Isoprene synthase

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Isoprene synthase
Isoprene synthase
Identifiers
EC no.	4.2.3.27
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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NCBI	proteins

Last updated August 27, 2023

The enzyme isoprene synthase (EC 4.2.3.27) catalyzes the chemical reaction

prenyl pyrophosphate

\rightleftharpoons

isoprene + diphosphate

This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is prenyl-diphosphate diphosphate-lyase (isoprene-forming). Other names in common use include ISPC, and ISPS.

Related Research Articles

Isoprene, or 2-methyl-1,3-butadiene, is a common volatile organic compound with the formula CH₂=C(CH₃)−CH=CH₂. In its pure form it is a colorless volatile liquid. It is produced by many plants and animals (including humans) and its polymers are the main component of natural rubber. C. G. Williams named the compound in 1860 after obtaining it from the pyrolysis of natural rubber; he correctly deduced the empirical formula C₅H₈.

Farnesyl pyrophosphate (FPP), also known as farnesyl diphosphate (FDP), is an intermediate in the biosynthesis of terpenes and terpenoids such as sterols and carotenoids. It is also used in the synthesis of CoQ, as well as dehydrodolichol diphosphate.

The enzyme (+)-δ-cadinene synthase catalyzes the chemical reaction

In enzymology, a copalyl diphosphate synthase is an enzyme that catalyzes the chemical reaction

In enzymology, an ent-copalyl diphosphate synthase is an enzyme that catalyzes the chemical reaction:

Strictosidine synthase (EC 4.3.3.2) is an enzyme in alkaloid biosynthesis that catalyses the condensation of tryptamine with secologanin to form strictosidine in a formal Pictet–Spengler reaction:

<span class="mw-page-title-main">Diphosphomevalonate decarboxylase</span> InterPro Family

Diphosphomevalonate decarboxylase (EC 4.1.1.33), most commonly referred to in scientific literature as mevalonate diphosphate decarboxylase, is an enzyme that catalyzes the chemical reaction

The enzyme (4S)-limonene synthase catalyzes the chemical reaction

The enzyme abieta-7,13-diene synthase catalyzes the chemical reaction

The enzyme amorpha-4,11-diene synthase (ADS) catalyzes the chemical reaction

The enzyme ent-kaurene synthase catalyzes the chemical reaction

The enzyme germacrene-A synthase (EC 4.2.3.23) catalyzes the chemical reaction

In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction

The enzyme (R)-limonene synthase (EC 4.2.3.20) catalyzes the reversible chemical reaction

The enzyme S-linalool synthase (EC 4.2.3.25) catalyzes the chemical reaction

Vetispiradiene synthase is an enzyme from Egyptian henbane that catalyzes the following chemical reaction:

Ditrans,polycis-polyprenyl diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase . This enzyme catalyses the following chemical reaction

(3S,6E)-nerolidol synthase (EC 4.2.3.48, (E)-nerolidol synthase, nerolidol synthase, (3S)-(E)-nerolidol synthase, FaNES1) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((3S,6E)-nerolidol-forming). This enzyme catalyses the following chemical reaction

(S)-β-bisabolene synthase (EC 4.2.3.55) is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate diphosphate-lyase ((S)-β-bisabolene-forming). This enzyme catalyses the following chemical reaction

(E)-β-Ocimene synthase (EC 4.2.3.106, β-ocimene synthase, AtTPS03, ama0a23, LjEbetaOS, MtEBOS) is an enzyme with systematic name geranyl-diphosphate diphosphate-lyase ((E)-β-ocimene-forming). This enzyme catalyses the following chemical reaction

References

Silver GM, Fall R (1991). "Enzymatic Synthesis of Isoprene from Dimethylallyl Diphosphate in Aspen Leaf Extracts". Plant Physiology. 97 (4): 1588–1591. doi:10.1104/pp.97.4.1588. PMC 1081206 . PMID 16668590.
Silver GM, Fall R (1995). "Characterization of aspen isoprene synthase, an enzyme responsible for leaf isoprene emission to the atmosphere". Journal of Biological Chemistry. 270 (22): 13010–6. doi: 10.1074/jbc.270.22.13010 . PMID 7768893.
Wildermuth MC, Fall R (1996). "Light-Dependent Isoprene Emission (Characterization of a Thylakoid-Bound Isoprene Synthase in Salix discolor Chloroplasts)". Plant Physiology. 112 (1): 171–182. doi:10.1104/pp.112.1.171. PMC 157936 . PMID 12226383.
Schnitzler JP, Arenz R, Steinbrecher R, Lehming A (1996). "Characterization of an Isoprene Synthase from Leaves of Quercus petraea (Mattuschka) Liebl". Botanica Acta. 109 (3): 216–221. doi:10.1111/j.1438-8677.1996.tb00566.x.
Miller B, Oschinski C, Zimmer W (2001). "First isolation of an isoprene synthase gene from poplar and successful expression of the gene in Escherichia coli". Planta. 213 (3): 483–7. doi:10.1007/s004250100557. PMID 11506373. S2CID 35340315.
Sivy TL, Shirk MC, Fall R (2002). "Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis". Biochemical and Biophysical Research Communications. 294 (1): 71–5. doi:10.1016/S0006-291X(02)00435-7. PMID 12054742.
Sasaki K, Ohara K, Yazaki K (2005). "Gene expression and characterization of isoprene synthase from Populus alba". FEBS Letters. 579 (11): 2514–8. doi: 10.1016/j.febslet.2005.03.066 . PMID 15848197.
Schnitzler JP, Zimmer I, Bachl A, Arend M, Fromm J, Fischbach RJ (2005). "Biochemical properties of isoprene synthase in poplar (Populus x canescens)". Planta. 222 (5): 777–86. doi:10.1007/s00425-005-0022-1. PMID 16052321. S2CID 29955976.
Vickers CE, Possell M, Cojocariu C, Velikova V, Laothawornkitkul J, Ryan A, Mullineaux PM, Hewitt CN (2009). "Isoprene synthesis protects transgenic tobacco plants from oxidative stress". Plant, Cell & Environment. 32 (5): 520–31. doi:10.1111/j.1365-3040.2009.01946.x. PMID 19183288.
Vickers CE, Possell M, Hewitt CN, Mullineaux P (2010). "Genetic structure and regulation of isoprene synthase in Poplar (Populus spp.)". Plant Molecular Biology. 73 (4–5): 547–58. doi:10.1007/s11103-010-9642-3. PMID 20467886. S2CID 22907306.
Vickers CE, Possell M, Laothawornkitkul J, Ryan AC, Hewitt CN, Mullineaux P (2011). "Isoprene synthesis in plants – lessons from a transgenic tobacco model". Plant, Cell & Environment. 34 (6): 1043–53. doi: 10.1111/j.1365-3040.2011.02303.x . PMID 21388420.

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v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)