Brenda Martins Vasconcellos , Victor Guimarães Ribeiro , Naysha do Nascimento Campos , Luis Guilherme da Silva Romão Mota , Mônica Ferreira Moreira
{"title":"A comprehensive review of arginine kinase proteins: What we need to know?","authors":"Brenda Martins Vasconcellos , Victor Guimarães Ribeiro , Naysha do Nascimento Campos , Luis Guilherme da Silva Romão Mota , Mônica Ferreira Moreira","doi":"10.1016/j.bbrep.2024.101837","DOIUrl":null,"url":null,"abstract":"<div><div>The enzyme arginine kinase (AK), EC 2.7.3.3, catalyzes the reversible phosphorylation of arginine with adenosine triphosphate, forming phosphoarginine, which acts as an energy reservoir due to its high-energy phosphate content that can be rapidly transferred to ADP for ATP renewal. It has been proposed that AK should be associated with some ATP biosynthesis mechanisms, such as glycolysis and oxidative phosphorylation. Arginine kinase is an analogue of creatine kinase found in vertebrates. A literature survey has recovered the physicochemical and structural characteristics of AK. This enzyme is widely distributed in invertebrates such as protozoa, bacteria, porifera, cnidaria, mollusca, and arthropods. Arginine kinase may be involved in the response to abiotic and biotic stresses, being up regulated in several organisms and controlling energy homeostasis during environmental changes. Additionally, phosphoarginine plays a role in providing energy for the transport of protozoa, the beating of cilia, and flagellar movement, processes that demand continuous energy. Arginine kinase is also associated with allergies to shellfish and arthropods, such as shrimp, oysters, and cockroaches. Phenolic compounds such as resveratrol, which decrease AK activity by 50 % in <em>Trypanosoma cruzi,</em> inhibit the growth of the epimastigote and trypomastigote forms, making them a significant target for the development of medications for Chagas Disease treatment.</div></div>","PeriodicalId":8771,"journal":{"name":"Biochemistry and Biophysics Reports","volume":"40 ","pages":"Article 101837"},"PeriodicalIF":2.3000,"publicationDate":"2024-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and Biophysics Reports","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2405580824002012","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
The enzyme arginine kinase (AK), EC 2.7.3.3, catalyzes the reversible phosphorylation of arginine with adenosine triphosphate, forming phosphoarginine, which acts as an energy reservoir due to its high-energy phosphate content that can be rapidly transferred to ADP for ATP renewal. It has been proposed that AK should be associated with some ATP biosynthesis mechanisms, such as glycolysis and oxidative phosphorylation. Arginine kinase is an analogue of creatine kinase found in vertebrates. A literature survey has recovered the physicochemical and structural characteristics of AK. This enzyme is widely distributed in invertebrates such as protozoa, bacteria, porifera, cnidaria, mollusca, and arthropods. Arginine kinase may be involved in the response to abiotic and biotic stresses, being up regulated in several organisms and controlling energy homeostasis during environmental changes. Additionally, phosphoarginine plays a role in providing energy for the transport of protozoa, the beating of cilia, and flagellar movement, processes that demand continuous energy. Arginine kinase is also associated with allergies to shellfish and arthropods, such as shrimp, oysters, and cockroaches. Phenolic compounds such as resveratrol, which decrease AK activity by 50 % in Trypanosoma cruzi, inhibit the growth of the epimastigote and trypomastigote forms, making them a significant target for the development of medications for Chagas Disease treatment.
精氨酸激酶(AK)(EC 2.7.3.3)催化精氨酸与三磷酸腺苷发生可逆磷酸化反应,形成磷精氨酸,由于磷精氨酸含有高能磷酸,可迅速转化为 ADP 用于 ATP 的更新,因此可作为能量储备。有人提出,精氨酸激酶与某些 ATP 生物合成机制有关,如糖酵解和氧化磷酸化。精氨酸激酶是脊椎动物体内肌酸激酶的类似物。一项文献调查发现了精氨酸激酶的理化和结构特征。这种酶广泛分布于无脊椎动物,如原生动物、细菌、多孔动物、刺丝胞动物、软体动物和节肢动物。精氨酸激酶可能参与了对非生物和生物压力的反应,在一些生物体内被上调,并在环境变化时控制能量平衡。此外,磷精氨酸还在为原生动物的运输、纤毛跳动和鞭毛运动等需要持续能量的过程提供能量方面发挥作用。精氨酸激酶还与对贝类和节肢动物(如虾、牡蛎和蟑螂)过敏有关。酚类化合物(如白藜芦醇)能使克氏锥虫的精氨酸激酶活性降低 50%,从而抑制表表型和试表型锥虫的生长,使其成为开发治疗南美锥虫病药物的重要目标。
期刊介绍:
Open access, online only, peer-reviewed international journal in the Life Sciences, established in 2014 Biochemistry and Biophysics Reports (BB Reports) publishes original research in all aspects of Biochemistry, Biophysics and related areas like Molecular and Cell Biology. BB Reports welcomes solid though more preliminary, descriptive and small scale results if they have the potential to stimulate and/or contribute to future research, leading to new insights or hypothesis. Primary criteria for acceptance is that the work is original, scientifically and technically sound and provides valuable knowledge to life sciences research. We strongly believe all results deserve to be published and documented for the advancement of science. BB Reports specifically appreciates receiving reports on: Negative results, Replication studies, Reanalysis of previous datasets.