Terpentetriene synthase

Last updated
Terpentetriene synthase
Identifiers
EC no. 4.2.3.36
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Terpentetriene synthase (EC 4.2.3.36, Cyc2) is an enzyme with systematic name terpentedienyl-diphosphate diphosphate-lyase (terpentetriene-forming). [1] [2] [3] This enzyme catalyses the following chemical reaction

terpentedienyl diphosphate terpentetriene + diphosphate

This enzyme requires Mg2+ for maximal activity but can use Mn2+, Fe2+ or Co2+ to a lesser extent.

Related Research Articles

<span class="mw-page-title-main">Fusicoccin</span> Chemical compound

Fusicoccins are organic compounds produced by a fungus. It has detrimental effect on plants and causes their death.

<span class="mw-page-title-main">Isopentenyl-diphosphate delta isomerase</span> Class of enzymes

Isopentenyl pyrophosphate isomerase, also known as Isopentenyl-diphosphate delta isomerase, is an isomerase that catalyzes the conversion of the relatively un-reactive isopentenyl pyrophosphate (IPP) to the more-reactive electrophile dimethylallyl pyrophosphate (DMAPP). This isomerization is a key step in the biosynthesis of isoprenoids through the mevalonate pathway and the MEP pathway.

<span class="mw-page-title-main">Bornyl diphosphate synthase</span>

In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction

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

The enzyme ent-kaurene synthase catalyzes the chemical reaction

In enzymology, a 1-deoxy-d-xylulose-5-phosphate synthase (EC 2.2.1.7) is an enzyme in the non-mevalonate pathway that catalyzes the chemical reaction

<span class="mw-page-title-main">Chlorophyll synthase</span> Class of enzymes

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

<span class="mw-page-title-main">2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase</span> Class of enzymes

In enzymology, a 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">Momilactone B</span> Chemical compound

Momilactone B is an allelopathic agent produced from the roots of rice. It has been shown to be produced in high concentrations by the roots of rice seedlings. The production of momilactone B has also been induced in response to infection by blast fungus or irradiated with UV light. More recently it has been shown to be a potential chemotherapeutic agent against human colon cancer.

<span class="mw-page-title-main">YgbB N terminal protein domain</span>

In molecular biology, YgbB is a protein domain. This entry makes reference to a number of proteins from eukaryotes and prokaryotes which share this common N-terminal signature and appear to be involved in terpenoid biosynthesis. The YgbB protein is a putative enzyme thought to aid terpenoid and isoprenoid biosynthesis, a vital chemical in all living organisms. This protein domain is part of an enzyme which catalyses a reaction in a complex pathway.

Futalosine hydrolase (EC 3.2.2.26, futalosine nucleosidase, MqnB) is an enzyme with systematic name futalosine ribohydrolase. This enzyme catalyses the following chemical reaction

ent-Sandaracopimaradiene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase [ent-sandaracopimara-8(14),15-diene-forming]. This enzyme catalyses the following chemical reaction

ent-Pimara-9(11),15-diene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Stemar-13-ene synthase is an enzyme with systematic name 9α-copalyl-diphosphate diphosphate-lyase (stemar-13-ene-forming). This enzyme catalyses the following chemical reaction

syn-Pimara-7,15-diene synthase is an enzyme with systematic name 9α-copalyl-diphosphate diphosphate-lyase (9β-pimara-7,15-diene-forming). This enzyme catalyses the following chemical reaction

Aphidicolan-16β-ol synthase (EC 4.2.3.42, PbACS) is an enzyme with systematic name 9α-copalyl-diphosphate diphosphate-lyase (aphidicolan-16β-ol-forming). This enzyme catalyses the following chemical reaction

Phyllocladan-16α-ol synthase (EC 4.2.3.45, PaDC1) is an enzyme with systematic name (+)-copalyl-diphosphate diphosphate-lyase (phyllocladan-16α-ol-forming). This enzyme catalyses the following chemical reaction

Miltiradiene synthase is an enzyme with systematic name (+)-copaly-diphosphate diphosphate-lyase . This enzyme catalyses the following chemical reaction

Terpentedienyl-diphosphate synthase is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction

Halimadienyl-diphosphate synthase is an enzyme with systematic name halima-5,13-dien-15-yl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction

References

  1. Dairi T, Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H (October 2001). "Eubacterial diterpene cyclase genes essential for production of the isoprenoid antibiotic terpentecin". Journal of Bacteriology. 183 (20): 6085–94. doi:10.1128/jb.183.20.6085-6094.2001. PMC   99688 . PMID   11567009.
  2. Hamano Y, Kuzuyama T, Itoh N, Furihata K, Seto H, Dairi T (October 2002). "Functional analysis of eubacterial diterpene cyclases responsible for biosynthesis of a diterpene antibiotic, terpentecin". The Journal of Biological Chemistry. 277 (40): 37098–104. doi: 10.1074/jbc.m206382200 . PMID   12138123.
  3. Eguchi T, Dekishima Y, Hamano Y, Dairi T, Seto H, Kakinuma K (July 2003). "A new approach for the investigation of isoprenoid biosynthesis featuring pathway switching, deuterium hyperlabeling, and 1H NMR spectroscopy. The reaction mechanism of a novel streptomyces diterpene cyclase". The Journal of Organic Chemistry. 68 (14): 5433–8. doi:10.1021/jo026728a. PMID   12839434.