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脱氨基作用,细胞内从有机化合物分子上除去氨基的酶促反应,是机体内 氨基酸代谢的第一步。脱氨基作用有氧化脱氨, 转氨,联合脱氨和非氧化脱氨等方式。其中以 联合脱氨基最为重要。 氧化脱氨作用基作用普遍存在于动植物细胞中,动物的脱氨基作用主要在肝脏进行;非氧化脱氨基作用见于微生物,但并不普遍。生物中许多含氨基的化合物在分解代谢过程里几乎都有这类反应。这些化合物包括各种 氨基酸、 腺嘌呤、 鸟嘌呤、 胞嘧啶及它们的衍生物。脱氨基作用是由各种脱氨酶催化的,反应产物是对应的酮基化合物。在氨基酸的分解代谢中, L-谷氨酸的氧化性脱氨作用很重要。因为在许多生物中只有谷氨酸一种氨基酸能进行氧化性脱氨,催化这一反应的谷氨酸脱氢酶的专一性又较高。现在认为,至少在动物体内,大部分氨基酸是通过氨基转换和谷氨酸氧化脱氨的联合作用脱氨的,也可通过此联合作用的逆反应合成某些氨基酸。
氧化脱氨基作用是指氨基酸在脱氨基时伴有氧化(脱氢)过程。
催化氧化脱氨基的酶有氨基酸氧化酶和L-谷氨酸脱氢酶。 L-谷氨酸脱氢酶是以NAD+(或NADP+)为辅酶的不需氧脱氢酶,其在体内分布广(除肌肉组织外)、活性强,能催化L-谷氨酸氧化脱氨,生成α-酮戊二酸。
L-谷氨酸脱氢酶的催化反应是可逆的。当谷氨酸浓度高时,则向分解方向进行。由于L-谷氨酸脱氢酶的底物仅限于L-谷氨酸,因此不是体内理想的脱氨基过程。
氨基转移作用在各组织细胞普遍存在。催化转氨基作用的酶,称为氨基转移酶或简称转氨酶。它的作用是使氨基酸的α-氨基转移至另一α-酮酸的羰基上。
氨基转移酶的辅酶是吡哆胺磷酸和吡哆醛磷酸,它们作为氨基传递体而起作用
氨基转移作用也是可逆反应,除个别几个氨基酸如赖氨酸、苏氨酸、脯氨酸、羟脯氨酸外,其他氨基酸都可参与氨基的转移作用。只要体内存在相应的酮酸,就可合成某种氨基酸,这是体内合成非必需氨基酸的主要途径。 丙氨酸:α-酮戊二酸氨基转移酶(称谷丙转氨酶(GPT),又称丙氨酸转氨酶(ALT) )和天冬氨酸:α-酮戊二酸氨基转移酶(称谷草转氨酶(GOT)、又称天冬氨酸转氨酶(AST))两种酶很重要。
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