羟酰谷胱甘肽水解酶： 由该基因编码的酶被归类为硫酯酶，负责将 S-乳酰谷胱甘肽水解为还原型谷胱甘肽和 D-乳酸。已发现该基因的三个转录变体编码不同的亚型。[RefSeq 提供，2013 年 10 月]

2024年12月25日 · HAGH (Hydroxyacylglutathione Hydrolase) is a Protein Coding gene. Diseases associated with HAGH include Hydroxyacyl Glutathione Hydrolase Deficiency and Abdominal Obesity-Metabolic Syndrome 1.

Hydroxyacylglutathione hydrolase, mitochondrial is an enzyme that in humans is encoded by the HAGH gene. [5][6][7] The enzyme encoded by this gene is classified as a thiolesterase and is responsible for the hydrolysis of S-lactoyl-glutathione to reduced glutathione and D-lactate.

2024年11月4日 · This study suggested that HAGH, rs11859266 and rs3743852 showed significant associations with schizophrenia in males at allelic and genotype levels.

In androgen-independent prostate cancer cells, it downregulates GLO2 mRNA. Data show that the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73. hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II Overexpression of glyoxalase II is associated with kidney tumor

HAGH的详细信息，包括基因名称，代码，染色体位置，相互作用关系和通路，简述为由该基因编码的酶被分类为thiolesterase并负责S-乳酰谷胱甘肽的水解还原的谷胱甘肽和D-乳酸。

2016年9月14日 · Gene target information for HAGH - hydroxyacylglutathione hydrolase (human). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.

预测在甲基乙二醛代谢过程的上游或S-乳酰谷胱甘肽内发挥作用，最终生成D-乳酸。 位于线粒体中。 在几个结构中表达，包括消化系统；大脑；生殖泌尿系统；呼吸系统；和感觉器官。 与人类的HAGH（羟基酰谷胱甘肽水解酶）正同源。

功能概要 Enables hydroxyacylglutathione hydrolase activity. Involved in carbohydrate metabolic process and glutathione metabolic process. Predicted to be located in mitochondrial matrix. Predicted to be active in mitochondrion. Orthologous to human HAGH (hydroxyacylglutathione hydrolase). [provided by Alliance of Genome Resources, Apr 2022]

In this paper, we demonstrate that extended transcripts from the human HAGH gene encode both cytosolic and mitochondrial isoforms of glyoxalase II, and that the previous mRNA sequence is incomplete. The cytosolic form originates by internal priming of protein synthesis from the initiating AUG codon previously identified in exon 1 (5).