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Printable Handouts
Navigable Slide Index
- Glutathione transferases (GSTs)
- Three superfamilies
- Fosfomycin resistance (Fos A)
- Cytosolic GSTs
- Multiple functions
- Evolutionary aspects
- Human soluble GSTs
- Tissue-distribution (human)
- The nucleophile substrate
- A model second substrate
- Dimer structure
- GSH binding
- Making GSH more reactive
- GSH binding
- The H-site
- Reactive compounds
- Reactive compounds in the cell
- Drugs conjugated to GSH - ex.
- Paracetamol
- Carbamazepine - reactive interm.
- Indomethacin - reactive interm.
- Conjugate export and processing
- Current issues
- Genetic polymorphism
- Drug resistance in tumors
- Induction and biomonitoring
- Induction & cancer chemoprevention
- Chemoprevention & Nrf2 regulation
- Multiple subcellular distribution
- The MAPEG superfamily
- The MAPEG theme - reactive lipid
- MGST1 structure
- Peroxidized lipid substrates
- Cellular protection by MGST1
- Specific functions
- PGE synthase
- MAPEG tissue distribution
- MGST1 activation
- Activation of MGST1 (1)
- Activation of MGST1 (2)
- Knockouts
- Capacity and throughput
- GSTs
Topics Covered
- Isoform properties
- Functional significance
- Protection from toxicity and genotoxicity
- Gene knock-out models
- Oxidative stress and cytostatic drugs
- Pharmacogenetics
- Biochemical transformations in catabolism
- Signalling events
- Biosynthesis of endogenous lipid mediators
- Prostaglandin and leukotriene pathways
Links
Series:
Categories:
Therapeutic Areas:
Talk Citation
Morgenstern, R. (2015, October 1). Glutathione transferases [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved August 23, 2024, from https://doi.org/10.69645/JLZQ3969.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Ralf Morgenstern has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Glutathione transferases
A selection of talks on Metabolism & Nutrition
Transcript
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0:00
Glutathione transferases constitute an important part
of the phase two by a transformation reactions.
The enzymes are made up of members of
three superfamilies with different locations in the cell.
In the rodent liver, glutathione transferases make
up an impressive five percent of the protein content.
The unique aspect of these enzymes is their specificity towards reactive compounds.
The substrates being lipophilic and electrophilic.
In this lecture, I will describe the enzymes and enzyme families,
the structure and mechanism of glutathione transferases,
their regulation and highly versatile functions.
I will refer to glutathione transferases also by their common abbreviation GSTs.
0:57
There are three superfamilies of glutathione transferases.
The soluble diameric enzymes,
the membrane bound trimeric enzymes and the fosfomycin resistance protein.
Soluble also called cytosolic and membrane bound glutathione transferases
have been found in all aerobic organisms,
whereas fosfomycin resistance protein is found in bacteria.
All of the enzymes involved in
xenobiotic metabolism display very broad substrate specificity,
whereas the fosfomycin resistance protein is clearly
different since it is specific for one substrate only.