{"title":"整合多种酶活性调控:以磷酸烯醇丙酮酸羧化激酶为例。","authors":"Bruno E Rojas, Alberto A Iglesias","doi":"10.1093/aobpla/plad053","DOIUrl":null,"url":null,"abstract":"<p><p>Data on protein post-translational modifications (PTMs) increased exponentially in the last years due to the refinement of mass spectrometry techniques and the development of databases to store and share datasets. Nevertheless, these data per se do not create comprehensive biochemical knowledge. Complementary studies on protein biochemistry are necessary to fully understand the function of these PTMs at the molecular level and beyond, for example, designing rational metabolic engineering strategies to improve crops. Phospho<i>enol</i>pyruvate carboxykinases (PEPCKs) are critical enzymes for plant metabolism with diverse roles in plant development and growth. Multiple lines of evidence showed the complex regulation of PEPCKs, including PTMs. Herein, we present PEPCKs as an example of the integration of combined mechanisms modulating enzyme activity and metabolic pathways. PEPCK studies strongly advanced after the production of the recombinant enzyme and the establishment of standardized biochemical assays. Finally, we discuss emerging open questions for future research and the challenges in integrating all available data into functional biochemical models.</p>","PeriodicalId":48955,"journal":{"name":"AoB Plants","volume":"15 4","pages":"plad053"},"PeriodicalIF":2.6000,"publicationDate":"2023-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441589/pdf/","citationCount":"0","resultStr":"{\"title\":\"Integrating multiple regulations on enzyme activity: the case of phospho<i>enol</i>pyruvate carboxykinases.\",\"authors\":\"Bruno E Rojas, Alberto A Iglesias\",\"doi\":\"10.1093/aobpla/plad053\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Data on protein post-translational modifications (PTMs) increased exponentially in the last years due to the refinement of mass spectrometry techniques and the development of databases to store and share datasets. Nevertheless, these data per se do not create comprehensive biochemical knowledge. Complementary studies on protein biochemistry are necessary to fully understand the function of these PTMs at the molecular level and beyond, for example, designing rational metabolic engineering strategies to improve crops. Phospho<i>enol</i>pyruvate carboxykinases (PEPCKs) are critical enzymes for plant metabolism with diverse roles in plant development and growth. Multiple lines of evidence showed the complex regulation of PEPCKs, including PTMs. Herein, we present PEPCKs as an example of the integration of combined mechanisms modulating enzyme activity and metabolic pathways. PEPCK studies strongly advanced after the production of the recombinant enzyme and the establishment of standardized biochemical assays. Finally, we discuss emerging open questions for future research and the challenges in integrating all available data into functional biochemical models.</p>\",\"PeriodicalId\":48955,\"journal\":{\"name\":\"AoB Plants\",\"volume\":\"15 4\",\"pages\":\"plad053\"},\"PeriodicalIF\":2.6000,\"publicationDate\":\"2023-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441589/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"AoB Plants\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1093/aobpla/plad053\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"ECOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"AoB Plants","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/aobpla/plad053","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"ECOLOGY","Score":null,"Total":0}
Integrating multiple regulations on enzyme activity: the case of phosphoenolpyruvate carboxykinases.
Data on protein post-translational modifications (PTMs) increased exponentially in the last years due to the refinement of mass spectrometry techniques and the development of databases to store and share datasets. Nevertheless, these data per se do not create comprehensive biochemical knowledge. Complementary studies on protein biochemistry are necessary to fully understand the function of these PTMs at the molecular level and beyond, for example, designing rational metabolic engineering strategies to improve crops. Phosphoenolpyruvate carboxykinases (PEPCKs) are critical enzymes for plant metabolism with diverse roles in plant development and growth. Multiple lines of evidence showed the complex regulation of PEPCKs, including PTMs. Herein, we present PEPCKs as an example of the integration of combined mechanisms modulating enzyme activity and metabolic pathways. PEPCK studies strongly advanced after the production of the recombinant enzyme and the establishment of standardized biochemical assays. Finally, we discuss emerging open questions for future research and the challenges in integrating all available data into functional biochemical models.
期刊介绍:
AoB PLANTS is an open-access, online journal that has been publishing peer-reviewed articles since 2010, with an emphasis on all aspects of environmental and evolutionary plant biology. Published by Oxford University Press, this journal is dedicated to rapid publication of research articles, reviews, commentaries and short communications. The taxonomic scope of the journal spans the full gamut of vascular and non-vascular plants, as well as other taxa that impact these organisms. AoB PLANTS provides a fast-track pathway for publishing high-quality research in an open-access environment, where papers are available online to anyone, anywhere free of charge.