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Target intelligence / Profile preview
Hydroxyacylglutathione hydrolase (HAGH)
- Target
- HAGH
- Molecular classification
- Enzyme, Thiolesterase
01
Overview
Hydroxyacylglutathione hydrolase (HAGH), also known as glyoxalase II, is a thiolesterase enzyme integral to the glyoxalase system, where it catalyzes the hydrolysis of S-lactoyl-glutathione to yield reduced glutathione and D-lactate[1][2][3][4][5]. This process detoxifies methylglyoxal, a reactive glycolytic by-product linked to advanced glycation end product (AGE) formation and cellular damage[1][3]. HAGH is expressed as both cytosolic and mitochondrial isoforms, ensuring detoxification in different cellular compartments[2]. Its regulation links cellular redox balance, oxidative stress, and survival pathways, implicating it in cancer, metabolic syndrome, neurodegenerative disease, and other stress-related disorders[1][4].
- Other names
- Glyoxalase IIGLO2GLXIIGLX2HAGH1hydroxyacylglutathione hydrolase, mitochondrialglyoxalase IIS-lactoyl-glutathione hydrolase
02
Mechanism of action
Catalytic inhibition or modulation of glyoxalase II activity, modulation of methylglyoxal detoxification and cellular redox homeostasis
03
Biological functions
Detoxification of methylglyoxalHydrolysis of S-lactoyl-glutathioneRecycling of glutathioneCellular redox balanceCellular protection from glycative and oxidative stress
04
Disease associations
CancerNeurodegenerative diseaseAbdominal obesity-metabolic syndromeOther (hydroxyacyl glutathione hydrolase deficiency)
05
Safety considerations
Potential for off-target impairment of cellular detoxification pathwaysdisturbance of cellular redox status
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