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Ligand (R)-mevalonate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

mevalonate metabolism

KEGG

Biosynthesis of plant hormones, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of terpenoids and steroids, Ferroptosis, Terpenoid backbone biosynthesis more

MetaCyc

isoprene biosynthesis II (engineered), mevalonate degradation, mevalonate pathway I (eukaryotes and bacteria), mevalonate pathway II (haloarchaea), mevalonate pathway III (Thermoplasma), mevalonate pathway IV (archaea) more

Show all BRENDA pathways known for (R)-mevalonate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+

740956, 740265, 761539, 740970, 740983, 741192, 760659

-

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 740104

1r31, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 740104

4i6y, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 740104

6eev, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

1r31, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

4i6y, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

6eev, 3D-view

1.1.1.88

6 entries

2.7.1.185

ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate

759486, 730902, 758668, 760079, 727046, 727978, 729049

-

2.7.1.36

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate

673439, 672817, 760041, 759225, 759158, 759694, 707737, 739684, 738399, 757716, 759224, 662499, 662019, 663293, 663334, 676284, 677036, 708647, 739434

2hfu, 3D-view

2.7.1.36

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate

673439, 672817, 760041, 759225, 759158, 759694, 707737, 739684, 738399, 757716, 759224, 662499, 662019, 663293, 663334, 676284, 677036, 708647, 739434

6mde, 3D-view

2.7.1.36

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (11 results)

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Show Natural Product (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + 2 NADP+ + CoA

0

-

1.1.1.34

(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + NADPH = (R)-mevalonate + CoA + NADP+

0

-

1.1.1.34

D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

-

1.1.1.34

mevaldyl-CoA + NADPH + H+ + H2O = (R)-mevalonate + CoA + NADP+

0

-

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

1r31, 3D-view

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

4i6y, 3D-view

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

6eev, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

1r31, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

4i6y, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

6eev, 3D-view

1.1.1.34

5 entries

1.1.1.88

6 entries

Substrate in Enzyme-catalyzed Reactions (64 results)

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Show Substrate (64 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

(R)-mevalonate + CoA + 2 NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+

740956, 286586, 740265, 761539, 740970, 740983, 741192, 760659

-

1.1.1.34

(R)-mevalonate + CoA + NADP+ = (S)-3-hydroxy-3-methylglutaryl-CoA + NADPH + H+

286586

-

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 287503, 287495, 287500, 287502, 287506, 287496, 287498, 287499, 740104, 287504, 287497

1r31, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 287503, 287495, 287500, 287502, 287506, 287496, 287498, 287499, 740104, 287504, 287497

4i6y, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = (S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

761340, 287503, 287495, 287500, 287502, 287506, 287496, 287498, 287499, 740104, 287504, 287497

6eev, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

1r31, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

4i6y, 3D-view

1.1.1.88

(R)-mevalonate + CoA + 2 NAD+ = 3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+

723092, 760603

6eev, 3D-view

1.1.1.88

(R)-mevalonate + CoA + NADP+ = 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+

287505

1r31, 3D-view

1.1.1.88

(R)-mevalonate + CoA + NADP+ = 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+

287505

4i6y, 3D-view

1.1.1.88

(R)-mevalonate + CoA + NADP+ = 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+

287505

6eev, 3D-view

1.1.1.34

2 entries

1.1.1.88

9 entries

2.7.1.185

ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate

759486, 727046, 727978, 730902, 758668, 729049, 760079

-

2.7.1.36

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate

662019, 708647, 662499, 673439, 641439, 663293, 676284, 691055, 641432, 641436, 672817, 663334, 721347, 760041, 759225, 690941, 759158, 759694, 707737, 721225, 727840, 739684, 738399, 757716, 759224, 677036, 722571, 739434

2hfu, 3D-view

2.7.1.36

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate

662019, 708647, 662499, 673439, 641439, 663293, 676284, 691055, 641432, 641436, 672817, 663334, 721347, 760041, 759225, 690941, 759158, 759694, 707737, 721225, 727840, 739684, 738399, 757716, 759224, 677036, 722571, 739434

6mde, 3D-view

2.7.1.36

Ca-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Ca-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Ca-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Ca-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Cd-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Co-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Co-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Co-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Co-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Co-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Co-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Co-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Co-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

CTP + (R)-mevalonate = CDP + (R)-5-phosphomevalonate

663334, 739434

2hfu, 3D-view

2.7.1.36

CTP + (R)-mevalonate = CDP + (R)-5-phosphomevalonate

663334, 739434

6mde, 3D-view

2.7.1.36

GTP + (R)-mevalonate = GDP + (R)-5-phosphomevalonate

663334, 739434

2hfu, 3D-view

2.7.1.36

GTP + (R)-mevalonate = GDP + (R)-5-phosphomevalonate

663334, 739434

6mde, 3D-view

2.7.1.36

ITP + (R)-mevalonate = IDP + (R)-5-phosphomevalonate

663334

2hfu, 3D-view

2.7.1.36

ITP + (R)-mevalonate = IDP + (R)-5-phosphomevalonate

663334

6mde, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(1-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(1-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mg-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Mn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Mn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Mn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Ni-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Ni-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Ni-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Ni-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

TTP + (R)-mevalonate = TDP + (R)-5-phosphomevalonate

663334, 739434

2hfu, 3D-view

2.7.1.36

TTP + (R)-mevalonate = TDP + (R)-5-phosphomevalonate

663334, 739434

6mde, 3D-view

2.7.1.36

UTP + (R)-mevalonate = UDP + (R)-5-phosphomevalonate

663334

2hfu, 3D-view

2.7.1.36

UTP + (R)-mevalonate = UDP + (R)-5-phosphomevalonate

663334

6mde, 3D-view

2.7.1.36

Zn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Zn-adenosine 5'-O-(2-thio-(R)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

Zn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

2hfu, 3D-view

2.7.1.36

Zn-adenosine 5'-O-(2-thio-(S)-triphosphate) + (R)-mevalonate = ?

641441

6mde, 3D-view

2.7.1.36

52 entries

Product in Enzyme-catalyzed Reactions (19 results)

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Show Product (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.32

mevaldate + NADH + H+ = (R)-mevalonate + NAD+

0

-

1.1.1.33

(3RS)-mevaldate + NADPH + H+ = (R)-mevalonate + NADP+

0

-

1.1.1.34

(R)-mevaldehyde + NADPH + H+ = (R)-mevalonate + NADP+

0

-

1.1.1.34

(R,S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

-

1.1.1.34

(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + 2 NADP+ + CoA

0

-

1.1.1.34

(S)-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + NADPH = (R)-mevalonate + CoA + NADP+

0

-

1.1.1.34

D-3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

-

1.1.1.34

mevaldehyde + NADPH + H+ = (R)-mevalonate + NADP+

0

-

1.1.1.34

mevaldyl-CoA + NADPH + H+ + H2O = (R)-mevalonate + CoA + NADP+

0

-

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

1r31, 3D-view

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

4i6y, 3D-view

1.1.1.88

(S)-3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = (R)-mevalonate + NAD+ + CoA

0

6eev, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

1r31, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

4i6y, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADH + 2 H+ = (R)-mevalonate + CoA + 2 NAD+

0

6eev, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

1r31, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

4i6y, 3D-view

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = (R)-mevalonate + CoA + 2 NADP+

0

6eev, 3D-view

1.1.1.34

8 entries

1.1.1.88

9 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (15 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (15 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.88

1r31, 3D-view

1.1.1.88

4i6y, 3D-view

1.1.1.88

6eev, 3D-view

1.1.1.88

1r31, 3D-view

1.1.1.88

4i6y, 3D-view

1.1.1.88

6eev, 3D-view

1.1.1.88

1r31, 3D-view

1.1.1.88

4i6y, 3D-view

1.1.1.88

6eev, 3D-view

2.7.1.36

2hfu, 3D-view

2.7.1.36

6mde, 3D-view

2.7.1.36

2hfu, 3D-view

2.7.1.36

6mde, 3D-view

2.7.1.36

2hfu, 3D-view

2.7.1.36

6mde, 3D-view

1.1.1.88

9 entries

2.7.1.36

6 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (18 results)

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Show Turnover Number (18 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.7.1.185

0.31

-

pH 8.5, 55°C, mutant enzyme R185K

730902

2.7.1.185

1.16

-

pH 8.5, 55°C, mutant enzyme S105A

730902

2.7.1.185

1.9

-

pH 7.5, 30°C

729049

2.7.1.185

5

-

pH 8.5, 55°C

727046

2.7.1.185

5.1

-

pH 8.5, 55°C, mutant enzyme L18A

730902

2.7.1.185

5.3

-

pH 8.5, 55°C, wild-type enzyme

730902

2.7.1.185

5.8

-

pH 8.5, 55°C, mutant enzyme T275A

730902

2.7.1.36

3.1

-

mutant C107S/C281S, pH 7.5, 34°C

691055

2.7.1.36

4.3

-

in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C

721347

2.7.1.36

5.2

-

mutant A141C, pH 7.5, 34°C

691055

2.7.1.36

8.6

-

mutant C107A/C281A, pH 7.5, 34°C

691055

2.7.1.36

10.5

-

mutant C107S, pH 7.5, 34°C

691055

2.7.1.36

12.7

-

mutant C281S, pH 7.5, 34°C

691055

2.7.1.36

17.1

-

mutant C107A, pH 7.5, 34°C

691055

2.7.1.36

21.9

-

wild-type, pH 7.5, 34°C

691055

2.7.1.36

23.3

-

mutant C281A, pH 7.5, 34°C

691055

2.7.1.36

28.5

-

wild-type, pH 7.5, 34°C

691055

2.7.1.36

143.8

-

at pH 7.0 and 30°C

738399

2.7.1.185

7 entries

2.7.1.36

11 entries

K_M Value (39 results)

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Show KM Value (39 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.34

0.0015

-

pH 9.0, 50°C, wild-type

286586

1.1.1.34

0.0015

-

wild type enzyme, at pH 9.0 and 50°C

286586

1.1.1.34

0.0017

-

mutant enzyme L403R/G404R/A406S, at pH 9.0 and 50°C

286586

1.1.1.34

0.0017

-

pH 9.0, 50°C, mutnant L403R/G404R/A406S

286586

1.1.1.34

0.252

-

pH 8.3, 25°C

655549

1.1.1.34

1

-

pH 6.5, 37°C, oxidation

487702

1.1.1.34

6 entries

1.1.1.88

0.15

-

oxidative acylation of mevalonate

287498

2.7.1.185

0.097

-

pH 8.5, 55°C

727046

2.7.1.185

0.13

-

pH 8.5, 55°C, wild-type enzyme

730902

2.7.1.185

0.131

-

pH 7.5, 30°C

729049

2.7.1.185

0.27

-

pH 8.5, 55°C, mutant enzyme S105A

730902

2.7.1.185

0.59

-

pH 8.5, 55°C, mutant enzyme T275A

730902

2.7.1.185

1.68

-

pH 8.5, 55°C, mutant enzyme R185K

730902

2.7.1.185

3.1

-

pH 8.5, 55°C, mutant enzyme L18A

730902

2.7.1.36

0.0324

-

mutant T104A, 30°C, pH 7.5

690941

2.7.1.36

0.035

-

native enzyme, pH 7.5, 25°C

663293

2.7.1.36

0.035

-

wild-type, pH 7.5, 34°C

691055

2.7.1.36

0.0408

-

wild-type, 30°C, pH 7.5

690941

2.7.1.36

0.0459

-

mutant R388X, 30°C, pH 7.5

690941

2.7.1.36

0.0473

-

mutant L54A, 30°C, pH 7.5

690941

2.7.1.36

0.061

-

mutant C281S, pH 7.5, 34°C

691055

2.7.1.36

0.068

-

apparent value, in 50 mM Tris, 50 mM NaCl (pH 7.6), at 30°C

721347

2.7.1.36

0.07

-

mutant C107A, pH 7.5, 34°C

691055

2.7.1.36

0.071

-

mutant C107A/C281A, pH 7.5, 34°C

691055

2.7.1.36

0.0745

-

mutant T104A/I196A, 30°C, pH 7.5

690941

2.7.1.36

0.076

-

mutant C107S, pH 7.5, 34°C

691055

2.7.1.36

0.09

-

at pH 7.5, temperature not specified in the publication

739434

2.7.1.36

0.106

-

mutant C281A, pH 7.5, 34°C

691055

2.7.1.36

0.106

-

wild-type, pH 7.5, 34°C

691055

2.7.1.36

0.111

-

mutant C107S/C281S, pH 7.5, 34°C

691055

2.7.1.36

0.1163

-

mutant I196A, 30°C, pH 7.5

690941

2.7.1.36

0.186

-

mutant A141C, pH 7.5, 34°C

691055

2.7.1.36

0.228

-

mutant I56A, 30°C, pH 7.5

690941

2.7.1.36

0.323

-

mutant Y149A, 30°C, pH 7.5

690941

2.7.1.36

0.33

-

pH 10, 37°C

663334

2.7.1.36

0.3319

-

at pH 7.0 and 30°C

738399

2.7.1.36

0.4591

-

mutant T104A/I196A/R388X, 30°C, pH 7.5

690941

2.7.1.36

0.616

-

H20L mutant enzyme, pH 7.5, 25°C

663293

2.7.1.36

2.16

-

H20Y mutant enzyme, pH 7.5, 25°C

663293

2.7.1.185

7 entries

2.7.1.36

25 entries

References & Links

Literature References (61)

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Show Reference (61 entries)

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PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

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Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase

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Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion

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Proc. Natl. Acad. Sci. USA

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Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 Angstrom resolution

1995

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Structural determinants of nucleotide coenzyme specificity in the distinctive dinucleotide binding fold of HMG-CoA reductase from Pseudomonas mevalonii

1996

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Biochemistry

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287506

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Active form of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase

1997

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Biochem. Mol. Med.

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487702

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Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme A reductase, a dual-function protein of isopentenyl diphosphate biosynthesis

2002

Hedl, M.; Sutherlin, A.; Wilding, E.I.; Mazzulla, M.; McDevitt, D.; Lane, P.; Burgner, J.W.; Lehnbeuter, K.R.; Stauffacher, C.V.; Gwynn, M.N.; Rodwell, V.W.

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641432

2991706

Mevalonate kinase

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An improved purification procedure, an alternative assay and activation of mevalonate kinase by ATP

1983

Soong Lee, C.; O'Sullivan, W.J.

Biochim. Biophys. Acta

747

215-224

641439

2153681

Purification and regulation of mevalonate kinase from rat liver

1990

Tanaka, R.D.; Schafer, B.L.; Lee, L.Y.; Freudenberger, J.S.; Mosley, S.T.

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641441

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Phosphorothioate analogues of adenosine triphosphate as substrates of the mevalonate kinase reaction

1984

Soong Lee, C.; O'Sullivan, W.J.O.

Biochim. Biophys. Acta

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655549

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Kinetic properties and inhibition of Trypanosoma cruzi 3-hydroxy-3-methylglutaryl CoA reductase

2002

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FEBS Lett.

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Staphylococcus aureus mevalonate kinase: isolation and characterization of an enzyme of the isoprenoid biosynthetic pathway

2004

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J. Bacteriol.

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61-67

662499

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Mevalonate kinase is a cytosolic enzyme in humans

2004

Hogenboom, S.; Tuyp, J.J.; Espeel, M.; Koster, J.; Wanders, R.J.; Waterham, H.R.

J. Cell Sci.

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631-639

663293

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Expression, purification, and characterization of His20 mutants of rat mevalonate kinase

2003

Chu, X.; Li, D.

Protein Expr. Purif.

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75-82

663334

14767074

Enterococcus faecalis mevalonate kinase

2004

Hedl, M.; Rodwell, V.W.

Protein Sci.

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672817

17397541

Structure, substrate recognition and reactivity of Leishmania major mevalonate kinase

2007

Sgraja, T.; Smith, T.K.; Hunter, W.N.

BMC Struct. Biol.

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20

673439

15657603

Identification of a novel mevalonate kinase gene mutation in combination with the common MVK V377I substitution and the low-penetrance TNFRSF1A R92Q mutation

2005

Hoffmann, F.; Lohse, P.; Stojanov, S.; Shin, Y.S.; Renner, E.D.; Kery, A.; Zellerer, S.; Belohradsky, B.H.

Eur. J. Hum. Genet.

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Bifunctional inhibitors of mevalonate kinase and mevalonate 5-diphosphate decarboxylase

2006

Qiu, Y.; Li, D.

Org. Lett.

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1013-1016

677036

17400916

Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate

2007

Andreassi, J.L.; Bilder, P.W.; Vetting, M.W.; Roderick, S.L.; Leyh, T.S.

Protein Sci.

16

983-989

690941

18302342

Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism

2008

Fu, Z.; Voynova, N.E.; Herdendorf, T.J.; Miziorko, H.M.; Kim, J.J.

Biochemistry

47

3715-3724

691055

17964869

Effect of a disulfide bond on mevalonate kinase

2007

Chu, X.; Yu, W.; Wu, L.; Liu, X.; Li, N.; Li, D.

Biochim. Biophys. Acta

1774

1571-1581

707737

20056424

Mevalonate analogues as substrates of enzymes in the isoprenoid biosynthetic pathway of Streptococcus pneumoniae

2009

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1124-1134

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19672814

Parathyroid hormone upregulates BMP-2 mRNA expression through mevalonate kinase and Rho kinase inhibition in osteoblastic MC3T3-E1 cells

2009

Takase, H.; Yano, S.; Yamaguchi, T.; Kanazawa, I.; Hayashi, K.; Yamamoto, M.; Yamauchi, M.; Sugimoto, T.

Horm. Metab. Res.

41

861-865

721225

23192048

Crystallization and preliminary X-ray diffraction analysis of mevalonate kinase from Methanosarcina mazei

2012

Zhuang, N.; Seo, K.H.; Chen, C.; Zhou, J.; Kim, S.W.; Lee, K.H.

Acta Crystallogr. Sect. F

68

1560-1563

721347

21908638

Characterization of a feedback-resistant mevalonate kinase from the archaeon Methanosarcina mazei

2011

Primak, Y.A.; Du, M.; Miller, M.C.; Wells, D.H.; Nielsen, A.T.; Weyler, W.; Beck, Z.Q.

Appl. Environ. Microbiol.

77

7772-7778

722571

23378249

Biochemical evidence supporting the presence of the classical mevalonate pathway in the thermoacidophilic archaeon Sulfolobus solfataricus

2013

Nishimura, H.; Azami, Y.; Miyagawa, M.; Hashimoto, C.; Yoshimura, T.; Hemmi, H.

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723092

21810477

Optimization of a heterologous mevalonate pathway through the use of variant HMG-CoA reductases

2011

Ma, S.M.; Garcia, D.E.; Redding-Johanson, A.M.; Friedland, G.D.; Chan, R.; Batth, T.S.; Haliburton, J.R.; Chivian, D.; Keasling, J.D.; Petzold, C.J.; Lee, T.S.; Chhabra, S.R.

Metab. Eng.

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727046

24914732

Evidence of a novel mevalonate pathway in archaea

2014

Vinokur, J.M.; Korman, T.P.; Cao, Z.; Bowie, J.U.

Biochemistry

53

4161-4168

727840

11751891

Structure of the Methanococcus jannaschii mevalonate kinase, a member of the GHMP kinase superfamily

2002

Yang, D.; Shipman, L.W.; Roessner, C.A.; Scott, A.I.; Sacchettini, J.C.

J. Biol. Chem.

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727978

24755225

(R)-Mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum

2014

Azami, Y.; Hattori, A.; Nishimura, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.

J. Biol. Chem.

289

15957-15967

729049

25636853

The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene

2015

Rossoni, L.; Hall, S.J.; Eastham, G.; Licence, P.; Stephens, G.

Appl. Environ. Microbiol.

81

2625-2634

730902

25422158

Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases

2015

Vinokur, J.M.; Korman, T.P.; Sawaya, M.R.; Collazo, M.; Cascio, D.; Bowie, J.U.

Protein Sci.

24

212-220

738399

25281875

Biochemical characterization of recombinant mevalonate kinase from Bacopa monniera

2015

Kumari, U.; Vishwakarma, R.K.; Sonawane, P.; Abbassi, S.; Khan, B.M.

Int. J. Biol. Macromol.

72

776-783

739434

26566274

Negative feedbacks by isoprenoids on a mevalonate kinase expressed in the corpora allata of mosquitoes

2015

Nyati, P.; Rivera-Perez, C.; Noriega, F.G.

PLoS ONE

10

e0143107

739684

27113535

Unique behavior of Trypanosoma cruzi mevalonate kinase: A conserved glycosomal enzyme involved in host cell invasion and signaling

2016

Ferreira, E.R.; Horjales, E.; Bonfim-Melo, A.; Cortez, C.; da Silva, C.V.; De Groote, M.; Sobreira, T.J.; Cruz, M.C.; Lima, F.M.; Cordero, E.M.; Yoshida, N.; da Silveira, J.F.; Mortara, R.A.; Bahia, D.

Sci. Rep.

6

24610

740104

24316250

Kinetic characterization of an oxidative, cooperative HMG-CoA reductase from Burkholderia cenocepacia

2014

Schwarz, B.H.; Driver, J.; Peacock, R.B.; Dembinski, H.E.; Corson, M.H.; Gordon, S.S.; Watson, J.M.

Biochim. Biophys. Acta

1844

457-464

740265

-

QM/MM study of the mechanism of reduction of 3-hydroxy-3-methylglutaryl coenzyme A catalyzed by human HMG-CoA reductase

2016

Oliveira, E.F.; Cerqueira, N.M.F.S.A.; Ramos, M.J.; Fernandes, P.A.

Catal. Sci. Technol.

6

7172-7185

740956

24777788

Determination of 3-hydroxy-3-methylglutaryl CoA reductase activity in plants

2014

Campos, N.; Arro, M.; Ferrer, A.; Boronat, A.

Methods Mol. Biol.

1153

21-40

740970

24239940

Exploring Leishmania donovani 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) as a potential drug target by biochemical, biophysical and inhibition studies

2014

Dinesh, N.; Pallerla, D.S.R.; Kaur, P.K.; Babu, N.K.; Singh, S.

Microb. Pathog.

66

14-23

740983

26311154

Molecular cloning, characterization and expression analysis of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene from Centella asiatica L.

2015

Kalita, R.; Patar, L.; Shasany, A.K.; Modi, M.K.; Sen, P.

Mol. Biol. Rep.

42

1431-1439

741192

26546781

Characterization and function of the 3-hydroxy-3-methylglutaryl-CoA reductase gene in Alisma orientale (Sam.) Juz. and its relationship with protostane triterpene production

2015

Gu, W.; Geng, C.; Xue, W.; Wu, Q.; Chao, J.; Xu, F.; Sun, H.; Jiang, L.; Han, Y.; Zhang, S.

Plant Physiol. Biochem.

97

378-389

757716

28045448

Molecular cloning, characterization, and functional analysis of acetyl-CoA C-acetyltransferase and mevalonate kinase genes involved in terpene trilactone biosynthesis from Ginkgo biloba

2017

Chen, Q.; Yan, J.; Meng, X.; Xu, F.; Zhang, W.; Liao, Y.; Qu, J.

Molecules

22

74

758668

30824437

Conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase by single amino acid mutations

2019

Motoyama, K.; Sobue, F.; Kawaide, H.; Yoshimura, T.; Hemmi, H.

Appl. Environ. Microbiol.

85

e00256-19

759158

32256770

Effects of mevalonate kinase interference on cell differentiation, apoptosis, prenylation and geranylgeranylation of human keratinocytes are attenuated by farnesyl pyrophosphate or geranylgeranyl pyrophosphate

2020

Li, M.; Min, W.; Wang, J.; Wang, L.; Li, Y.; Zhou, N.; Yang, Z.; Qian, Q.

Exp. Therap. Med.

19

2861-2870

759224

29034216

A new trick for a conserved enzyme Mevalonate kinase, a glycosomal enzyme, can be secreted by Trypanosoma cruzi and modulate cell invasion and signaling. Is it another moonlighting enzyme?

2017

Bahia, D.

Front. Cell. Infect. Microbiol.

7

426

759225

30042928

Molecular characterization of Trypanosoma evansi mevalonate kinase (TeMVK)

2018

Duarte, D.P.; Ferreira, E.R.; Lima, F.M.; Batista, F.; De Groote, M.; Horjales, E.; Miletti, L.C.; Bahia, D.

Front. Cell. Infect. Microbiol.

8

223

759486

28003359

A single amino acid mutation converts (R)-5-diphosphomevalonate decarboxylase into a kinase

2017

Motoyama, K.; Unno, H.; Hattori, A.; Takaoka, T.; Ishikita, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.

J. Biol. Chem.

292

2457-2469

759694

29693064

Novel mevalonate kinase missense mutation in a patient with disseminated superficial actinic porokeratosis

2018

Glinos, G.; Pastar, I.; Giubellino, A.; Tomic-Canic, M.; Miteva, M.; Stone, R.

JAAD Case Rep.

4

340-343

760041

30521590

Structural insight into substrate and product binding in an archaeal mevalonate kinase

2018

Miller, B.R.; Kung, Y.

PLoS ONE

13

e0208419

760079

31872250

Attempts to develop an enzyme converting DHIV to KIV

2019

Oki, K.; Lee, F.S.; Mayo, S.L.

Protein Eng. Des. Sel.

32

261-270

760603

31469273

Structural and functional characterization of dynamic oligomerization in Burkholderia cenocepacia HMG-CoA reductase

2019

Peacock, R.B.; Hicks, C.W.; Walker, A.M.; Dewing, S.M.; Lewis, K.M.; Abboud, J.C.; Stewart, S.W.A.; Kang, C.; Watson, J.M.

Biochemistry

58

3960-3970

760659

28469419

An insight into structure, function, and expression analysis of 3-hydroxy-3-methylglutaryl-CoA reductase of Cymbopogon winterianus

2017

Devi, K.; Patar, L.; Modi, M.K.; Sen, P.

Bioinform. Biol. Insights

11

1177932217701735

761340

30969121

Soybean peptides exert multifunctional bioactivity modulating 3-hydroxy-3-methylglutaryl-CoA reductase and dipeptidyl peptidase-IV targets in vitro

2019

Lammi, C.; Arnoldi, A.; Aiello, G.

J. Agric. Food Chem.

67

4824-4830

761539

30470158

Computational study of conformational changes in human 3-hydroxy-3-methylglutaryl coenzyme reductase induced by substrate binding

2019

Costa, C.H.S.; Oliveira, A.R.S.; Dos Santos, A.M.; da Costa, K.S.; Lima, A.H.L.E.; Alves, C.N.; Lameira, J.

J. Biomol. Struct. Dyn.

37

4374-4383

Links to other databases for (R)-mevalonate

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