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• • In Vivo Substrate
  • In Vivo Product
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  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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Ligand neryl diphosphate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.20

polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit

723103, 723380, 723468, 738652

-

2.5.1.92

neryl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate

723434

-

4.2.3.51

5 neryl diphosphate = 5 diphosphate + alpha-phellandrene + beta-phellandrene + alpha-terpinene + beta-terpinene + limonene

706501

-

4.2.3.51

neryl diphosphate = beta-phellandrene + diphosphate

746608, 748551, 747657, 749040

-

4.2.3.51

2 entries

4.2.3.52

neryl diphosphate = (4S)-beta-phellandrene + diphosphate

749040

-

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.28

dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate

-

-

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.20

polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit

723103, 723380, 723468, 738652

-

2.5.1.28

neryl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6Z)-farnesyl diphosphate

737748

-

2.5.1.31

isopentenyl diphosphate + neryl diphosphate = C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate

637475, 637481, 637483, 637474

-

2.5.1.31

neryl diphosphate + isopentenyl diphosphate = ?

637474

-

2.5.1.31

2 entries

2.5.1.68

(E)-neryl diphosphate + isopentenyl diphosphate = (2Z,6Z)-farnesyl diphosphate + diphosphate

669192

-

2.5.1.86

neryl diphosphate + isopentenyl diphosphate = diphosphate + decaprenyl diphosphate + nonaprenyl diphosphate + octaprenyl diphosphate

704266

-

2.5.1.88

neryl diphosphate + n isopentenyl diphosphate = n diphosphate + poly-cis-polyprenyl diphosphate

704741

-

2.5.1.91

neryl diphosphate + isopentenyl diphosphate = diphosphate + nonaprenyl diphosphate

704266

-

2.5.1.92

neryl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6Z)-farnesyl diphosphate

706218, 737748

-

2.5.1.92

neryl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate

723434

-

2.5.1.92

2 entries

3.1.7.1

neryl diphosphate + H2O = nerol + diphosphate

95168

-

3.1.7.3

neryl-diphosphate + H2O = nerol + diphosphate

95170

-

4.2.3.104

(2Z)-neryl diphosphate = limonene + diphosphate

747656

-

4.2.3.107

neryl diphosphate = limonene + diphosphate

748962

-

4.2.3.108

neryl diphosphate + H2O = 1,8-cineole + diphosphate

718223

-

4.2.3.108

neryl diphosphate + H2O = ? + diphosphate

717147

-

4.2.3.108

2 entries

4.2.3.11

neryl diphosphate = sabinene hydrate + diphosphate

648550, 648551

-

4.2.3.113

neryl diphosphate = terpinolene + diphosphate

210758

-

4.2.3.114

neryl diphosphate = gamma-terpinene + diphosphate

717142

-

4.2.3.116

neryl diphosphate = (+)-camphene + diphosphate

210757

-

4.2.3.117

neryl diphosphate = (-)-camphene + diphosphate

210757

-

4.2.3.119

neryl diphosphate = (-)-alpha-pinene + diphosphate

210757, 210758

-

4.2.3.120

neryl diphosphate = (-)-beta-pinene + diphosphate

210757

-

4.2.3.121

neryl diphosphate = (+)-alpha-pinene + diphosphate

210757, 210758

-

4.2.3.122

neryl diphosphate = myrcene + diphosphate

210758

-

4.2.3.15

neryl diphosphate = limonene

649456

-

4.2.3.16

neryl diphosphate = ?

210768

-

4.2.3.23

neryl diphosphate = limonene + terpinolene + diphosphate

747865

-

4.2.3.51

5 neryl diphosphate = 5 diphosphate + alpha-phellandrene + beta-phellandrene + alpha-terpinene + beta-terpinene + limonene

706501

-

4.2.3.51

neryl diphosphate = diphosphate + beta-phellandrene + alpha-terpinene + beta-terpinene + limonene + alpha-phellandrene

706501

-

4.2.3.51

neryl diphosphate = beta-phellandrene + diphosphate

746608, 748551, 747657, 749040

-

4.2.3.52

neryl diphosphate = beta-phellandrene + diphosphate

730660

-

4.2.3.52

neryl diphosphate = (4S)-beta-phellandrene + diphosphate

749040

-

4.2.3.51

3 entries

4.2.3.52

2 entries

4.2.3.70

neryl diphosphate = ?

746782

-

5.5.1.22

neryl diphosphate = ?

3773

-

5.5.1.22

neryl diphosphate = (-)-bornyl diphosphate

3770

-

5.5.1.22

2 entries

5.5.1.8

Neryl diphosphate = (+)-Bornyl-diphosphate

3773, 3767

-

Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.28

dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate

638430, 638431

-

2.5.1.88

neryl diphosphate + n isopentenyl diphosphate = n diphosphate + poly-cis-polyprenyl diphosphate

-

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.20

accelerates activity

638725

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

5.3.3.2

-

2936

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

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Show Turnover Number (8 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.28

0.18

-

pH 7.6, 30°C, mutant NDPS1-M4

737748

2.5.1.28

3.7

-

pH 7.6, 30°C, mutant NDPS1-M10

737748

2.5.1.28

2 entries

2.5.1.86

0.16

-

pH 7.9, 37°C

704266

2.5.1.91

0.052

-

pH 7.9, 37°C

704266

2.5.1.92

0.069

-

pH 7.6, 30°C, wild-type enzyme

737748

4.2.3.104

4.26

-

pH 7.5, 38°C, recombinant His-tagged enzyme

747656

4.2.3.107

0.636

-

recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication

748962

4.2.3.51

4.1

-

pH 8.0, 30°C

706501

K_M Value (26 results)

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Show KM Value (26 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.5.1.28

0.014

-

pH 7.6, 30°C, mutant NDPS1-M10

737748

2.5.1.28

0.097

-

pH 7.6, 30°C, mutant NDPS1-M4

737748

2.5.1.31

0.0267

-

pH 8.5, 37°C

637474

2.5.1.31

0.032

-

pH 7.5, 35°C

637483

2.5.1.28

2 entries

2.5.1.31

2 entries

2.5.1.68

0.016

-

pH 7.9, 37°C

669192

2.5.1.86

0.029

-

pH 7.9, 37°C

704266

2.5.1.91

0.029

-

pH 7.9, 37°C

704266

2.5.1.92

0.051

-

pH 7.6, 30°C, wild-type enzyme

737748

4.2.3.104

0.068

-

pH 7.5, 38°C, recombinant His-tagged enzyme

747656

4.2.3.107

0.0143

-

recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication

748962

4.2.3.108

0.0045

-

pH 6.3, 30°C

717147

4.2.3.11

0.0105

-

pH 7.0, 30°C

648550

4.2.3.11

0.0105

-

pH 7.0, 30°C

648551

4.2.3.113

0.0021

-

pH 6.5, 30°C

210758

4.2.3.113

0.006

-

pH 6.5, 30°C

210758

4.2.3.11

2 entries

4.2.3.113

2 entries

4.2.3.114

0.009

-

pH 6.6, 30°C

717142

4.2.3.119

0.0021

-

pH 6.5, 30°C

210758

4.2.3.119

0.0023

-

pH 7.2, 30°C

210757

4.2.3.119

2 entries

4.2.3.120

0.0023

-

pH 7.2, 30°C

210757

4.2.3.121

0.006

-

pH 6.5, 30°C

210758

4.2.3.16

0.001

-

-

210768

4.2.3.51

0.0091

-

pH 8.0, 30°C

706501

5.5.1.22

0.0037

-

pH and temperature not specified in the publication

3773

5.5.1.8

0.0037

-

-

3773

5.5.1.8

0.0121

-

-

3773

5.5.1.8

0.018

-

-

3767

5.5.1.8

3 entries

References & Links

Literature References (42)

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Show Reference (42 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2936

202196

Isopentenyl pyrophosphate isomerase from pig liver

1977

Banthorpe, D.V.; Doonan, S.; Gutowski, J.A.

Arch. Biochem. Biophys.

184

381-390

3767

42356

Biosynthesis of monoterpenes: preliminary characterization of bornyl pyrophosphate synthetase from sage (Salvia officinalis) and demonstration that geranyl pyrophosphate is the preferred substrate for cyclization

1979

Croteau, R.; Karp, F.

Arch. Biochem. Biophys.

198

512-522

3770

3997807

Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate

1985

Croteau, R.; Felton, N.M.; Wheeler, C.J.

J. Biol. Chem.

260

5956-5962

3773

3759972

Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate

1986

Croteau, R.; Satterwhite, D.M.; Cane, D.E.; Chang, C.C.

J. Biol. Chem.

261

13438-13445

95168

-

Hydrolysis of allylic phosphates by enzymes from the flavedo of Citrus sinensis

1980

Perez, L.M.; Taucher, G.; Cori, O.

Phytochemistry

19

183-187

95170

42357

Biosynthesis of monoterpenes: Hydrolysis of bornyl pyrophosphate, an essential step in camphor biosynthesis, and hydrolysis of geranyl pyrophosphate, the acyclic precursor of camphor, by enzymes from Sage (Salvia officinalis)

1979

Croteau R.; Karp, F.

Arch. Biochem. Biophys.

198

523-532

210757

3392006

Biosynthesis of monoterpenes: Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophospahte to (+)- and (-) pinene and (+)- and (-)-camphene

1988

Croteau, R.; Satterwhite, D.M.; Cane, D.E.; Chang, C.C.

J. Biol. Chem.

263

10063-10071

210758

2768265

Biosynthesis of monoterpenes: Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage

1989

Croteau, R.; Satterwhite, D.M.

J. Biol. Chem.

264

15309-15315

210768

1605644

Characterization and mechanism of (4S)-limonene synthase, a monoterpene cyclase from the glandular trichomes of peppermint (Mentha x piperita)

1992

Rajaonarivony, J.I.M.; Gershenzon, J.; Croteau, R.

Arch. Biochem. Biophys.

296

49-57

637474

6818223

Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase

1982

Takahashi, I.; Ogura, K.

J. Biochem.

92

1527-1537

637475

2991704

Purification and characterization of undecaprenylpyrophosphate synthetase

1985

Allen, C.M.

Methods Enzymol.

110

281-299

637481

7436416

Prenyl transferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetase

1980

Baba, T.; Allen, C.M.

Arch. Biochem. Biophys.

200

474-484

637483

728420

Substrate specificity of undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum

1978

Baba, T.; Allen, C.M.

Biochemistry

17

5598-5604

638430

4303098

Terpene biosynthesis: formation of nerol, geraniol, and other prenols by an enzyme system from Pinus radiata seedlings

1969

Beytia, E.; Valenzuela, P.; Cori, O.

Arch. Biochem. Biophys.

129

346-356

638431

-

Biosynthesis of geraniol and nerol in cell-free extracts of Tanatecum vulgare

1976

Banthorpe, D.V.; Bucknall, G.A.; Doonan, H.J.; Doonan, S.; Rowan, M.G.

Phytochemistry

15

91-100

638725

-

Rubber transferase from hevea brasiliensis latex

1969

Archer, B.L.; Cockbain, E.G.

Methods Enzymol.

15

476-480

648550

2916845

Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate

1989

Hallahan, T.W.; Croteau, R.

Arch. Biochem. Biophys.

269

313-326

648551

3401015

Monoterpene biosynthesis: demonstration of a geranyl pyrophosphate:sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis)

1988

Hallahan, T.W.; Croteau, R.

Arch. Biochem. Biophys.

264

618-631

649456

11913979

Biosynthesis of marine natural products: isolation and characterization of a myrcene synthase from cultured tissues of the marine red alga Ochtodes secundiramea

2002

Wise, M.L.; Rorrer, G.L.; Polzin, J.J.; Croteau, R.

Arch. Biochem. Biophys.

400

125-132

669192

11152452

Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis

2001

Schulbach, M.C.; Mahapatra, S.; Macchia, M.; Barontini, S.; Papi, C.; Minutolo, F.; Bertini, S.; Brennan, P.J.; Crick, D.C.

J. Biol. Chem.

276

11624-11630

704266

15516568

Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis

2004

Kaur, D.; Brennan, P.J.; Crick, D.C.

J. Bacteriol.

186

7564-7570

704741

19447338

Cloning and functional analysis of cis-prenyltransferase from Thermobifida fusca

2009

Ambo, T.; Noike, M.; Kurokawa, H.; Koyama, T.

J. Biosci. Bioeng.

107

620-622

706218

19155349

A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites

2009

Sallaud, C.; Rontein, D.; Onillon, S.; Jabe, F.; Duffé, P.; Giacalone, C.; Thoraval, S.; Escoffier, C.; Herbette, G.; Leonhardt, N.; Causse, M.; Tissier, A.

Plant Cell

21

301-317

706501

19487664

Monoterpenes in the glandular trichomes of tomato are synthesized from a neryl diphosphate precursor rather than geranyl diphosphate

2009

Schilmiller, A.L.; Schauvinhold, I.; Larson, M.; Xu, R.; Charbonneau, A.L.; Schmidt, A.; Wilkerson, C.; Last, R.L.; Pichersky, E.

Proc. Natl. Acad. Sci. USA

106

10865-10870

717142

736574

gamma-Terpinene synthetase: A key enzyme in the biosynthesis of aromatic monoterpenes

1978

Poulose, A.; Croteau, R.

Arch. Biochem. Biophys.

191

400-411

717147

8117108

Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase

1994

Croteau, R.; Alonso, W.R.; Koepp, A.E.; Johnson, M.A.

Arch. Biochem. Biophys.

309

184-192

718223

22592779

Cloning, functional characterization and genomic organization of 1,8-cineole synthases from Lavandula

2012

Demissie, Z.A.; Cella, M.A.; Sarker, L.S.; Thompson, T.J.; Rheault, M.R.; Mahmoud, S.S.

Plant Mol. Biol.

79

393-411

723103

22999170

Natural rubber biosynthesis in plants: rubber transferase

2012

Cornish, K.; Xie, W.

Methods Enzymol.

515

63-82

723380

-

Characterization of cis-prenyltransferases from the rubber producing plant Hevea brasiliensis heterologously expressed in yeast and plant cells

2012

Takahashi, S.; Lee, H.; Yamashita, S.; Koyama, T.

Plant Biotechnol.

29

411-417

723434

23134568

The tomato cis-prenyltransferase gene family

2013

Akhtar, T.A.; Matsuba, Y.; Schauvinhold, I.; Yu, G.; Lees, H.A.; Klein, S.E.; Pichersky, E.

Plant J.

73

640-652

723468

22238421

Laticifer-specific cis-prenyltransferase silencing affects the rubber, triterpene, and inulin content of Taraxacum brevicorniculatum

2012

Post, J.; van Deenen, N.; Fricke, J.; Kowalski, N.; Wurbs, D.; Schaller, H.; Eisenreich, W.; Huber, C.; Twyman, R.M.; Pruefer, D.; Gronover, C.S.

Plant Physiol.

158

1406-1417

730660

21165645

Cloning and functional characterization of beta-phellandrene synthase from Lavandula angustifolia

2011

Demissie, Z.; Sarker, L.; Mahmoud, S.

Planta

233

685-696

737748

24291644

cis-Prenyltransferase atCPT6 produces a family of very short-chain polyisoprenoids in planta

2014

Surmacz, L.; Plochocka, D.; Kania, M.; Danikiewicz, W.; Swiezewska, E.

Biochim. Biophys. Acta

1841

240-250

738652

25477521

A lettuce (Lactuca sativa) homolog of human Nogo-B receptor interacts with cis-prenyltransferase and is necessary for natural rubber biosynthesis

2015

Qu, Y.; Chakrabarty, R.; Tran, H.T.; Kwon, E.J.; Kwon, M.; Nguyen, T.D.; Ro, D.K.

J. Biol. Chem.

290

1898-1914

746608

29397685

Heterologous leader sequences in fusion constructs enhance expression of geranyl diphosphate synthase and yield of beta-phellandrene production in cyanobacteria (Synechocystis)

2018

Betterle, N.; Melis, A.

ACS Synth. Biol.

7

912-921

746782

26100386

Characterisation of a recombinant patchoulol synthase variant for biocatalytic production of terpenes

2015

Frister, T.; Hartwig, S.; Alemdar, S.; Schnatz, K.; Thoens, L.; Scheper, T.; Beutel, S.

Appl. Biochem. Biotechnol.

176

2185-2201

747656

-

Bioproduction of alpha-humulene in metabolically engineered Escherichia coli and application in zerumbone synthesis

2017

Alemdar, S.; Koenig, J.; Hartwig, S.; Frister, T.; Scheper, T.; Beutel, S.

Eng. Life Sci.

17

900-907

747657

29367791

Mono- and sesquiterpene release from tomato (Solanum lycopersicum) leaves upon mild and severe heat stress and through recovery From gene expression to emission responses

2016

Pazouki, L.; Kanagendran, A.; Li, S.; Kaennaste, A.; Rajabi Memari, H.; Bichele, R.; Niinemets, U.

Environ. Exp. Bot.

132

1-15

747865

25784918

Germacrene A synthase in yarrow (Achillea millefolium) is an enzyme with mixed substrate specificity gene cloning, functional characterization and expression analysis

2015

Pazouki, L.; Memari, H.R.; Kaennaste, A.; Bichele, R.; Niinemets, U.E.

Front. Plant Sci.

6

111

748551

26410450

A phycocyanin-phellandrene synthase fusion enhances recombinant protein expression and beta-phellandrene (monoterpene) hydrocarbons production in Synechocystis (cyanobacteria)

2015

Formighieri, C.; Melis, A.

Metab. Eng.

32

116-124

748962

28258552

Isolation and functional characterization of a methyl jasmonate-responsive 3-carene synthase from Lavandula x intermedia

2017

Adal, A.M.; Sarker, L.S.; Lemke, A.D.; Mahmoud, S.S.

Plant Mol. Biol.

93

641-657

749040

29974209

Cyanobacterial production of plant essential oils

2018

Formighieri, C.; Melis, A.

Planta

248

933-946

Links to other databases for neryl diphosphate

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Show Links (1 entry)

ChEBI

PubChem