [22] Description: in vitro assay, enzyme expressed in E coli, purified Conditions: pH 7.0-8.0, temp 30 ºC. Concentration of substrates: 4mM ATP, 3mM RS-mevalonate, 0.16mM NADH.

View species-specific inhibitor tables

Immuno Process Associations

Immuno Process:

Inflammation

Immuno Process:

Immune regulation

Tissue Distribution

Liver, kidney, brain and heart tissue

Expression level:	High
Species:	Human
Technique:	Northern blot
References:	19

Liver

Species:	Human
Technique:	Immunocytochemistry
References:	14

Liver, kidney, brain and heart tissue

Expression level:	High
Species:	Mouse
Technique:	Northern blot
References:	19

Clinically-Relevant Mutations and Pathophysiology

Disease:

Hyper-IgD syndrome

Synonyms:	Hyperimmunoglobulinemia D with periodic fever [Orphanet: ORPHA343]
OMIM:	260920
Orphanet:	ORPHA343

References:

15-16

Click column headers to sort

Type	Species	Amino acid change	Nucleotide change	Description	Reference
Missense	Human	H20Q	60T>A		5
Missense	Human	H20N	149C>A		4
Missense	Human	H20P	150A>C		4,16-17
Missense	Human	L39P	116T>C		4,16
Missense	Human	V132I	394G>A		5
Missense	Human	S135L	404C>T		16
Missense	Human	A148T	442G>T		5,16
Missense	Human	S150L	540C>T		4
Missense	Human	P167L	591C>T		4,6
Missense	Human	G171R	511G>A		5
Missense	Human	G202R	695G>A		4
Missense	Human	G211E	632G>A		5
Missense	Human	R215Q	735G>A		4-5
Missense	Human	V250I	748G>A		5
Missense	Human	L265R	794T>G		5
Missense	Human	I268T	803T>C		4-6,10,16-17
Missense	Human	G309S	1016G>A		4
Missense	Human	V310M	928G>A		5,16,18
Missense	Human	G326R	1067G>A		4
Missense	Human	G376V	1127G>T		5
Missense	Human	V377I	1129G>A	This is the most frequent mutation in Hyper-IgD syndrome	4-6,16-17

Disease:

Mevalonic aciduria

Disease Ontology:	DOID:0050452
OMIM:	610377
Orphanet:	ORPHA29

References:

12-13

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Type	Species	Amino acid change	Nucleotide change	Description	Reference
Missense	Human	H20P	59A>C	Compound heterozygosity for the nucleotide transversion with 1129G>A (V377I)	4,16-17
Missense	Human	T243I	728C>T		10
Missense	Human	L264F	790C>T		10,16
Missense	Human	L265P	794T>C	This mutation leads to a significant increase in the quantity of MVK protein produced.	10
Missense	Human	I268T	803T>C		4-6,10,16-17
Missense	Human	N301T	902A>C	The presence of the missense mutation in the patient was confirmed by PCR amplification	23
Missense	Human	V310M	928G>A		5,16,18
Missense	Human	A334T	1000G>A		4,16,18

Disease:

Porokeratosis 3, disseminated superficial actinic type; POROK3

Synonyms:	Disseminated superficial actinic porokeratosis [Orphanet: ORPHA79152]
OMIM:	175900
Orphanet:	ORPHA79152

References:

Click column headers to sort

Type	Species	Amino acid change	Nucleotide change	Description	Reference
Missense	Human	L41P	122T>C	Heterozygous nucleotide transition in exon 3 of the MVK gene	27
Missense	Human	L225P	764T>C	Heterozygous nucleotide transition in exon 8 of the MVK gene	27
Missense	Human	F364S	1094T>C	Heterozygous nucleotide transition in exon 11 of the MVK gene.	27
Splice site	Human	L348IfsX17	c.1039+2T>C	The insertion of 11 bp at the splice donor site in intron 10 results in a frameshift and premature truncation of the protein	27

General Comments
Deficiency in mevalonate kinase causes metabolic inflammatory disease [25].

References

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1. Chu X, Li D. (2003) Cloning, expression, and purification of His-tagged rat mevalonate kinase. Protein Expr Purif, 27 (1): 165-70. [PMID:12509999]

2. Chu X, Li D. (2003) Expression, purification, and characterization of His20 mutants of rat mevalonate kinase. Protein Expr Purif, 32 (1): 75-82. [PMID:14680942]

3. Chu X, Yu W, Wu L, Liu X, Li N, Li D. (2007) Effect of a disulfide bond on mevalonate kinase. Biochim Biophys Acta, 1774 (12): 1571-81. [PMID:17964869]

4. Cuisset L, Drenth JP, Simon A, Vincent MF, van der Velde Visser S, van der Meer JW, Grateau G, Delpech M, International Hyper-IgD Study Group. (2001) Molecular analysis of MVK mutations and enzymatic activity in hyper-IgD and periodic fever syndrome. Eur J Hum Genet, 9 (4): 260-6. [PMID:11313769]

5. D'Osualdo A, Picco P, Caroli F, Gattorno M, Giacchino R, Fortini P, Corona F, Tommasini A, Salvi G, Specchia F et al.. (2005) MVK mutations and associated clinical features in Italian patients affected with autoinflammatory disorders and recurrent fever. Eur J Hum Genet, 13 (3): 314-20. [PMID:15536479]

6. Drenth JP, Cuisset L, Grateau G, Vasseur C, van de Velde-Visser SD, de Jong JG, Beckmann JS, van der Meer JW, Delpech M. (1999) Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group. Nat Genet, 22 (2): 178-81. [PMID:10369262]

7. Fu Z, Voynova NE, Herdendorf TJ, Miziorko HM, Kim JJ. (2008) Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism. Biochemistry, 47 (12): 3715-24. [PMID:18302342]

8. Gibson KM, Hoffmann GF, Tanaka RD, Bishop RW, Chambliss KL. (1997) Mevalonate kinase map position 12q24. Chromosome Res, 5 (2): 150. [PMID:9146921]

9. Hinson DD, Chambliss KL, Toth MJ, Tanaka RD, Gibson KM. (1997) Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J Lipid Res, 38 (11): 2216-23. [PMID:9392419]

10. Hinson DD, Ross RM, Krisans S, Shaw JL, Kozich V, Rolland MO, Divry P, Mancini J, Hoffmann GF, Gibson KM. (1999) Identification of a mutation cluster in mevalonate kinase deficiency, including a new mutation in a patient of Mennonite ancestry. Am J Hum Genet, 65 (2): 327-35. [PMID:10417275]

11. Hoffmann F, Lohse P, Stojanov S, Shin YS, Renner ED, Kéry A, Zellerer S, Belohradsky BH. (2005) Identification of a novel mevalonate kinase gene mutation in combination with the common MVK V377I substitution and the low-penetrance TNFRSF1A R92Q mutation. Eur J Hum Genet, 13 (4): 510-2. [PMID:15657603]

12. Hoffmann G, Gibson KM, Brandt IK, Bader PI, Wappner RS, Sweetman L. (1986) Mevalonic aciduria--an inborn error of cholesterol and nonsterol isoprene biosynthesis. N Engl J Med, 314 (25): 1610-4. [PMID:3012338]

13. Hoffmann GF, Charpentier C, Mayatepek E, Mancini J, Leichsenring M, Gibson KM, Divry P, Hrebicek M, Lehnert W, Sartor K. (1993) Clinical and biochemical phenotype in 11 patients with mevalonic aciduria. Pediatrics, 91 (5): 915-21. [PMID:8386351]

14. Hogenboom S, Tuyp JJ, Espeel M, Koster J, Wanders RJ, Waterham HR. (2004) Mevalonate kinase is a cytosolic enzyme in humans. J Cell Sci, 117 (Pt 4): 631-9. [PMID:14730012]

15. Houten SM, Frenkel J, Rijkers GT, Wanders RJ, Kuis W, Waterham HR. (2002) Temperature dependence of mutant mevalonate kinase activity as a pathogenic factor in hyper-IgD and periodic fever syndrome. Hum Mol Genet, 11 (25): 3115-24. [PMID:12444096]

16. Houten SM, Koster J, Romeijn GJ, Frenkel J, Di Rocco M, Caruso U, Landrieu P, Kelley RI, Kuis W, Poll-The BT et al.. (2001) 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, 9 (4): 253-9. [PMID:11313768]

17. Houten SM, Kuis W, Duran M, de Koning TJ, van Royen-Kerkhof A, Romeijn GJ, Frenkel J, Dorland L, de Barse MM, Huijbers WA et al.. (1999) Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat Genet, 22 (2): 175-7. [PMID:10369261]

18. Houten SM, Romeijn GJ, Koster J, Gray RG, Darbyshire P, Smit GP, de Klerk JB, Duran M, Gibson KM, Wanders RJ et al.. (1999) Identification and characterization of three novel missense mutations in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of isoprene biosynthesis. Hum Mol Genet, 8 (8): 1523-8. [PMID:10401001]

19. Murphy C, Murray AM, Meaney S, Gåfvels M. (2007) Regulation by SREBP-2 defines a potential link between isoprenoid and adenosylcobalamin metabolism. Biochem Biophys Res Commun, 355 (2): 359-64. [PMID:17300749]

20. Potter D, Miziorko HM. (1997) Identification of catalytic residues in human mevalonate kinase. J Biol Chem, 272 (41): 25449-54. [PMID:9325256]

21. Potter D, Wojnar JM, Narasimhan C, Miziorko HM. (1997) Identification and functional characterization of an active-site lysine in mevalonate kinase. J Biol Chem, 272 (9): 5741-6. [PMID:9038186]

22. Qiu Y, Li D. (2006) Bifunctional inhibitors of mevalonate kinase and mevalonate 5-diphosphate decarboxylase. Org Lett, 8 (6): 1013-6. [PMID:16524256]

23. Schafer BL, Bishop RW, Kratunis VJ, Kalinowski SS, Mosley ST, Gibson KM, Tanaka RD. (1992) Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria. J Biol Chem, 267 (19): 13229-38. [PMID:1377680]

24. Tanaka RD, Schafer BL, Lee LY, Freudenberger JS, Mosley ST. (1990) Purification and regulation of mevalonate kinase from rat liver. J Biol Chem, 265 (4): 2391-8. [PMID:2153681]

25. van der Burgh R, Ter Haar NM, Boes ML, Frenkel J. (2013) Mevalonate kinase deficiency, a metabolic autoinflammatory disease. Clin Immunol, 147 (3): 197-206. [PMID:23110805]

26. Voynova NE, Rios SE, Miziorko HM. (2004) Staphylococcus aureus mevalonate kinase: isolation and characterization of an enzyme of the isoprenoid biosynthetic pathway. J Bacteriol, 186 (1): 61-7. [PMID:14679225]

27. Zhang SQ, Jiang T, Li M, Zhang X, Ren YQ, Wei SC, Sun LD, Cheng H, Li Y, Yin XY et al.. (2012) Exome sequencing identifies MVK mutations in disseminated superficial actinic porokeratosis. Nat Genet, 44 (10): 1156-60. [PMID:22983302]

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