PathWhiz ID | Pathway | Meta Data |
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PW122501View Pathway |
Triterpenoid BiosynthesisArabidopsis thaliana
Triterpenoids have 30 carbons and six isoprene units. They are derived from (S)-2,3-epoxysqualene. They may contain rings or be acyclic, depending on the bonds formed by the loss of the diphosphate group.
First, the terpenoid backbone is synthesized, producing farnesyl pyrophosphate. Two molecules of farnesyl pyrophosphate then join together to form presqualene diphosphate, catalyzed by squalene synthase 1. Then, the same enzyme removes the pyrophosphate group and replaces it with a hydrogen ion, forming squalene. Squalene then undergoes oxidation of one of its bonds via squlene monooxygenase 1, to form (S)-2,3-epoxysqualene. This may then proceed to the steroid biosynthesis pathway or may react with an isomerase or lyase to form a chair-chair-chair-boat triterpenoid. Similarly, squalene may interact with an isomerase or lyase to form a chair-chair-chair-chair triterpenoid.
After the backbone is complete, (S)-2,3-epoxysqualene can interact with many enzymes in order to form the triterpenoids. It can interact with camelliol C synthase to form camelliol C, thalianol synthase to form thalianol, baruol synthase to form baruol, tirucalladienol synthase to form tirucalla-7,24-dien-3-beta-ol, amyrun synthase LUP2 to form lupeol, alpha- and beta-amyrin synthases to form alpha- and beta-amyrin respectively. It can also interact with lupan-3beta,20-diol synthase to add a water molecule to form lupan-3beta,20-diol, alpha- and beta-seco-amyrin synthases to form alpha- and beta-seco-amyrin respectively, marneral synthase to form marneral, and finally arabidiol synthase to add a water molecule and form arabidiol.
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Creator: Eponine Oler Created On: May 08, 2019 at 15:20 Last Updated: May 08, 2019 at 15:20 |
PW126958View Pathway |
triterpenoid biosynthesisCamellia nitidissima
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Creator: Ping Created On: May 25, 2022 at 18:41 Last Updated: May 25, 2022 at 18:41 |
PW146669View Pathway |
drug action
Tritoqualine Drug Metabolism Action PathwayHomo sapiens
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Creator: Ray Kruger Created On: October 07, 2023 at 18:45 Last Updated: October 07, 2023 at 18:45 |
PW063854View Pathway |
drug action
Tritoqualine H1-Antihistamine ActionHomo sapiens
Tritoqualine is an H1-antihistamine. H1-antihistamines interfere with the agonist action of histamine at the H1 receptor and are administered to attenuate inflammatory process in order to treat conditions such as allergic rhinitis, allergic conjunctivitis, and urticaria. Reducing the activity of the NF-κB immune response transcription factor through the phospholipase C and the phosphatidylinositol (PIP2) signalling pathways also decreases antigen presentation and the expression of pro-inflammatory cytokines, cell adhesion molecules, and chemotactic factors. Furthermore, lowering calcium ion concentration leads to increased mast cell stability which reduces further histamine release. First-generation antihistamines readily cross the blood-brain barrier and cause sedation and other adverse central nervous system (CNS) effects (e.g. nervousness and insomnia). Second-generation antihistamines are more selective for H1-receptors of the peripheral nervous system (PNS) and do not cross the blood-brain barrier. Consequently, these newer drugs elicit fewer adverse drug reactions.
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Creator: Carin Li Created On: September 24, 2017 at 23:27 Last Updated: September 24, 2017 at 23:27 |
PW122589View Pathway |
tRNA ChargingPseudomonas aeruginosa
This pathway is a compilation of Escherichia coli tRNA charging reactions involving amino acids transported into the cell. The aminoacyl-tRNA synthetase is an enzyme that attaches the appropriate amino acid onto its tRNA by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA, which plays an important role in RNA translation. 20 different Aminoacyl-tRNA synthetases can make 20 different types of aa-tRNA for each amino acid according to the genetic code. This process is called "charging" or "loading" the tRNA with amino acid. Ribosome can transfer the amino acid from tRNA to a growing peptide after the tRNA is charged.
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Creator: Ana Marcu Created On: August 12, 2019 at 18:18 Last Updated: August 12, 2019 at 18:18 |
PW000799View Pathway |
tRNA ChargingEscherichia coli
This pathway is a compilation of Escherichia coli tRNA charging reactions involving amino acids transported into the cell. The aminoacyl-tRNA synthetase is an enzyme that attaches the appropriate amino acid onto its tRNA by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA, which plays an important role in RNA translation. 20 different Aminoacyl-tRNA synthetases can make 20 different types of aa-tRNA for each amino acid according to the genetic code. This process is called "charging" or "loading" the tRNA with amino acid. Ribosome can transfer the amino acid from tRNA to a growing peptide after the tRNA is charged.
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Creator: miguel ramirez Created On: March 09, 2015 at 23:49 Last Updated: March 09, 2015 at 23:49 |
PW122591View Pathway |
tRNA Charging 2Pseudomonas aeruginosa
This pathway is a compilation of Escherichia coli tRNA charging reactions involving biosynthesized amino acids. The aminoacyl-tRNA synthetase is an enzyme that attaches the appropriate amino acid onto its tRNA by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA, which plays an important role in RNA translation. 20 different Aminoacyl-tRNA synthetases can make 20 different types of aa-tRNA for each amino acid according to the genetic code. This process is called "charging" or "loading" the tRNA with amino acid. Ribosome can transfer the amino acid from tRNA to a growing peptide after the tRNA is charged.
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Creator: Ana Marcu Created On: August 12, 2019 at 18:19 Last Updated: August 12, 2019 at 18:19 |
PW000803View Pathway |
tRNA Charging 2Escherichia coli
This pathway is a compilation of Escherichia coli tRNA charging reactions involving biosynthesized amino acids. The aminoacyl-tRNA synthetase is an enzyme that attaches the appropriate amino acid onto its tRNA by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA, which plays an important role in RNA translation. 20 different Aminoacyl-tRNA synthetases can make 20 different types of aa-tRNA for each amino acid according to the genetic code. This process is called "charging" or "loading" the tRNA with amino acid. Ribosome can transfer the amino acid from tRNA to a growing peptide after the tRNA is charged.
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Creator: miguel ramirez Created On: March 14, 2015 at 14:45 Last Updated: March 14, 2015 at 14:45 |
PW123859View Pathway |
protein
tRNA Charging: SerineHomo sapiens
An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its tRNA. It does so by catalyzing the esterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. The 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code. This process is sometimes called "charging" or "loading" the tRNA with the amino acid. Once the tRNA is charged, a ribosome can transfer the amino acid from the tRNA onto a growing peptide, according to the genetic code. Aminoacyl-tRNA, therefore, plays an important role in translation, the expression of genes to create proteins. Translation is carried out by ribosomes in the cytoplasm or endoplasmic reticulum after the process of transcription of DNA to RNA in the cell's nucleus (Wikipedia).
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Creator: WishartLab Created On: April 15, 2020 at 12:18 Last Updated: April 15, 2020 at 12:18 |
PW144328View Pathway |
drug action
Troglitazone Drug Metabolism Action PathwayHomo sapiens
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Creator: Ray Kruger Created On: October 07, 2023 at 13:24 Last Updated: October 07, 2023 at 13:24 |