Enzymes最新文献_第9页

Flavoenzymes for biocatalysis. 用于生物催化的黄酶。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-07-18 DOI: 10.1016/bs.enz.2020.05.001

Mélanie Hall

引用次数: 6

Flavin-dependent dehalogenases. Flavin-dependent dehalogenases。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-08-24 DOI: 10.1016/bs.enz.2020.05.010

Panu Pimviriyakul, Pimchai Chaiyen

{"title":"Flavin-dependent dehalogenases.","authors":"Panu Pimviriyakul, Pimchai Chaiyen","doi":"10.1016/bs.enz.2020.05.010","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.05.010","url":null,"abstract":"Flavin-dependent dehalogenases use flavin as a cofactor to catalyze carbon-halogen (C-X) bond cleavage from halogenated compounds which are mainly distributed as persistent environmental pollutants via anthropogenic activities. The accumulation of these compounds results in adaptation of bacteria to evolve metabolic pathways to metabolize the agents for four decades. Flavin-dependent enzymes have been evolved to catalyze dehalogenation in addition to its basal function. Apart from bacterial biodegradation, flavin-dependent dehalogenases also naturally appear in cellular metabolisms of higher organisms such as in human thyroid hormone. Although the removal of halogen is required in various applications, the usage of dehalogenases remains limited. In-depth understanding of their enzymatic mechanisms is useful for development of dehalogenases applications. Three main types of flavin-dependent dehalogenases are classified based on their reaction mechanisms reported to date: (1) flavin-dependent O2-utilizing dehalogenases; (2) flavin-dependent reductive dehalogenases; and (3) non-redox flavin-dependent dehalogenases. In this chapter, the catalytic properties, substrate scope, protein structures, enzymatic mechanisms, enzyme engineering, and also development of enzymes for novel applications are discussed.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"47 ","pages":"365-397"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.05.010","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38401150","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Biochemistry of prenylated-FMN enzymes. 预甲基化fmn酶的生物化学。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-07-18 DOI: 10.1016/bs.enz.2020.05.013

Annica Saaret, Arune Balaikaite, David Leys

{"title":"Biochemistry of prenylated-FMN enzymes.","authors":"Annica Saaret, Arune Balaikaite, David Leys","doi":"10.1016/bs.enz.2020.05.013","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.05.013","url":null,"abstract":"The reversible (de)carboxylation of unsaturated carboxylic acids is carried out by the UbiX-UbiD system, ubiquitously present in microbes. The biochemical basis of this challenging reaction has recently been uncovered by the discovery of the UbiD cofactor, prenylated FMN (prFMN). This heavily modified flavin is synthesized by the flavin prenyltransferase UbiX, which catalyzes the non-metal dependent prenyl transfer from dimethylallyl(pyro)phosphate (DMAP(P)) to the flavin N5 and C6 positions, creating a fourth non-aromatic ring. Following prenylation, prFMN undergoes oxidative maturation to form the iminium species required for UbiD activity. prFMNiminium acts as a prostethic group and is bound via metal ion mediated interactions between UbiD and the prFMNiminium phosphate moiety. The modified isoalloxazine ring is place adjacent to the E(D)-R-E UbiD signature sequent motif. The fungal ferulic acid decarboxylase Fdc from Aspergillus niger has emerged as a UbiD-model system, and has yielded atomic level insight into the prFMNiminium mediated (de)carboxylation. A wealth of data now supports a mechanism reliant on reversible 1,3 dipolar cycloaddition between substrate and cofactor for this enzyme. This poses the intriguing question whether a similar mechanism is used by all UbiD enzymes, especially those that act as carboxylases on inherently more difficult substrates such as phenylphosphate or benzene/naphthalene. Indeed, considerable variability in terms of oligomerization, domain motion and active site structure is now reported for the UbiD family.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"47 ","pages":"517-549"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.05.013","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38498527","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Non-canonical functions of human cytoplasmic tyrosyl-, tryptophanyl- and other aminoacyl-tRNA synthetases. 人细胞质酪氨酸-、色氨酸-和其他氨基- trna合成酶的非规范功能。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-06-12 DOI: 10.1016/bs.enz.2020.04.001

Keisuke Wakasugi, Takumi Yokosawa

{"title":"Non-canonical functions of human cytoplasmic tyrosyl-, tryptophanyl- and other aminoacyl-tRNA synthetases.","authors":"Keisuke Wakasugi, Takumi Yokosawa","doi":"10.1016/bs.enz.2020.04.001","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.04.001","url":null,"abstract":"Aminoacyl-tRNA synthetases catalyze the aminoacylation of their cognate tRNAs. Here we review the accumulated knowledge of non-canonical functions of human cytoplasmic aminoacyl-tRNA synthetases, especially tyrosyl- (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS). Human TyrRS and TrpRS have an extra domain. Two distinct cytokines, i.e., the core catalytic \"mini TyrRS\" and the extra C-domain, are generated from human TyrRS by proteolytic cleavage. Moreover, the core catalytic domains of human TyrRS and TrpRS function as angiogenic and angiostatic factors, respectively, whereas the full-length forms are inactive for this function. It is also known that many synthetases change their localization in response to a specific signal and subsequently exhibit alternative functions. Furthermore, some synthetases function as sensors for amino acids by changing their protein interactions in an amino acid-dependent manner. Further studies will be necessary to elucidate regulatory mechanisms of non-canonical functions of aminoacyl-tRNA synthetases in particular, by analyzing the effect of their post-translational modifications.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"48 ","pages":"207-242"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.04.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25576704","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 5

The endless frontier of tRNA synthetases. tRNA合成酶的无限前沿。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-10-14 DOI: 10.1016/bs.enz.2020.09.001

Paul Schimmel

引用次数: 2

Styrene monooxygenases, indole monooxygenases and related flavoproteins applied in bioremediation and biocatalysis. 苯乙烯单加氧酶、吲哚单加氧酶及相关黄蛋白在生物修复和生物催化中的应用。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-07-18 DOI: 10.1016/bs.enz.2020.05.011

Dirk Tischler, Antje Kumpf, Daniel Eggerichs, Thomas Heine

{"title":"Styrene monooxygenases, indole monooxygenases and related flavoproteins applied in bioremediation and biocatalysis.","authors":"Dirk Tischler, Antje Kumpf, Daniel Eggerichs, Thomas Heine","doi":"10.1016/bs.enz.2020.05.011","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.05.011","url":null,"abstract":"Styrene and indole are naturally occurring compounds, which are also produced and processed by various chemical industries. Thus, it is not surprisingly that microorganisms evolved pathways to detoxify or even to utilize those compounds as carbon sources. Especially, among bacteria several routes are described specifically for the activation and degradation of styrene and indole. Respectively, the initial attack toward these compounds occurs via a flavin-dependent monooxygenase: styrene monooxygenase (SMO) or indole monooxygenase (IMO). In the first place, SMOs have been described to initiate a styrene specific degradation. These are in general two-component systems, whereas a small FAD-reductase (SMOB) delivers reduced FAD on the expense of NADH toward the monooxygenase (SMOA). Various modes of interaction are possible and for both mostly dimeric protein subunits structural data were reported. Thus, this flavoprotein monooxygenase-especially the one from Pseudomonas putida S12 can be seen as the prototype of this class of enzymes. In the course of describing related members of this enzyme family some remarkable findings were made. For example, self-sufficient fusion proteins have been reported as well as enzymes, which could not be assigned to a styrene metabolic activity, rather to indole conversion. Later it was found that this flavoprotein group can be separated at least into two subgroups: styrene and indole monooxygenases. And both enzymes rely on a FAD-reductase to obtain the reduced cofactor (FADred), which is employed to activate molecular oxygen toward hydroperoxy-FAD, which allows substrate epoxidation and the formation of hydroxy-FAD, which finally yields H2O and oxidized FAD.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"47 ","pages":"399-425"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.05.011","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38401152","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Preface. 前言。

Enzymes Pub Date : 2020-01-01 DOI: 10.1016/S1874-6047(20)30048-2

Lluís Ribas de Pouplana, Laurie S Kaguni

引用次数: 0

Novel functions of cytoplasmic aminoacyl-tRNA synthetases shaping the hallmarks of cancer. 细胞质氨基- trna合成酶的新功能塑造癌症的特征。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-09-26 DOI: 10.1016/bs.enz.2020.06.005

Justin Wang, Xiang-Lei Yang

{"title":"Novel functions of cytoplasmic aminoacyl-tRNA synthetases shaping the hallmarks of cancer.","authors":"Justin Wang, Xiang-Lei Yang","doi":"10.1016/bs.enz.2020.06.005","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.06.005","url":null,"abstract":"With the intense protein synthesis demands of cancer, the classical enzymatic role of aminoacyl-tRNA synthetases (aaRSs) is required to sustain tumor growth. However, many if not all aaRSs also possess regulatory functions outside of the domain of catalytic tRNA aminoacylation, which can further contribute to or even antagonize cancers in non-translational ways. These regulatory functions of aaRS are likely to be manipulated in cancer to ensure uncontrolled growth and survival. This review will largely focus on the unique capacities of individual and sometimes collaborating synthetases to influence the hallmarks of cancer, which represent the principles and characteristics of tumorigenesis. An interesting feature of cytoplasmic aaRSs in higher eukaryotes is the formation of a large multi-synthetase complex (MSC) with nine aaRSs held together by three non-enzymatic scaffolding proteins (AIMPs). The MSC-associated aaRSs, when released from the complex in response to certain stimulations, often participate in pathways that promote tumorigenesis. In contrast, the freestanding aaRSs are associated with activities in both directions-some promoting while others inhibiting cancer. The AIMPs have emerged as potent tumor suppressors through their own distinct mechanisms. We propose that the tumor-suppressive roles of AIMPs may also be a consequence of keeping the cancer-promoting aaRSs within the MSC. The rich connections between cancer and the synthetases have inspired the development of innovative cancer treatments that target or take advantage of these novel functions of aaRSs.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"48 ","pages":"397-423"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.06.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25593406","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Trans-editing by aminoacyl-tRNA synthetase-like editing domains. 氨基酰基- trna类合成酶编辑结构域的反式编辑。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-09-08 DOI: 10.1016/bs.enz.2020.07.002

Alexandra B Kuzmishin Nagy, Marina Bakhtina, Karin Musier-Forsyth

{"title":"Trans-editing by aminoacyl-tRNA synthetase-like editing domains.","authors":"Alexandra B Kuzmishin Nagy, Marina Bakhtina, Karin Musier-Forsyth","doi":"10.1016/bs.enz.2020.07.002","DOIUrl":"https://doi.org/10.1016/bs.enz.2020.07.002","url":null,"abstract":"Aminoacyl-tRNA synthetases (aaRS) are ubiquitous enzymes responsible for aminoacyl-tRNA (aa-tRNA) synthesis. Correctly formed aa-tRNAs are necessary for proper decoding of mRNA and accurate protein synthesis. tRNAs possess specific nucleobases that promote selective recognition by cognate aaRSs. Selecting the cognate amino acid can be more challenging because all amino acids share the same peptide backbone and several are isosteric or have similar side chains. Thus, aaRSs can misactivate non-cognate amino acids and produce mischarged aa-tRNAs. If left uncorrected, mischarged aa-tRNAs deliver their non-cognate amino acid to the ribosome resulting in misincorporation into the nascent polypeptide chain. This changes the primary protein sequence and potentially causes misfolding or formation of non-functional proteins that impair cell survival. A variety of proofreading or editing pathways exist to prevent and correct mistakes in aa-tRNA formation. Editing may occur before the amino acid transfer step of aminoacylation via hydrolysis of the aminoacyl-adenylate. Alternatively, post-transfer editing, which occurs after the mischarged aa-tRNA is formed, may be carried out via a distinct editing site on the aaRS where the mischarged aa-tRNA is deacylated. In recent years, it has become clear that most organisms also encode factors that lack aminoacylation activity but resemble aaRS editing domains and function to clear mischarged aa-tRNAs in trans. This review focuses on these trans-editing factors, which are encoded in all three domains of life and function together with editing domains present within aaRSs to ensure that the accuracy of protein synthesis is sufficient for cell survival.","PeriodicalId":39097,"journal":{"name":"Enzymes","volume":"48 ","pages":"69-115"},"PeriodicalIF":0.0,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/bs.enz.2020.07.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25593408","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 10

Thermal, electrochemical and photochemical reactions involving catalytically versatile ene reductase enzymes. 涉及多用途催化烯还原酶的热、电化学和光化学反应。

Enzymes Pub Date : 2020-01-01 Epub Date: 2020-07-18 DOI: 10.1016/bs.enz.2020.05.012

Helen S Toogood, Nigel S Scrutton

引用次数: 2