来自人类和大肠杆菌的血清氧甲基转移酶的多功能性分析
Mahiro Hayashi1, Kumiko Sakai-Kato2, Tetsuya Miyamoto2
1School of Pharmacy, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo 108-8641, Japan.
Biochimica et biophysica acta. Proteins and proteomics
|December 22, 2025
概括
血清基甲基转移酶 (SHMTs) 是多功能酶. 它们表现出正规的基甲基转移酶活性,d-氨酸脱水酶活性和低特异性的l-氨酸阿尔多酶活性.
科学领域:
- 生物化学 生物化学
- 酶学 是一种酶学.
背景情况:
- 已知血清基甲基转移酶 (SHMT) 能够催化血清和甘氨酸的相互转化,利用四基酸盐 (THF).
- 以前的研究表明,SHMTs具有THF依赖的d-氨酸脱水酶活性和潜在的阿尔多酶/赛马酶功能.
- SHMT的多功能性需要进一步研究.
研究的目的:
- 调查大肠杆菌SHMT和两个人类SHMT的多功能性.
- 描述SHMTs对各种酶活性的基质特异性和催化效率.
主要方法:
- 进行了酶试验,以评估阿尔多酶,赛马酶,酶,氨基转移酶,阿斯巴酸脱酶和脱水酶活动.
- 确定了特定基板的动力参数,包括催化效率 (kcat/Km).
主要成果:
- 所有测试的SHMT都显示出对l-三胺和l-三胺的显著阿尔多酶活性,对l-三胺的催化效率更高.
- 对于大肠杆菌SHMT,观察到最小的氨酸赛马体活性,而其他测试的赛马体活性是可以忽略不计的.
- SHMTs对d-serine表现出特定的脱水酶活性,而不是其他氨基酸,并且缺乏酶,氨基转移酶和酸盐脱碳酶活性.
结论:
- 证实SHMT是一种多功能酶.
- 主要活动包括正规氧甲基转移酶,d-氨酸脱水酶和低特异性的l-氨酸阿尔多酶.
- 酶的基质特异性超出了其正规作用,突出了其多功能的酶能力.
关键词:
氨基酸赛马酶的氨基酸赛马酶.多功能性 多功能性血清氧甲基转移酶的氧甲基转移酶.叶酸四酸 (tetrahydrofolate) 是一种酸的化合物.三氨酸阿尔多酶的使用.在d-氨基酸中.在d-Serine脱水酶.更多相关视频
相关概念视频
Allosteric Proteins-ATCase
6.4K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
6.4K
Ligand Binding and Linkage
5.4K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.4K
tRNA Activation
22.4K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
22.4K


