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Pesquisa : D08.811.520.232 [Categoria DeCS]
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  1 / 213 MEDLINE  
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[PMID]:28613863
[Au] Autor:Schlachter CR; Klapper V; Wybouw N; Radford T; Van Leeuwen T; Grbic M; Chruszcz M
[Ad] Endereço:Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
[Ti] Título:Structural Characterization of a Eukaryotic Cyanase from Tetranychus urticae.
[So] Source:J Agric Food Chem;65(27):5453-5462, 2017 Jul 12.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The two-spotted spider mite Tetranychus urticae is a polyphagous agricultural pest and poses a high risk to global crop production as it is rapidly developing pesticide resistance. Genomic and transcriptomic analysis has revealed the presence of a remarkable cyanase gene in T. urticae and related mite species within the Acariformes lineage. Cyanase catalyzes the detoxification of cyanate and is potentially an attractive protein target for the development of new acaricides. Phylogenetic analysis indicates that within the Acariformes, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation. Our structural studies presented here compare and contrast prokaryotic cyanases to T. urticae cyanase, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/química
Carbono-Nitrogênio Liases/química
Tetranychidae/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas de Artrópodes/genética
Proteínas de Artrópodes/metabolismo
Carbono-Nitrogênio Liases/genética
Carbono-Nitrogênio Liases/metabolismo
Dados de Sequência Molecular
Filogenia
Conformação Proteica
Alinhamento de Sequência
Tetranychidae/química
Tetranychidae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); EC 4.2.1.104 (cyanate hydrolase); EC 4.3.- (Carbon-Nitrogen Lyases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170720
[Lr] Data última revisão:
170720
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170615
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01333


  2 / 213 MEDLINE  
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[PMID]:28483520
[Au] Autor:Xie X; Wang X; Jiang D; Wang J; Fei R; Cong X; Wei L; Wang Y; Chen H
[Ad] Endereço:Peking University People's Hospital, Peking University Hepatology Institute, Beijing Key Laboratory of Hepatitis C and Immunotherapy for Liver Disease, Beijing 100044, China; Chinese Center for Disease Control and Prevention, Beijing 102206, China.
[Ti] Título:PPPDE1 is a novel deubiquitinase belonging to a cysteine isopeptidase family.
[So] Source:Biochem Biophys Res Commun;488(2):291-296, 2017 Jun 24.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ubiquitinlation of proteins is prevalent and important in both normal and pathological cellular processes. Deubiquitinating enzymes (DUBs) can remove the ubiquitin tags on substrate proteins and dynamically regulate the ubiquitination process. The PPPDE family proteins were predicted to be a novel class of deubiquitinating peptidase, but this has not yet been experimentally proved. Here we validated the deubiquitinating activity of PPPDE1 and revealed its isopeptidase activity against ubiquitin conjugated through Lys 48 and Lys 63. We also identified ribosomal protein S7, RPS7, as a substrate protein of PPPDE1. Moreover, PPPDE1 could mediate the ubiquitin chain editing of RPS7, deubiquitinating Lys 48-linked ubiquitination, and finally stabilize RPS7 proteins. Taken together, we report that PPPDE1 is a novel deubiquitinase that belongs to a cysteine isopeptidase family.
[Mh] Termos MeSH primário: Carbono-Nitrogênio Liases/classificação
Carbono-Nitrogênio Liases/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (DESI2 protein, human); EC 4.3.- (isopeptidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE


  3 / 213 MEDLINE  
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[PMID]:28343358
[Au] Autor:Kebeish R; Al-Zoubi O
[Ad] Endereço:Biology Department, Faculty of Science Yanbu, Taibah University, KSA, King Khalid Rd, Al amoedi, Yanbu El-Bahr, 46423, Saudi Arabia. rkebeish@gmail.com.
[Ti] Título:Expression of the cyanobacterial enzyme cyanase increases cyanate metabolism and cyanate tolerance in Arabidopsis.
[So] Source:Environ Sci Pollut Res Int;24(12):11825-11835, 2017 Apr.
[Is] ISSN:1614-7499
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Cyanate and its derivatives are considered as environmental hazardous materials. Cyanate is released to the environment through many chemical industries and mining wastewater. Cyanase enzyme converts cyanate into CO and NH in a bicarbonate-dependent reaction. At low cyanate concentrations, the endogenous plant cyanases play a vital role in cyanate detoxification. However, such cyanate biodegradation system is probably insufficient due to the excess cyanate concentrations at contaminated sites. In this study, we have transferred the activity of the cyanobacterial cyanase into Arabidopsis thaliana plants in order to enhance plant resistance against cyanate toxicity. The enzyme was shown to be active in planta. Transgenic plants exposed to cyanate, either applied by foliar spray or supplemented in growth medium, showed less reduction in pigment contents, antioxidant enzymes, carbohydrate contents, and reduced levels of plant growth retardation. Plant growth assays under cyanate stress showed enhanced growth and biomass accumulation in cyanase overexpressors compared to control plants. Results of this study provide evidence for developing novel eco-friendly phytoremediation systems for cyanate detoxification.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Carbono-Nitrogênio Liases/metabolismo
Cianatos/metabolismo
Cianobactérias/enzimologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Carbono-Nitrogênio Liases/genética
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyanates); EC 4.2.1.104 (cyanate hydrolase); EC 4.3.- (Carbon-Nitrogen Lyases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170327
[St] Status:MEDLINE
[do] DOI:10.1007/s11356-017-8866-z


  4 / 213 MEDLINE  
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[PMID]:27626674
[Au] Autor:Kunz K; Wagner K; Mendler L; Hölper S; Dehne N; Müller S
[Ad] Endereço:Institute of Biochemistry II, Goethe University, Medical School, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany.
[Ti] Título:SUMO Signaling by Hypoxic Inactivation of SUMO-Specific Isopeptidases.
[So] Source:Cell Rep;16(11):3075-3086, 2016 Sep 13.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Post-translational modification of proteins with ubiquitin-like SUMO modifiers is a tightly regulated and highly dynamic process. The SENP family of SUMO-specific isopeptidases comprises six cysteine proteases. They are instrumental in counterbalancing SUMO conjugation, but their regulation is not well understood. We demonstrate that in hypoxic cell extracts, the catalytic activity of SENP family members, in particular SENP1 and SENP3, is inhibited in a rapid and fully reversible process. Comparative mass spectrometry from normoxic and hypoxic cells defines a subset of hypoxia-induced SUMO1 targets, including SUMO ligases RanBP2 and PIAS2, glucose transporter 1, and transcriptional regulators. Among the most strongly induced targets, we identified the transcriptional co-repressor BHLHE40, which controls hypoxic gene expression programs. We provide evidence that SUMOylation of BHLHE40 is reversed by SENP1 and contributes to transcriptional repression of the metabolic master regulator gene PGC-1α. We propose a pathway that connects oxygen-controlled SENP activity to hypoxic reprogramming of metabolism.
[Mh] Termos MeSH primário: Carbono-Nitrogênio Liases/metabolismo
Transdução de Sinais
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Hipóxia Celular
Proteínas Correpressoras/metabolismo
Cisteína Endopeptidases/metabolismo
Ativação Enzimática
Células HeLa
Seres Humanos
Especificidade por Substrato
Sumoilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (Small Ubiquitin-Related Modifier Proteins); EC 3.4.- (SENP1 protein, human); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (SENP3 protein, human); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (isopeptidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE


  5 / 213 MEDLINE  
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[PMID]:27131890
[Au] Autor:Thangaraju K; Biri B; Schlosser G; Kiss B; Nyitray L; Fésüs L; Király R
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Debrecen, 4012 Debrecen, Hungary.
[Ti] Título:Real-time kinetic method to monitor isopeptidase activity of transglutaminase 2 on protein substrate.
[So] Source:Anal Biochem;505:36-42, 2016 Jul 15.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transglutaminase 2 (TG2) is a ubiquitously expressed multifunctional protein with Ca(2+)-dependent transamidase activity forming protease-resistant N(ε)-(γ-glutamyl) lysine crosslinks between proteins. It can also function as an isopeptidase cleaving the previously formed crosslinks. The biological significance of this activity has not been revealed yet, mainly because of the lack of a protein-based method for its characterization. Here we report the development of a novel kinetic method for measuring isopeptidase activity of human TG2 by monitoring decrease in the fluorescence polarization of a protein substrate previously formed by crosslinking fluorescently labeled glutamine donor FLpepT26 to S100A4 at a specific lysine residue. The developed method could be applied to test mutant enzymes and compounds that influence isopeptidase activity of TG2.
[Mh] Termos MeSH primário: Carbono-Nitrogênio Liases/metabolismo
Proteínas de Ligação ao GTP/metabolismo
Transglutaminases/metabolismo
[Mh] Termos MeSH secundário: Carbono-Nitrogênio Liases/química
Reagentes para Ligações Cruzadas/química
Polarização de Fluorescência
Corantes Fluorescentes/química
Proteínas de Ligação ao GTP/química
Seres Humanos
Cinética
Fatores de Tempo
Transglutaminases/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Fluorescent Dyes); EC 2.3.2.- (transglutaminase 2); EC 2.3.2.13 (Transglutaminases); EC 3.6.1.- (GTP-Binding Proteins); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (isopeptidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160502
[St] Status:MEDLINE


  6 / 213 MEDLINE  
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[PMID]:26778648
[Au] Autor:Beckert A; Wiesner J; Schmidtberg H; Lehmann R; Baumann A; Vogel H; Vilcinskas A
[Ad] Endereço:Department of Bioresources, Fraunhofer Institute for Molecular Biology and Applied Ecology, Gießen, Germany.
[Ti] Título:Expression and characterization of a recombinant i-type lysozyme from the harlequin ladybird beetle Harmonia axyridis.
[So] Source:Insect Mol Biol;25(3):202-15, 2016 06.
[Is] ISSN:1365-2583
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lysozymes are enzymes that destroy bacterial cell walls by hydrolysing the polysaccharide component of peptidoglycan. In insects, there are two classes of lysozymes, the c-type with muramidase activity and the i-type whose prototypical members from annelids and molluscs possess both muramidase and isopeptidase activities. Many insect genes encoding c-type and i-type lysozymes have been identified during genome and transcriptome analyses, but only c-type lysozymes have been functionally characterized at the protein level. Here we produced one of five i-type lysozymes represented in the immunity-related transcriptome of the invasive harlequin ladybird beetle Harmonia axyridis as recombinant protein. This was the only one containing the serine and histidine residues that are thought to be required for isopeptidase activity. This i-type lysozyme was recombinantly expressed in the yeast Pichia pastoris, but the purified protein was inactive in both muramidase and isopeptidase assays. Transcription and immunofluorescence analysis revealed that this i-type lysozyme is produced in the fat body but is not inducible by immune challenge. These data suggest that i-type lysozymes in insects may have acquired novel and as yet undetermined functions in the course of evolution.
[Mh] Termos MeSH primário: Coleópteros/enzimologia
Muramidase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Carbono-Nitrogênio Liases/análise
Coleópteros/genética
Coleópteros/imunologia
Imunidade Inata
Dados de Sequência Molecular
Muramidase/genética
Pichia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.17 (Muramidase); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (isopeptidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160119
[St] Status:MEDLINE
[do] DOI:10.1111/imb.12213


  7 / 213 MEDLINE  
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[PMID]:26719050
[Au] Autor:Ingallina C; D'Acquarica I; Delle Monache G; Ghirga F; Quaglio D; Ghirga P; Berardozzi S; Markovic V; Botta B
[Ti] Título:The Pictet-Spengler Reaction Still on Stage.
[So] Source:Curr Pharm Des;22(12):1808-50, 2016.
[Is] ISSN:1873-4286
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Today, in spite of being older than a century (born in 1911), the Pictet-Spengler two component reaction (PS-2CR) is still one of the most popular reactions, not only for the synthesis of tetrahydroisoquinolines (THIQs), tetrahydro-ß-carbolines (THBCs), or more complex structures containing these two privileged moieties, but also for the construction of novel scaffolds, available for structure-activity relationship (SAR) studies and/or for combinatorial libraries targeted at drug discovery. The prominence of the P-S cyclization is brought about by the inheritance from analogous enzyme-catalyzed reactions of the biogenetic pathways of natural products, mainly indole alkaloids, with a broad range of biological activities. This knowledge has been the starting point for the biomimetic synthesis or the bio-engineering production of pharmacologically important drugs. The long-lasting life of the P-S reaction depends on the discovery of its multiple facets, the modifications of its parameters and components, as well as the continuous renovation of solutions for the challenging stereochemical outcome of the transformation. This paper deals with an updated visit to the P-S reaction aiming to find the threads of the story without forgetting the numerous facets of the prism. It is organized as a theater piece, with a prologue and the main scene (namely, Act 1) where the readers can follow the parade of the two above-mentioned very recurring motifs (namely, THIQ and THBC) by moving from one step to another (a cyclization, an intramolecular attack, a stereoselective passage) to find the way out of the labyrinth of the P-S reaction.
[Mh] Termos MeSH primário: Carbono-Nitrogênio Liases/metabolismo
Alcaloides de Indol/metabolismo
[Mh] Termos MeSH secundário: Bioengenharia
Ciclização
Seres Humanos
Alcaloides de Indol/química
Estrutura Molecular
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Indole Alkaloids); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.3.2 (strictosidine synthetase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160101
[St] Status:MEDLINE


  8 / 213 MEDLINE  
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[PMID]:26318142
[Au] Autor:Takayama S; Hashimoto K; Kokubu E; Taniguchi M; Tajima K; Ochiai A; Saitoh E; Saito A; Ishihara K; Kato T
[Ad] Endereço:Department of Periodontology, Tokyo Dental College, Tokyo 101-0061, Japan.
[Ti] Título:Inhibitory effects of a novel cationic dodecapeptide [CL(14-25)] derived from cyanate lyase of rice on endotoxic activities of LPSs from Escherichia coli and periodontopathic Aggregatibacter actinomycetemcomitans.
[So] Source:Microb Pathog;94:2-11, 2016 May.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: CL(14-25), a dodecapeptide of cyanate lyase from rice, is a novel cationic α-helical antimicrobial peptide. In this study, we examined inhibitory ability of CL(14-25) against endotoxic activities of lipopolysaccharides (LPSs) from Escherichia coli and periodontal pathogenic Aggregatibacter actinomycetemcomitans. METHODS: Endotoxin-neutralizing activity of CL(14-25) was evaluated by inhibition to induction of cytokine and nitric oxide in human aortic endothelial cells (HAECs) and RAW264 mouse macrophage cells, respectively. Protective effect of CL(14-25) was determined in mice against lethal toxicity of LPS. RESULTS: IL-6 in HAECs was induced by stimulation with LPS preparations of A. actinomycetemcomitans and E. coli tested in this study, and addition of CL(14-25) to the medium caused inhibition of their induction in a dose-dependent manner. CL(14-25) inhibited NO induction in RAW264 cells by a smooth type LPS of E. coli O55:B5 and an Rc type LPS of E. coli J5 as well as lipid A of E. coli R515 in a dose-dependent manner. Simultaneous injection of E. coli O55:B5 LPS and CL(14-25) in BALB/c mice resulted in prevention of lethal toxicity of the former. The results of a Limulus amebocyte lysate assay and surface plasmon resonance analysis of interaction between CL(14-25) and E. coli LPS or lipid A showed that CL(14-25) specifically binds to a lipid A moiety of LPS. CONCLUSION: The results of present study suggest that CL(14-25) has a potential to be used as a nutraceutical agent for periodontal therapy.
[Mh] Termos MeSH primário: Aggregatibacter actinomycetemcomitans/metabolismo
Carbono-Nitrogênio Liases/química
Escherichia coli/metabolismo
Lipopolissacarídeos/antagonistas & inibidores
Fragmentos de Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Aggregatibacter actinomycetemcomitans/química
Animais
Citocinas/biossíntese
Citocinas/metabolismo
Relação Dose-Resposta a Droga
Interações Medicamentosas
Células Endoteliais/efeitos dos fármacos
Escherichia coli/química
Seres Humanos
Interleucina-6/biossíntese
Lipídeo A/antagonistas & inibidores
Lipídeo A/química
Lipídeo A/toxicidade
Lipopolissacarídeos/química
Lipopolissacarídeos/toxicidade
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Óxido Nítrico/biossíntese
Óxido Nítrico/metabolismo
Oryza/enzimologia
Fragmentos de Peptídeos/química
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CL(14-25)); 0 (Cytokines); 0 (Interleukin-6); 0 (Lipid A); 0 (Lipopolysaccharides); 0 (Peptide Fragments); 31C4KY9ESH (Nitric Oxide); EC 4.2.1.104 (cyanate hydrolase); EC 4.3.- (Carbon-Nitrogen Lyases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150831
[St] Status:MEDLINE


  9 / 213 MEDLINE  
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[PMID]:26250429
[Au] Autor:Király R; Thangaraju K; Nagy Z; Collighan R; Nemes Z; Griffin M; Fésüs L
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Debrecen, Egyetem tér 1., Debrecen, 4012, Hungary.
[Ti] Título:Isopeptidase activity of human transglutaminase 2: disconnection from transamidation and characterization by kinetic parameters.
[So] Source:Amino Acids;48(1):31-40, 2016 Jan.
[Is] ISSN:1438-2199
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Transglutaminase 2 (TG2) is a multifunctional protein with diverse catalytic activities and biological roles. Its best studied function is the Ca(2+)-dependent transamidase activity leading to formation of γ-glutamyl-ε-lysine isopeptide crosslinks between proteins and γ-glutamyl-amine derivatives. TG2 has a poorly studied isopeptidase activity cleaving these bonds. We have developed and characterised TG2 mutants which are significantly deficient in transamidase activity while have normal or increased isopeptidase activity (W332F) and vice versa (W278F). The W332F mutation led to significant changes of both the K m and the V max kinetic parameters of the isopeptidase reaction of TG2 while its calcium and GTP sensitivity was similar to the wild-type enzyme. The W278F mutation resulted in six times elevated amine incorporating transamidase activity demonstrating the regulatory significance of W278 and W332 in TG2 and that mutations can change opposed activities located at the same active site. The further application of our results in cellular systems may help to understand TG2-driven physiological and pathological processes better and lead to novel therapeutic approaches where an increased amount of crosslinked proteins correlates with the manifestation of degenerative disorders.
[Mh] Termos MeSH primário: Aminas/metabolismo
Carbono-Nitrogênio Liases/química
Carbono-Nitrogênio Liases/metabolismo
Proteínas de Ligação ao GTP/química
Proteínas de Ligação ao GTP/metabolismo
Transglutaminases/química
Transglutaminases/metabolismo
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Carbono-Nitrogênio Liases/genética
Domínio Catalítico
Proteínas de Ligação ao GTP/genética
Seres Humanos
Cinética
Mutação de Sentido Incorreto
Transglutaminases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amines); EC 2.3.2.- (transglutaminase 2); EC 2.3.2.13 (Transglutaminases); EC 3.6.1.- (GTP-Binding Proteins); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (isopeptidase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150808
[St] Status:MEDLINE
[do] DOI:10.1007/s00726-015-2063-5


  10 / 213 MEDLINE  
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[PMID]:26534965
[Au] Autor:Maksimov MO; Koos JD; Zong C; Lisko B; Link AJ
[Ad] Endereço:From the Departments of Chemical and Biological Engineering.
[Ti] Título:Elucidating the Specificity Determinants of the AtxE2 Lasso Peptide Isopeptidase.
[So] Source:J Biol Chem;290(52):30806-12, 2015 Dec 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lasso peptide isopeptidase is an enzyme that specifically hydrolyzes the isopeptide bond of lasso peptides, rendering these peptides linear. To carry out a detailed structure-activity analysis of the lasso peptide isopeptidase AtxE2 from Asticcacaulis excentricus, we solved NMR structures of its substrates astexin-2 and astexin-3. Using in vitro enzyme assays, we show that the C-terminal tail portion of these peptides is dispensable with regards to isopeptidase activity. A collection of astexin-2 and astexin-3 variants with alanine substitutions at each position within the ring and the loop was constructed, and we showed that all of these peptides except for one were cleaved by the isopeptidase. Thus, much like the lasso peptide biosynthetic enzymes, lasso peptide isopeptidase has broad substrate specificity. Quantitative analysis of the cleavage reactions indicated that alanine substitutions in loop positions of these peptides led to reduced cleavage, suggesting that the loop is serving as a recognition element for the isopeptidase.
[Mh] Termos MeSH primário: Alphaproteobacteria/enzimologia
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Carbono-Nitrogênio Liases/química
Carbono-Nitrogênio Liases/metabolismo
[Mh] Termos MeSH secundário: Alphaproteobacteria/química
Alphaproteobacteria/genética
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Biocatálise
Carbono-Nitrogênio Liases/genética
Cristalografia por Raios X
Modelos Moleculares
Peptídeos/química
Peptídeos/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Peptides); EC 4.3.- (Carbon-Nitrogen Lyases); EC 4.3.- (isopeptidase)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161225
[Lr] Data última revisão:
161225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151105
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.694083



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