{"title":"真菌和细菌天冬酰胺酶的分子内比较。","authors":"Negar Tafvizi, Mandana Behbahani, Hassan Mohabatkar","doi":"10.22099/mbrc.2024.50123.1981","DOIUrl":null,"url":null,"abstract":"<p><p>L-asparaginase is a commercial enzyme with a wide variety of applications. Asparaginase is known as an anti-cancer agent that is effective for the treatment of certain lymphomas and leukemias by growth inhibition of human cancer cells. Additionally, asparaginase is used in the food industry in a pretreatment process to decrease the accumulation of carcinogenic acrylamide. In this paper, different aspects of bacterial and fungal asparaginases such as mass, hydrophobicity and hydrophilicity of pseudo amino acid composition (PseAAC), physicochem-ical properties, and structural motifs were studied, and ROC curve statistical analysis was used for the comparison. The results showed that none of the physicochemical properties of fungal and bacterial asparaginase could not be differed, except molecular weight and sequence length. MEME Suite analysis demonstrated that there was a motif that was specific for bacterial asparaginases. However, analysis based on the concept of PseACC indicated a differentiation line between fungal and bacterial asparaginases. In conclusion, although there was not any specific demonstration to separate the bacterial and fungal asparaginases in the case of physicochemical properties, PseAAC analysis can be an appropriate and usable method to differentiate between them.</p>","PeriodicalId":19025,"journal":{"name":"Molecular Biology Research Communications","volume":"13 4","pages":"183-191"},"PeriodicalIF":1.5000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11416853/pdf/","citationCount":"0","resultStr":"{\"title\":\"In-silico comparison of fungal and bacterial asparaginase enzymes.\",\"authors\":\"Negar Tafvizi, Mandana Behbahani, Hassan Mohabatkar\",\"doi\":\"10.22099/mbrc.2024.50123.1981\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>L-asparaginase is a commercial enzyme with a wide variety of applications. Asparaginase is known as an anti-cancer agent that is effective for the treatment of certain lymphomas and leukemias by growth inhibition of human cancer cells. Additionally, asparaginase is used in the food industry in a pretreatment process to decrease the accumulation of carcinogenic acrylamide. In this paper, different aspects of bacterial and fungal asparaginases such as mass, hydrophobicity and hydrophilicity of pseudo amino acid composition (PseAAC), physicochem-ical properties, and structural motifs were studied, and ROC curve statistical analysis was used for the comparison. The results showed that none of the physicochemical properties of fungal and bacterial asparaginase could not be differed, except molecular weight and sequence length. MEME Suite analysis demonstrated that there was a motif that was specific for bacterial asparaginases. However, analysis based on the concept of PseACC indicated a differentiation line between fungal and bacterial asparaginases. In conclusion, although there was not any specific demonstration to separate the bacterial and fungal asparaginases in the case of physicochemical properties, PseAAC analysis can be an appropriate and usable method to differentiate between them.</p>\",\"PeriodicalId\":19025,\"journal\":{\"name\":\"Molecular Biology Research Communications\",\"volume\":\"13 4\",\"pages\":\"183-191\"},\"PeriodicalIF\":1.5000,\"publicationDate\":\"2024-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11416853/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular Biology Research Communications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.22099/mbrc.2024.50123.1981\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Biology Research Communications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.22099/mbrc.2024.50123.1981","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
摘要
L- 天冬酰胺酶是一种用途广泛的商用酶。众所周知,天冬酰胺酶是一种抗癌剂,通过抑制人类癌细胞的生长,可有效治疗某些淋巴瘤和白血病。此外,天冬酰胺酶还被用于食品工业的预处理过程,以减少致癌物质丙烯酰胺的积累。本文研究了细菌和真菌天冬酰胺酶的不同方面,如质量、假氨基酸组成(PseAAC)的疏水性和亲水性、理化性质和结构基团,并采用 ROC 曲线统计分析进行比较。结果表明,除分子量和序列长度外,真菌和细菌天冬酰胺酶的理化性质均无差异。MEME Suite 分析表明,细菌天冬酰胺酶有一个特异的主题。不过,基于 PseACC 概念的分析表明,真菌和细菌天冬酰胺酶之间存在着一条分界线。总之,虽然在理化性质方面没有任何具体的证据可以区分细菌和真菌天冬酰胺酶,但 PseAAC 分析可以作为区分它们的一种适当和可用的方法。
In-silico comparison of fungal and bacterial asparaginase enzymes.
L-asparaginase is a commercial enzyme with a wide variety of applications. Asparaginase is known as an anti-cancer agent that is effective for the treatment of certain lymphomas and leukemias by growth inhibition of human cancer cells. Additionally, asparaginase is used in the food industry in a pretreatment process to decrease the accumulation of carcinogenic acrylamide. In this paper, different aspects of bacterial and fungal asparaginases such as mass, hydrophobicity and hydrophilicity of pseudo amino acid composition (PseAAC), physicochem-ical properties, and structural motifs were studied, and ROC curve statistical analysis was used for the comparison. The results showed that none of the physicochemical properties of fungal and bacterial asparaginase could not be differed, except molecular weight and sequence length. MEME Suite analysis demonstrated that there was a motif that was specific for bacterial asparaginases. However, analysis based on the concept of PseACC indicated a differentiation line between fungal and bacterial asparaginases. In conclusion, although there was not any specific demonstration to separate the bacterial and fungal asparaginases in the case of physicochemical properties, PseAAC analysis can be an appropriate and usable method to differentiate between them.
期刊介绍:
“Molecular Biology Research Communications” (MBRC) is an international journal of Molecular Biology. It is published quarterly by Shiraz University (Iran). The MBRC is a fully peer-reviewed journal. The journal welcomes submission of Original articles, Short communications, Invited review articles, and Letters to the Editor which meets the general criteria of significance and scientific excellence in all fields of “Molecular Biology”.