Ent-kaurene synthase

Last updated
ent-kaurene synthase
Identifiers
EC no. 4.2.3.19
CAS no. 9055-64-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme ent-kaurene synthase (EC 4.2.3.19) catalyzes the chemical reaction

ent-copalyl diphosphate ent-kaurene + 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 ent-copalyl-diphosphate diphosphate-lyase (cyclizing, ent-kaurene-forming). Other names in common use include ent-kaurene synthase B, ent-kaurene synthetase B, ent-copalyl-diphosphate diphosphate-lyase, and (cyclizing). This enzyme participates in diterpenoid biosynthesis.

In Stevia

In Stevia spp., ent-kaurene synthase is a required part of the biosynthesis of steviol. [1] [2] Hajihashemi et al., 2013 find that it is involved in the drought stress response and – because it mimics drought stress – paclobutrazol toxicity. [1] [2] Both inhbit transcription of steviol glycoside synthesis genes including ent-kaurene synthase. [1] [2] This is believed to reduce steviol content in the final plant product. [1] [2]

Related Research Articles

Gibberellins (GAs) are plant hormones that regulate various developmental processes, including stem elongation, germination, dormancy, flowering, flower development, and leaf and fruit senescence. GAs are one of the longest-known classes of plant hormone. It is thought that the selective breeding of crop strains that were deficient in GA synthesis was one of the key drivers of the "green revolution" in the 1960s, a revolution that is credited to have saved over a billion lives worldwide.

<span class="mw-page-title-main">Steviol glycoside</span> Sweet chemicals derived from the Stevia plant

Steviol glycosides are the chemical compounds responsible for the sweet taste of the leaves of the South American plant Stevia rebaudiana (Asteraceae) and the main ingredients of many sweeteners marketed under the generic name stevia and several trade names. They also occur in the related species S. phlebophylla and in the plant Rubus chingii (Rosaceae).

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

Steviol is a diterpene first isolated from the plant Stevia rebaudiana in 1931. Its chemical structure was not fully elucidated until 1960.

In enzymology, an ent-copalyl diphosphate synthase 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 taxadiene synthase 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">Terpene synthase N terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the N terminal domain of the TPS protein.

<span class="mw-page-title-main">Terpene synthase C terminal domain</span> Protein domain

In molecular biology, this protein domain belongs to the terpene synthase family (TPS). Its role is to synthesize terpenes, which are part of primary metabolism, such as sterols and carotene, and also part of the secondary metabolism. This entry will focus on the C terminal domain of the TPS protein.

ent-Cassa-12,15-diene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase (ent-cassa-12,15-diene-forming). 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-8(14),15-diene synthase is an enzyme with systematic name ent-copalyl-diphosphate diphosphate-lyase [ent-pimara-8(14),15-diene-forming]. 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

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

Syn-copalyl-diphosphate synthase is an enzyme with systematic name 9alpha-copalyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction

References

  1. 1 2 3 4 Zhou, Xuan; Gong, Mengyue; Lv, Xueqin; Liu, Yanfeng; Li, Jianghua; Du, Guocheng; Liu, Long (2021). "Metabolic engineering for the synthesis of steviol glycosides: current status and future prospects". Applied Microbiology and Biotechnology . Springer. 105 (13): 5367–5381. doi:10.1007/s00253-021-11419-3. ISSN   0175-7598.
  2. 1 2 3 4 Hajihashemi, Shokoofeh (2021). "Agronomic practices". Steviol Glycosides. Elsevier. pp. 31–56. doi:10.1016/b978-0-12-820060-5.00002-9.


This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.