V. I. Tishkov, M. D. Shelomov, A. A. Pometun, S. S. Savin, D. L. Atroshenko
{"title":"d -氨基酸的生理作用和d -氨基酸氧化酶的生物分析潜力","authors":"V. I. Tishkov, M. D. Shelomov, A. A. Pometun, S. S. Savin, D. L. Atroshenko","doi":"10.3103/S0027131423010066","DOIUrl":null,"url":null,"abstract":"<p>D-amino acid oxidase (DAAO) plays an important role in the functioning of both prokaryotes and eukaryotes. DAAO is increasingly being used in practice, including for the determination of D-amino acids in complex samples, involving human tissues and fluids. There are generally two types of DAAO in all organisms. The first type is an enzyme highly specific for D-aspartate and has its own name D-aspartate oxidase (DASPO). DAAO of the second type is characterized by a wide spectrum of substrate specificity, with preference for one or another D-amino acid varying from source to source. The activity of DAAO with a large number of substrates greatly complicates the selective determination of a particular D-amino acid. The problem is often solved by choosing an enzyme that, under the conditions of analysis, has low or no activity with other D-amino acids present in the sample. For the convenience of selecting a particular enzyme, we have collected and analyzed literature data on the catalytic parameters of known DAAOs with the most important D-amino acids. In addition, similar data are presented for novel recombinant DAAOs from the methylotrophic yeast <i>Ogataea parapolymorpha</i> DL-1. Analysis of the data shows that, with the D-amino acid series, the new OpaDASPO and OpaDAAO have the highest catalytic parameters.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"78 1","pages":"1 - 9"},"PeriodicalIF":0.7000,"publicationDate":"2023-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Physiological Role of D-amino Acids and Bioanalytical Potential of D-amino Acid Oxidases\",\"authors\":\"V. I. Tishkov, M. D. Shelomov, A. A. Pometun, S. S. Savin, D. L. Atroshenko\",\"doi\":\"10.3103/S0027131423010066\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>D-amino acid oxidase (DAAO) plays an important role in the functioning of both prokaryotes and eukaryotes. DAAO is increasingly being used in practice, including for the determination of D-amino acids in complex samples, involving human tissues and fluids. There are generally two types of DAAO in all organisms. The first type is an enzyme highly specific for D-aspartate and has its own name D-aspartate oxidase (DASPO). DAAO of the second type is characterized by a wide spectrum of substrate specificity, with preference for one or another D-amino acid varying from source to source. The activity of DAAO with a large number of substrates greatly complicates the selective determination of a particular D-amino acid. The problem is often solved by choosing an enzyme that, under the conditions of analysis, has low or no activity with other D-amino acids present in the sample. For the convenience of selecting a particular enzyme, we have collected and analyzed literature data on the catalytic parameters of known DAAOs with the most important D-amino acids. In addition, similar data are presented for novel recombinant DAAOs from the methylotrophic yeast <i>Ogataea parapolymorpha</i> DL-1. Analysis of the data shows that, with the D-amino acid series, the new OpaDASPO and OpaDAAO have the highest catalytic parameters.</p>\",\"PeriodicalId\":709,\"journal\":{\"name\":\"Moscow University Chemistry Bulletin\",\"volume\":\"78 1\",\"pages\":\"1 - 9\"},\"PeriodicalIF\":0.7000,\"publicationDate\":\"2023-04-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Moscow University Chemistry Bulletin\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://link.springer.com/article/10.3103/S0027131423010066\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Moscow University Chemistry Bulletin","FirstCategoryId":"1085","ListUrlMain":"https://link.springer.com/article/10.3103/S0027131423010066","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
Physiological Role of D-amino Acids and Bioanalytical Potential of D-amino Acid Oxidases
D-amino acid oxidase (DAAO) plays an important role in the functioning of both prokaryotes and eukaryotes. DAAO is increasingly being used in practice, including for the determination of D-amino acids in complex samples, involving human tissues and fluids. There are generally two types of DAAO in all organisms. The first type is an enzyme highly specific for D-aspartate and has its own name D-aspartate oxidase (DASPO). DAAO of the second type is characterized by a wide spectrum of substrate specificity, with preference for one or another D-amino acid varying from source to source. The activity of DAAO with a large number of substrates greatly complicates the selective determination of a particular D-amino acid. The problem is often solved by choosing an enzyme that, under the conditions of analysis, has low or no activity with other D-amino acids present in the sample. For the convenience of selecting a particular enzyme, we have collected and analyzed literature data on the catalytic parameters of known DAAOs with the most important D-amino acids. In addition, similar data are presented for novel recombinant DAAOs from the methylotrophic yeast Ogataea parapolymorpha DL-1. Analysis of the data shows that, with the D-amino acid series, the new OpaDASPO and OpaDAAO have the highest catalytic parameters.
期刊介绍:
Moscow University Chemistry Bulletin is a journal that publishes review articles, original research articles, and short communications on various areas of basic and applied research in chemistry, including medical chemistry and pharmacology.