该综述考虑了糖酵解酶精子特异性甘油醛-3-磷酸脱氢酶（GAPDS）对精子能量代谢以及精子和其他细胞中多种病理发生的影响。GAPDS是一种唯一存在于哺乳动物精子中的酶。GAPDS通过糖酵解反应中的ATP形成提供精子鞭毛运动。 GAPDS中半胱氨酸残基的氧化导致酶的失活并降低精子的运动能力。特别是在糖尿病中，GAPDS被糖基化反应产生的超氧阴离子氧化。 GAPDS基因突变导致运动能力的丧失，并且在某些情况下破坏精子鞭毛的结构元素形成，而该酶在精子发生过程中被结合。 GAPDS激活可以用于增加精子的生育能力，而该酶的抑制剂正在尝试作为避孕药。在黑色素瘤细胞系中和黑色素瘤和其他肿瘤标本中发现了缺乏连接酶与精子鞭毛的N端72个氨基酸片段的截短GAPDS。肿瘤细胞中同时产生体细胞形式的GAPDH和精子特异性GAPDS引起能量代谢的重组，这伴随着某些癌症形式转移效率的变化。讨论了使用GAPDS诊断癌症的问题，以及调节该酶的活性以预防转移的可能性。版权所有© 2023 Naletova，Schmalhausen，Tomasello，Pozdyshev，Attanasio和Muronetz。

The review considers various aspects of the influence of the glycolytic enzyme, sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) on the energy metabolism of spermatozoa and on the occurrence of several pathologies both in spermatozoa and in other cells. GAPDS is a unique enzyme normally found only in mammalian spermatozoa. GAPDS provides movement of the sperm flagellum through the ATP formation in glycolytic reactions. Oxidation of cysteine residues in GAPDS results in inactivation of the enzyme and decreases sperm motility. In particular, reduced sperm motility in diabetes can be associated with GAPDS oxidation by superoxide anion produced during glycation reactions. Mutations in GAPDS gene lead in the loss of motility, and in some cases, disrupts the formation of the structural elements of the sperm flagellum, in which the enzyme incorporates during spermiogenesis. GAPDS activation can be used to increase the spermatozoa fertility, and inhibitors of this enzyme are being tried as contraceptives. A truncated GAPDS lacking the N-terminal fragment of 72 amino acids that attaches the enzyme to the sperm flagellum was found in melanoma cell lines and then in specimens of melanoma and other tumors. Simultaneous production of the somatic form of GAPDH and sperm-specific GAPDS in cancer cells leads to a reorganization of their energy metabolism, which is accompanied by a change in the efficiency of metastasis of certain forms of cancer. Issues related to the use of GAPDS for the diagnosis of cancer, as well as the possibility of regulating the activity of this enzyme to prevent metastasis, are discussed.Copyright © 2023 Naletova, Schmalhausen, Tomasello, Pozdyshev, Attanasio and Muronetz.