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Ligand 3-hydroxy-3-methylglutaryl-CoA

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Biosynthesis of alkaloids derived from terpenoid and polyketide, Biosynthesis of plant hormones, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of terpenoids and steroids, Butanoate metabolism, Ferroptosis, HMG-CoA reductase inhibitors, Terpenoid backbone biosynthesis, Valine, leucine and isoleucine degradation more

MetaCyc

ferrichrome A biosynthesis, isoprene biosynthesis II (engineered), ketogenesis, L-leucine degradation I, mevalonate degradation, mevalonate pathway I (eukaryotes and bacteria), mevalonate pathway II (haloarchaea), mevalonate pathway III (Thermoplasma), mevalonate pathway IV (archaea) more

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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

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

712198, 712676, 712189

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = mevalonolactone + CoA + 2 NADP+ + H2O

654375

-

1.1.1.34

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

286587, 286582, 286571, 286576, 286557, 286559, 286560, 286561, 286565, 286567, 286568, 286569, 286572, 286573, 286574, 286566, 286558, 286578, 286580, 286575, 286581, 286577, 286585, 286586, 286579, 286562, 286563, 286583, 286564, 286570, 286584

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + NADPH = mevalonate + CoA + NADP+

700852, 700682

-

1.1.1.34

hydroxymethylglutaryl-CoA + NADPH + H+ = mevalonate + NADP+ + CoA

685581, 687713, 685520, 685531, 688473, 685680, 687094, 689453

-

1.1.1.88

3-hydroxy-3-methyl-glutaryl-CoA + NADH + H+ = mevalonate + CoA + NAD+

654225

-

1.1.1.88

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

760594, 761344

-

1.1.1.B38

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

760596

-

1.1.1.B38

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

760596

-

1.1.1.34

5 entries

1.1.1.88

2 entries

1.1.1.B38

2 entries

3.1.2.27

hydroxymethylglutaryl-CoA + H2O = hydroxymethylglutarate + CoA

646200

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.88

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

-

-

2.8.3.13

succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + 3-hydroxy-3-methylglutaryl-CoA

643832, 643833, 643834

-

Substrate in Enzyme-catalyzed Reactions (28 results)

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Show Substrate (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

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

740970

-

1.1.1.34

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

712198, 712676, 712189

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + 2 NADPH + 2 H+ = mevalonolactone + CoA + 2 NADP+ + H2O

654375

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + NADPH + H+ = mevalonate + CoA + NADP+

669695

-

1.1.1.34

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

286587, 286582, 286571, 286576, 286557, 286559, 286560, 286561, 286565, 286567, 286568, 286569, 286572, 286573, 286574, 286566, 286558, 286578, 286580, 286575, 286581, 286577, 286585, 286586, 286579, 286562, 286563, 286583, 286564, 286570, 286584

-

1.1.1.34

3-hydroxy-3-methylglutaryl-CoA + NADPH = mevalonate + CoA + NADP+

700852, 667627, 700682

-

1.1.1.34

DL-3-hydroxy-3-methylglutaryl-CoA + NADPH = mevalonate + CoA + NADP+

696687

-

1.1.1.34

hydroxymethylglutaryl-CoA + NADPH + H+ = mevalonate + NADP+ + CoA

685581, 687713, 685520, 685531, 688473, 689453, 685680, 687094

-

1.1.1.88

3-hydroxy-3-methyl-glutaryl-CoA + NADH + H+ = mevalonate + CoA + NAD+

656615, 654225

-

1.1.1.88

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

760594, 761344

-

1.1.1.88

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

760594

-

1.1.1.88

3-hydroxy-3-methylglutaryl-CoA + NADH + H+ = mevalonate + CoA + NAD+

287495, 287496, 287497, 287499, 287502, 657303

-

1.1.1.B38

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

760596

-

1.1.1.B38

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

760596

-

1.1.1.34

8 entries

1.1.1.88

4 entries

1.1.1.B38

2 entries

2.3.1.137

3-hydroxy-3-methylglutaryl-CoA + L-carnitine = 3-hydroxy-3-methylglutaryl-L-carnitine + CoA

486292

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + adipate = 3-hydroxy-3-methylglutarate + adipyl-CoA

643834

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + glutarate = 3-hydroxy-3-methylglutarate + glutaryl-CoA

643834, 738808

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + malonate = 3-hydroxy-3-methylglutarate + malonyl-CoA

643834

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + methylmalonate = 3-hydroxy-3-methylglutarate + methylmalonyl-CoA

643834

-

2.8.3.13

3-hydroxy-3-methylglutaryl-CoA + succinate = 3-hydroxy-3-methylglutarate + succinyl-CoA

643834, 738808

-

3.1.2.2

3-hydroxy-3-methyl glutaryl-CoA + H2O = CoA + 3-hydroxy-3-methyl glutarate

646200

-

3.1.2.2

3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate

646200

-

3.1.2.20

3-hydroxy-3-methyl glutaryl-CoA + H2O = CoA + 3-hydroxy-3-methyl glutarate

646200

-

3.1.2.20

3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate

707430, 707486

-

3.1.2.20

DL-3-hydroxy-3-methylglutaryl-CoA + H2O = CoA + 3-hydroxy-3-methylglutarate

732296, 690932

-

2.8.3.13

5 entries

3.1.2.2

2 entries

3.1.2.20

3 entries

3.1.2.27

hydroxymethylglutaryl-CoA + H2O = hydroxymethylglutarate + CoA

646200

-

4.1.3.4

3-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA

5369, 5373, 715529, 5371, 5362, 5366, 5375, 713966

-

4.2.1.18

(R,S)-3-hydroxy-3-methylglutaryl-CoA = ?

679737

-

Product in Enzyme-catalyzed Reactions (14 results)

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Show Product (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.88

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

-

-

1.1.1.88

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

-

-

1.1.1.88

DL-mevalonate + CoA + NADP+ = 3-hydroxy-3-methylglutaryl-CoA + NADPH + H+

-

-

1.1.1.B38

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

-

-

1.1.1.B38

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

-

-

1.1.1.88

3 entries

1.1.1.B38

2 entries

2.3.1.137

beta-hydroxy-beta-methylglutaryl-L-carnitine + CoA = beta-hydroxy-beta-methylglutaryl-CoA + L-carnitine

-

-

2.3.3.10

acetyl-3'-dephospho-CoA + acetoacetyl-CoA + H2O = 3-hydroxy-3-methylglutaryl-CoA + 3'-dephospho-CoA

-

-

2.3.3.10

acetylpantetheine + acetoacetyl-CoA + H2O = 3-hydroxy-3-methylglutaryl-CoA + pantetheine

-

-

2.8.3.13

adipyl-CoA + 3-hydroxy-3-methylglutarate = adipate + 3-hydroxy-3-methylglutaryl-CoA

643834

-

2.8.3.13

butyryl-CoA + 3-hydroxy-3-methylglutarate = butyrate + 3-hydroxy-3-methylglutaryl-CoA

643832

-

2.8.3.13

glutaryl-CoA + 3-hydroxy-3-methylglutarate = glutarate + 3-hydroxy-3-methylglutaryl-CoA

643834

-

2.8.3.13

malonyl-CoA + 3-hydroxy-3-methylglutarate = malonate + 3-hydroxy-3-methylglutaryl-CoA

643832, 643834

-

2.8.3.13

methylmalonyl-CoA + 3-hydroxy-3-methylglutarate = methylmalonate + 3-hydroxy-3-methylglutaryl-CoA

643834

-

2.8.3.13

succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + 3-hydroxy-3-methylglutaryl-CoA

643832, 643833, 643834

-

2.3.3.10

2 entries

2.8.3.13

6 entries

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.34

0.05 mM

286566

-

2.3.3.10

-

701677

-

2.3.3.10

-

488103

-

2.3.3.10

competitive inhibition

488107

-

2.3.3.10

mixed product inhibition

488103

-

2.3.3.10

product inhibition

488105

-

2.3.3.10

uncompetitive inhibition

488091

-

2.3.3.10

-

488091

-

2.3.3.10

7 entries

2.7.11.31

only with hydroxymethylglutaryl-CoA reductase as substrate

644963

-

3.1.3.16

-

134607, 134616

-

3.1.3.47

does not inhibit the reductase phosphatase itself but interacts with the reductase and prevents its activation

94960, 94961

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (7 results)

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Show Turnover Number (7 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.34

0.023

-

-

688473

1.1.1.88

22.3

-

at pH 7.4, temperature not specified in the publication

760594

3.1.2.20

0.007

-

-

707430

3.1.2.20

0.079

-

wild-type protein, pH7.5, 25°C

707486

3.1.2.20

8.9

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

12

-

pH 7.5, 37°C

732296

3.1.2.20

4 entries

4.2.1.18

0.26

-

-

679737

K_M Value (44 results)

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Show KM Value (44 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.34

0.003

-

-

286575

1.1.1.34

0.006

-

only one enantiomer

286559

1.1.1.34

0.008

-

-

286581

1.1.1.34

0.01

-

reductase from tumor

286582

1.1.1.34

0.012

-

-

286559

1.1.1.34

0.014

-

reductase from liver and reductase from tumor

286582

1.1.1.34

0.015

-

reductase from liver, implanted tumor

286582

1.1.1.34

0.017

-

-

286584

1.1.1.34

0.017

-

pH 5.5, 50°C

286584

1.1.1.34

0.019

-

reductase from liver, implanted tumor

286582

1.1.1.34

0.021

-

-

286563

1.1.1.34

0.024

-

reductase from liver

286582

1.1.1.34

0.028

-

-

286580

1.1.1.34

0.0357

-

pH 7.2, 37°C

740970

1.1.1.34

0.04

-

-

286583

1.1.1.34

0.045

-

wild type

286586

1.1.1.34

0.056

-

-

286568

1.1.1.34

0.068

-

-

688473

1.1.1.34

0.07

-

-

667627

1.1.1.34

0.076

-

mutant

286586

1.1.1.34

0.6

-

pH 7.5, temperature not specified in the publication

712198

1.1.1.88

0.00734

-

at pH 7.4, temperature not specified in the publication

760594

1.1.1.88

0.05

-

reductive deacylation to mevalonate

287496, 287497

1.1.1.88

0.3

-

reductive deacylation to mevalonate

287499

2.8.3.13

0.18

-

pH 7.8, 30°C, cosubstrate adipate, reverse reaction

643834

2.8.3.13

0.32

-

pH 7.8, 30°C, cosubstrate succinate or malonate, reverse reaction

643833

2.8.3.13

0.39

-

pH 7.8, 30°C, cosubstrate succinate or glutarate, reverse reaction

643834

2.8.3.13

0.62

-

pH 7.8, 30°C, cosubstrate methylmalonate, reverse reaction

643834

3.1.2.20

0.02

-

pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

690932

3.1.2.20

0.0868

-

pH 7.5, 37°C

732296

3.1.2.20

0.3057

-

-

707430

3.1.2.20

2.9

-

wild-type protein, pH7.5, 25°C

707486

4.1.3.4

0.008

-

-

5362

4.1.3.4

0.0134

-

K48Q mutant protein, pH not specified in the publication, 30°C

715529

4.1.3.4

0.02

-

wild-type

5366, 5375

4.1.3.4

0.0209

-

K48N mutant protein, pH not specified in the publication, 30°C

715529

4.1.3.4

0.024

-

wild-type

5373

4.1.3.4

0.026

-

pH not specified in the publication, temperature not specified in the publication

713966

4.1.3.4

0.0265

-

wild type protein, pH not specified in the publication, 30°C

715529

4.1.3.4

0.04

-

-

5371

4.1.3.4

0.0448

-

both isoenzymes

5369

4.1.3.4

0.045

-

C323S mutant

5373

4.1.3.4

0.053

-

C237A mutant

5366

1.1.1.34

21 entries

1.1.1.88

3 entries

2.8.3.13

4 entries

3.1.2.20

4 entries

4.1.3.4

11 entries

4.2.1.18

2.25

-

-

679737

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.3.10

0.0011

-

comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A300 nm standard assay

701677

2.3.3.10

0.0015

-

comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A412 nm standard assay

701677

2.3.3.10

0.0031

-

comparison of kinetic parameters measured in spectrophotometric cuvette and microplate format assays, DELTA A412 nm microplate assay

701677

2.3.3.10

0.012

-

-

488105, 488107

2.3.3.10

0.013

-

pH 8.0, competitive inhibition, substrate acetyl-CoA

488091

2.3.3.10

0.1

-

pH 8.0

488091

2.3.3.10

6 entries

References & Links

Literature References (89)

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Show Reference (89 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5362

6159358

Purification and characterization of avian liver 3-hydroxy-3-methylglutaryl coenzyme A lyase

1980

Kramer, P.R.; Miziorko, H.M.

J. Biol. Chem.

255

11023-11028

5366

7632692

Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase: testing the function of the active site cysteine by site-directed mutation

1995

Narasimhan, C.; Roberts, J.R.; Miziorko, H.M.

Biochemistry

34

9930-9935

5369

8670134

Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria

1996

Ashmarina, L.I.; Robert, M.F.; Elsliger, M.A.; Mitchell, G.A.

Biochem. J.

315

71-75

5371

-

Partial purification and characterization of membrane-associated 3-hydroxy-3-methylglutaryl coenzyme A lyase from radish seedlings

1993

Weber, T.; Bach, T.J.

Z. Naturforsch. C

48

444-450

5373

8027038

3-Hydroxy-3-methylglutaryl-CoA lyase: expression and isolation of the recombinant human enzyme and investigation of a mechanism for regulation of enzyme activity

1994

Roberts, J.R.; Narasimhan, C.; Hruz, P.W.; Mitchell, G.A.; Miziorko, H.M.

J. Biol. Chem.

269

17841-17846

5375

1332752

Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl-CoA lyase: characterization of the isolated recombinant protein and investigation of the enzyme's cation requirements

1992

Narasimhan, C.; Miziorko, H.M.

Biochemistry

31

11224-11230

94960

7138544

Inhibition of HMG-CoA reductase by its substrates

1982

Feingold K.R.; Wiley M.H.; Moser A.H.; Lear S.R.; Siperstein M.D.

Biochem. Biophys. Res. Commun.

107

1376-1383

94961

6282220

Some properties of purified 3-hydroxy-3-methylglutaryl Coenzyme A reductase phosphatase from rat liver

1982

Gil G.; Hegardt F.

Arch. Biochem. Biophys.

214

192-198

134607

-

Regulation of rat liver HMG-CoA reductase by reductase kinase and the cytosolic and microsomal protein phosphatases

1986

Hegardt, F.G.

Adv. Protein Phosphatases

3

1-30

134616

-

Mitochondrial protein phosphatases

1987

Reed, L.J.; Damuni, Z.

Adv. Protein Phosphatases

4

59-76

286557

13805544

beta-Hydroxy-beta-methylglutaryl coenzyme A reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver

1960

Bucher, N.L.R.; Overath, P.; Lynen, F.

Biochim. Biophys. Acta

40

491-501

286558

13818862

The reduction of beta-hydroxy-beta-methylglutaryl coenzyme A to mevalonic acid

1960

Durr, I.F.; Rudney, H.

J. Biol. Chem.

235

2572-2578

286559

4985697

Solubilization and purification of beta-hydroxy-beta-methylglutaryl coenzyme A reductase from rat liver

1970

Kawachi, T.; Rudney, H.

Biochemistry

9

1700-1705

286560

4607673

Inhibition of yeast hydroxymethylglutaryl-CoA reductase by a rat liver mitochondrial preperation

1974

Madhosingh, C.; Migicovski, B.B.; Wood, I.M.

FEBS Lett.

46

20-22

286561

237546

Prevention of cold inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by NADPH

1975

Heller, R.A.; Gould, R.G.

Biochim. Biophys. Acta

388

254-259

286562

-

Hydroxymethylglutaryl coenzyme A reductase in Fusarium oxysporum

1977

Madhosingh, C.; Orr, W.

Agric. Biol. Chem.

41

1519-1521

286563

26407

Hydroxymethylglutaryl coenzyme A reductase purification and properties of the enzyme from Fusarium oxysporum

1978

Madhosingh, C.; Orr, W.

Biochim. Biophys. Acta

523

283-296

286564

223570

Hydroxymethylglutaryl coenzyme A reductase activity in hamster adrenal mitochondria purified on a sucrose gradient

1979

Preiss, B.; Lehoux, J.G.

Biochem. Biophys. Res. Commun.

88

1140-1146

286565

6256385

Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system

1981

Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.

J. Biol. Chem.

256

1138-1144

286566

7007371

Inactivation of hydroxymethylglutaryl-CoA reductase from yeast by coenzyme A disulfide

1981

Gilbert, H.F.; Stewart, M.D.

J. Biol. Chem.

256

1782-1785

286567

7077140

Recovery and activation from hydroxymethylglutaryl coenzyme A reductase from rat small intestine

1982

Young, N.L.; Saudek, C.D.; Crawford, S.A.; Zuckerbrod, S.L.

J. Lipid Res.

23

257-265

286568

-

Hydroxymethylglutaryl CoA reductase (NADPH) in the latex of Hevea brasiliensis

1982

Sipat, A.P.

Phytochemistry

21

2613-2618

286569

6707519

Hydroxymethylglutaryl CoA reductase and the modulation of microsomal cholesterol content by the none specific lipid transfer protein

1984

Van Heusden, G.P.H.; Wirtz, K.W.A.

J. Lipid Res.

25

27-32

286570

-

Cellular distribution of 3-hydroxy-3-methylglutaryl coenzyme A reductase and mevalonate kinase in leaves of Nepeta cataria

1984

Arebalo, R.E.; Mitchell, Jr., E.D.

Phytochemistry

23

13-18

286571

6487662

Regulation of human leukocyte microsomal hydroxymethylglutaryl-CoA reductase activity by a phosphorylation and dephosphorylation mechanism

1984

Harwood, Jr., H.J.; Schneider, M.; Stacpool, P.W.

Biochim. Biophys. Acta

805

245-251

286572

3850089

Activation of rat liver microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase by NADPH

1985

Ness, G.C.; Eales, S.J.; Pendleton, L.C.; Smith, M.

J. Biol. Chem.

260

12391-12393

286573

3017222

The effect of substrates and competitive inhibitors on the phosphatase dependent activation of hepatic hydroxymethylglutaryl CoA reductase

1986

Feingold, K.R.; Moser, A.H.

Arch. Biochem. Biophys.

249

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Further purification and characterization of the succinyl-CoA:3-hydroxy-3-methylglutarate coenzyme A transferase from rat-liver mitochondria

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Regulated accumulation of 3-hydroxy-3-methylglutaryl CoA reductase protein in potato cell cultures: Effects of calcium and enzyme inhibitors

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Rat HMGCoA reductase activation in thioacetamide-induced liver injury is related to an increased reactive oxygen species content

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Biochemical characterization of human 3-methylglutaconyl-CoA hydratase and its role in leucine metabolism

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Binding effect and design of a competitive inhibitory peptide for HMG-CoA reductase through modeling of an active peptide backbone

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Cloning and characterization of a gene encoding HMG-CoA reductase from Ganoderma lucidum and its functional identification in yeast

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Implication of HMGR in homeostasis of sequestered and de novo produced precursors of the iridoid biosynthesis in leaf beetle larvae

2008

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Biphasic regulation of HMG-CoA reductase expression and activity during wound healing and its functional role in the control of keratinocyte angiogenic and proliferative responses

2008

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J. Mol. Recognit.

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Up-regulation of an N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase enhances production of essential oils and sterols in transgenic Lavandula latifolia

2007

Munoz-Bertomeu, J.; Sales, E.; Ros, R.; Arrillaga, I.; Segura, J.

Plant Biotechnol. J.

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Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA

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Biochemistry

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Application of a 3,3-diphenylpentane skeleton as a multi-template for creation of HMG-CoA reductase inhibitors

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Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways

2009

Nieto, B.; Fores, O.; Arro, M.; Ferrer, A.

Phytochemistry

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Overexpression of the HMG-CoA reductase gene leads to enhanced artemisinin biosynthesis in transgenic Artemisia annua plants

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Biochemistry

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Novel synthetic inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase activity that inhibit tumor cell proliferation and are structurally unrelated to existing statins

2009

Perchellet, J.P.; Perchellet, E.M.; Crow, K.R.; Buszek, K.R.; Brown, N.; Ellappan, S.; Gao, G.; Luo, D.; Minatoya, M.; Lushington, G.H.

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Inhibitory activity of some plant methanol extracts on 3-hydroxy-3-methylglutaryl coenzyme A reductase

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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.

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New Crystallographic snapshots of large domain movements in bacterial 3-hydroxy-3-methylglutaryl coenzyme A reductase

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Ragwan, E.R.; Arai, E.; Kung, Y.

Biochemistry

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Structural features and domain movements controlling substrate binding and cofactor specificity in class II HMG-CoA reductase

2018

Miller, B.R.; Kung, Y.

Biochemistry

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Metabolic engineering of Saccharomyces cerevisiae to overproduce squalene

2020

Li, T.; Liu, G.S.; Zhou, W.; Jiang, M.; Ren, Y.H.; Tao, X.Y.; Liu, M.; Zhao, M.; Wang, F.Q.; Gao, B.; Wei, D.Z.

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Links to other databases for 3-hydroxy-3-methylglutaryl-CoA

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