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Glyoxalase domain-containing protein 4 (GLOD4)
- Target
- GLOD4
- Molecular classification
- Glyoxalase domain-containing protein, Vicinal oxygen chelate (VOC) superfamily, Metalloenzyme (putative, based on domain), Other (function not clearly established)
01
Overview
Glyoxalase domain-containing protein 4 is a member of the glyoxalase gene family, characterized by the presence of a glyoxalase domain and vicinal oxygen chelate (VOC) motif. It is considered an ancient paralog of glyoxalase 1 (GLO1), but its enzymatic activity, metal-binding properties, and physiological function remain uncharacterized in humans. There are multiple spliced isoforms with conserved glyoxalase domains. While related glyoxalases are involved in detoxifying reactive dicarbonyl compounds and have recognized roles in metabolic diseases, the function of GLOD4 is unknown. Cadherin binding activity has been annotated, but its biological and clinical relevance is unclear. GLOD4 has no reported drug interactions or clinical utility as a therapeutic target, and further research is needed to elucidate its biological function. Family-level functions involve metabolism and cellular stress responses, but specific roles for GLOD4 have not yet been determined[1][2][3][4][5].
- Other names
- GLOD4C17orf25CGI-150HC71glyoxalase domain containing 4HC6My027
02
Biological functions
Other (No confirmed biological function in humans)Predicted: May be involved in reactive dicarbonyl detoxification and metabolic homeostasis, seen in related glyoxalase family membersCadherin binding activity (experimental annotation)
03
Disease associations
Other (Insufficient evidence for specific disease association)Reported relationships with congenital myopathy 4A and Hawkinsinuria, but no mechanistic evidenceFamily implicated in metabolic disease, cancer, diabetes in broader context of dicarbonyl stressHeavily expressed in Leydig cells in certain mammalian models, suggesting possible testicular development involvement (unconfirmed relevance in humans)
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