In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family

Boopathi Subramani, K. Hwa
{"title":"In silico Analysis for Enhancing the Rubisco Activity among the C3 Plants of Poaceae Family","authors":"Boopathi Subramani, K. Hwa","doi":"10.1109/ITCS.2010.5581267","DOIUrl":null,"url":null,"abstract":"Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in CO_2 fixation. It is an important enzyme for biomass production, especially for alternate energy production. Rubisco is an inefficient catalyst. Its carboxylase activity is compromised by numerous side-reactions including oxygenation of the sugar phosphate substrate by atmospheric O_2. However, naturally occurring enzyme variants with different kinetic properties suggest that it is possible to alter the enzyme to be in favor of the carboxylation activity than of the oxygenation. In this study the C_3 and C_4 plants of Poaceae family with variation in Rubisco activity was phylogenetically analyzed. Our analysis focused on the key regulatory mechanisms such as phosphorylation sites of the enzymes and suggests that these phosphorylation sites can be a putative target site to engineer Rubisco in C_3 plants to increase the turnover rate for CO_2 fixation that can be important for biomass generation.","PeriodicalId":166169,"journal":{"name":"2010 2nd International Conference on Information Technology Convergence and Services","volume":"75 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2010-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"2010 2nd International Conference on Information Technology Convergence and Services","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ITCS.2010.5581267","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the key enzyme involved in CO_2 fixation. It is an important enzyme for biomass production, especially for alternate energy production. Rubisco is an inefficient catalyst. Its carboxylase activity is compromised by numerous side-reactions including oxygenation of the sugar phosphate substrate by atmospheric O_2. However, naturally occurring enzyme variants with different kinetic properties suggest that it is possible to alter the enzyme to be in favor of the carboxylation activity than of the oxygenation. In this study the C_3 and C_4 plants of Poaceae family with variation in Rubisco activity was phylogenetically analyzed. Our analysis focused on the key regulatory mechanisms such as phosphorylation sites of the enzymes and suggests that these phosphorylation sites can be a putative target site to engineer Rubisco in C_3 plants to increase the turnover rate for CO_2 fixation that can be important for biomass generation.
提高禾科C3植物Rubisco活性的硅片分析
核酮糖-1,5-二磷酸羧化酶/加氧酶(Rubisco)是参与CO_2固定的关键酶。它是生物质生产,特别是替代能源生产的重要酶。Rubisco是一种低效催化剂。它的羧化酶活性受到许多副反应的影响,包括磷酸糖底物被大气中的氧气氧化。然而,天然存在的具有不同动力学性质的酶变体表明,有可能改变酶,使其有利于羧化活性而不是氧化活性。本文对禾科C_3和C_4植物Rubisco活性的变化进行了系统发育分析。我们的分析集中在关键的调控机制上,如酶的磷酸化位点,并表明这些磷酸化位点可能是C_3植物中设计Rubisco的一个假定的靶点,以提高CO_2固定的周转率,这对生物质产生是重要的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信