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[PMID]:28739446
[Au] Autor:Panneerselvam S; Shehzad A; Mueller-Dieckmann J; Wilmanns M; Bocola M; Davari MD; Schwaneberg U
[Ad] Endereço:HASYLAB, DESY, Notkestrasse 85, 22603 Hamburg, Germany.
[Ti] Título:Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
[So] Source:Biochim Biophys Acta;1866(1):134-140, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source. The crystal structure shows a binding site for the mediator cobalt (III) sepulchrate at the entrance of the substrate access channel. The mediator occupies an unusual position which is far from the active site and distinct from the binding of the natural redox partner (FAD/NADPH binding domain).
[Mh] Termos MeSH primário: Bacillus megaterium/química
Proteínas de Bactérias/química
Cobalto/química
Coenzimas/química
Sistema Enzimático do Citocromo P-450/química
Elétrons
Heme/química
NADPH-Ferri-Hemoproteína Redutase/química
NADP/química
[Mh] Termos MeSH secundário: Bacillus megaterium/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Domínio Catalítico
Clonagem Molecular
Cobalto/metabolismo
Coenzimas/metabolismo
Cristalografia por Raios X
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Heme/metabolismo
Modelos Moleculares
NADP/metabolismo
NADPH-Ferri-Hemoproteína Redutase/genética
NADPH-Ferri-Hemoproteína Redutase/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Zinco/química
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Recombinant Proteins); 3G0H8C9362 (Cobalt); 42VZT0U6YR (Heme); 53-59-8 (NADP); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.6.2.4 (NADPH-Ferrihemoprotein Reductase); EC 1.6.2.4 (flavocytochrome P450 BM3 monoxygenases); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


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[PMID]:28467834
[Au] Autor:Yin R; Mo J; Dai J; Wang H
[Ad] Endereço:State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences , Beijing 100085, China.
[Ti] Título:Nickel(II) Inhibits Tet-Mediated 5-Methylcytosine Oxidation by High Affinity Displacement of the Cofactor Iron(II).
[So] Source:ACS Chem Biol;12(6):1494-1498, 2017 06 16.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ten-eleven translocation (Tet) family proteins are Fe(II)- and 2-oxoglutarate-dependent dioxygenases that regulate the dynamics of DNA methylation by catalyzing the oxidation of DNA 5-methylcytosine (5mC). To exert physiologically important functions, redox-active iron chelated in the catalytic center of Tet proteins directly involves the oxidation of the multiple substrates. To understand the function and interaction network of Tet dioxygenases, it is interesting to obtain high affinity and a specific inhibitor. Surprisingly, here we found that natural Ni(II) ion can bind to the Fe(II)-chelating motif (HXD) with an affinity of 7.5-fold as high as Fe(II). Consistently, we further found that Ni(II) ion can displace the cofactor Fe(II) of Tet dioxygenases and inhibit Tet-mediated 5mC oxidation activity with an estimated IC of 1.2 µM. Essentially, Ni(II) can be used as a high affinity and selective inhibitor to explore the function and dynamics of Tet proteins.
[Mh] Termos MeSH primário: 5-Metilcitosina/metabolismo
Dioxigenases/antagonistas & inibidores
Ferro/metabolismo
Níquel/farmacologia
[Mh] Termos MeSH secundário: Coenzimas
Compostos Ferrosos
Seres Humanos
Concentração Inibidora 50
Oxirredução/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coenzymes); 0 (Ferrous Compounds); 6R795CQT4H (5-Methylcytosine); 7OV03QG267 (Nickel); E1UOL152H7 (Iron); EC 1.13.11.- (Dioxygenases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00261


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[PMID]:29227595
[Au] Autor:Vynogradova RP; Lugovska GG; Yurasova SP
[Ti] Título:[Analysis of inventive activity of the department of vitamin and coenzyme biochemistry of Palladin Institute of Biochemistry NAS of Ukraine in the period of 1980-2015].
[So] Source:Ukr Biochem J;88(1):126-40, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:rus; ukr
[Mh] Termos MeSH primário: Academias e Institutos/história
Bioquímica/história
Invenções/história
[Mh] Termos MeSH secundário: Coenzimas/metabolismo
Coenzimas/farmacologia
História do Século XX
História do Século XXI
Ucrânia
Vitaminas/metabolismo
Vitaminas/farmacologia
[Pt] Tipo de publicação:HISTORICAL ARTICLE; JOURNAL ARTICLE; PORTRAITS
[Nm] Nome de substância:
0 (Coenzymes); 0 (Vitamins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.126


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[PMID]:29176894
[Au] Autor:Levillain F; Poquet Y; Mallet L; Mazères S; Marceau M; Brosch R; Bange FC; Supply P; Magalon A; Neyrolles O
[Ad] Endereço:Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.
[Ti] Título:Horizontal acquisition of a hypoxia-responsive molybdenum cofactor biosynthesis pathway contributed to Mycobacterium tuberculosis pathoadaptation.
[So] Source:PLoS Pathog;13(11):e1006752, 2017 Nov.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The unique ability of the tuberculosis (TB) bacillus, Mycobacterium tuberculosis, to persist for long periods of time in lung hypoxic lesions chiefly contributes to the global burden of latent TB. We and others previously reported that the M. tuberculosis ancestor underwent massive episodes of horizontal gene transfer (HGT), mostly from environmental species. Here, we sought to explore whether such ancient HGT played a part in M. tuberculosis evolution towards pathogenicity. We were interested by a HGT-acquired M. tuberculosis-specific gene set, namely moaA1-D1, which is involved in the biosynthesis of the molybdenum cofactor. Horizontal acquisition of this gene set was striking because homologues of these moa genes are present all across the Mycobacterium genus, including in M. tuberculosis. Here, we discovered that, unlike their paralogues, the moaA1-D1 genes are strongly induced under hypoxia. In vitro, a M. tuberculosis moaA1-D1-null mutant has an impaired ability to respire nitrate, to enter dormancy and to survive in oxygen-limiting conditions. Conversely, heterologous expression of moaA1-D1 in the phylogenetically closest non-TB mycobacterium, Mycobacterium kansasii, which lacks these genes, improves its capacity to respire nitrate and grants it with a marked ability to survive oxygen depletion. In vivo, the M. tuberculosis moaA1-D1-null mutant shows impaired survival in hypoxic granulomas in C3HeB/FeJ mice, but not in normoxic lesions in C57BL/6 animals. Collectively, our results identify a novel pathway required for M. tuberculosis resistance to host-imposed stress, namely hypoxia, and provide evidence that ancient HGT bolstered M. tuberculosis evolution from an environmental species towards a pervasive human-adapted pathogen.
[Mh] Termos MeSH primário: Coenzimas/biossíntese
Transferência Genética Horizontal
Metaloproteínas/biossíntese
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/metabolismo
Oxigênio/metabolismo
Tuberculose/microbiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Feminino
Regulação Bacteriana da Expressão Gênica
Seres Humanos
Hipóxia/metabolismo
Hipóxia/microbiologia
Camundongos
Camundongos Endogâmicos C57BL
Mycobacterium/genética
Mycobacterium/metabolismo
Nitratos/metabolismo
Pteridinas
Tuberculose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Metalloproteins); 0 (Nitrates); 0 (Pteridines); 73508-07-3 (molybdenum cofactor); S88TT14065 (Oxygen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006752


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[PMID]:29177972
[Au] Autor:Hanukoglu I
[Ad] Endereço:Laboratory of Cell Biology, Ariel University, 40700, Ariel, Israel. mbiochem@gmail.com.
[Ti] Título:Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme.
[So] Source:J Mol Evol;85(5-6):205-218, 2017 Dec.
[Is] ISSN:1432-1432
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:FAD and NAD(P) together represent an ideal pair for coupled redox reactions in their capacity to accept two electrons and their redox potentials. Enzymes that bind both NAD(P) and FAD represent large superfamilies that fulfill essential roles in numerous metabolic pathways. Adrenodoxin reductase (AdxR) shares Rossmann fold features with some of these superfamilies but remains in a group of its own in the absence of sequence homology. This article documents the phylogenetic distribution of AdxR by examining whole genome databases for Metazoa, Plantae, Fungi, and Protista, and determines the conserved structural features of AdxR. Scanning these databases showed that most organisms have a single gene coding for an AdxR ortholog. The sequence identity between AdxR orthologs is correlated with the phylogenetic distance among metazoan species. The NADP binding site of all AdxR orthologs showed a modified Rossmann fold motif with a GxGxxA consensus instead of the classical GxGxxG at the edge of the first ßα-fold. To examine the hypothesis that enzyme-coenzyme interfaces represent the conserved regions of AdxR, the residues interfacing FAD and NADP were identified and compared with multiple-sequence alignment results. Most conserved residues were indeed found at sites that surround the interfacing residues between the enzyme and the two coenzymes. In contrast to protein-protein interaction hot-spots that may appear in isolated patches, in AdxR the conserved regions show strict preservation of the overall structure. This structure maintains the precise positioning of the two coenzymes for optimal electron transfer between NADP and FAD without electron leakage to other acceptors.
[Mh] Termos MeSH primário: Ferredoxina-NADP Redutase/química
Ferredoxina-NADP Redutase/genética
Ferredoxina-NADP Redutase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Coenzimas/metabolismo
Sequência Conservada/genética
Transporte de Elétrons
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/genética
Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas Mitocondriais/metabolismo
Modelos Moleculares
NADP/química
NADP/genética
NADP/metabolismo
Filogenia
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Mitochondrial Proteins); 146-14-5 (Flavin-Adenine Dinucleotide); 53-59-8 (NADP); EC 1.18.1.2 (Ferredoxin-NADP Reductase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1007/s00239-017-9821-9


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[PMID]:28949132
[Au] Autor:Goetzl S; Teutloff C; Werther T; Hennig SE; Jeoung JH; Bittl R; Dobbek H
[Ad] Endereço:Institut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin , Berlin, Germany.
[Ti] Título:Protein Dynamics in the Reductive Activation of a B12-Containing Enzyme.
[So] Source:Biochemistry;56(41):5496-5502, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:B12-dependent proteins are involved in methyl transfer reactions ranging from the biosynthesis of methionine in humans to the formation of acetyl-CoA in anaerobic bacteria. During their catalytic cycle, they undergo large conformational changes to interact with various proteins. Recently, the crystal structure of the B12-containing corrinoid iron-sulfur protein (CoFeSP) in complex with its reductive activator (RACo) was determined, providing a first glimpse of how energy is transduced in the ATP-dependent reductive activation of corrinoid-containing methyltransferases. The thermodynamically uphill electron transfer from RACo to CoFeSP is accompanied by large movements of the cofactor-binding domains of CoFeSP. To refine the structure-based mechanism, we analyzed the conformational change of the B12-binding domain of CoFeSP by pulsed electron-electron double resonance and Förster resonance energy transfer spectroscopy. We show that the site-specific labels on the flexible B12-binding domain and the small subunit of CoFeSP move within 11 Å in the RACo:CoFeSP complex, consistent with the recent crystal structures. By analyzing the transient kinetics of formation and dissociation of the RACo:CoFeSP complex, we determined values of 0.75 µM s and 0.33 s for rate constants k and k , respectively. Our results indicate that the large movement observed in crystals also occurs in solution and that neither the formation of the protein encounter complex nor the large movement of the B12-binding domain is rate-limiting for the ATP-dependent reductive activation of CoFeSP by RACo.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Coenzimas/metabolismo
Ativadores de Enzimas/metabolismo
Firmicutes/enzimologia
Proteínas com Ferro-Enxofre/metabolismo
Modelos Moleculares
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/química
Aldeído Oxirredutases/genética
Aldeído Oxirredutases/metabolismo
Substituição de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Coenzimas/química
Cristalografia por Raios X
Bases de Dados de Proteínas
Dimerização
Ativadores de Enzimas/química
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Cinética
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Oxirredução
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Vitamina B 12/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Enzyme Activators); 0 (Iron-Sulfur Proteins); 0 (Multienzyme Complexes); 0 (Protein Subunits); 0 (Recombinant Proteins); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.99.2 (carbon monoxide dehydrogenase); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00477


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[PMID]:28882541
[Au] Autor:Yuan M; Vásquez-Valdivieso MG; McNae IW; Michels PAM; Fothergill-Gilmore LA; Walkinshaw MD
[Ad] Endereço:Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Michael Swann Building, Max Born Crescent, Edinburgh EH9 3BF, UK.
[Ti] Título:Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition.
[So] Source:J Mol Biol;429(20):3075-3089, 2017 Oct 13.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The gluconeogenic enzyme fructose-1,6-bisphosphatase has been proposed as a potential drug target against Leishmania parasites that cause up to 20,000-30,000 deaths annually. A comparison of three crystal structures of Leishmania major fructose-1,6-bisphosphatase (LmFBPase) along with enzyme kinetic data show how AMP acts as an allosteric inhibitor and provides insight into its metal-dependent reaction mechanism. The crystal structure of the apoenzyme form of LmFBPase is a homotetramer in which the dimer of dimers adopts a planar conformation with disordered "dynamic loops". The structure of LmFBPase, complexed with manganese and its catalytic product phosphate, shows the dynamic loops locked into the active sites. A third crystal structure of LmFBPase complexed with its allosteric inhibitor AMP shows an inactive form of the tetramer, in which the dimer pairs are rotated by 18° relative to each other. The three structures suggest an allosteric mechanism in which AMP binding triggers a rearrangement of hydrogen bonds across the large and small interfaces. Retraction of the "effector loop" required for AMP binding releases the side chain of His23 from the dimer-dimer interface. This is coupled with a flip of the side chain of Arg48 which ties down the key catalytic dynamic loop in a disengaged conformation and also locks the tetramer in an inactive rotated T-state. The structure of the effector site of LmFBPase shows different structural features compared with human FBPases, thereby offering a potential and species-specific drug target.
[Mh] Termos MeSH primário: Monofosfato de Adenosina/metabolismo
Frutose-Bifosfatase/antagonistas & inibidores
Frutose-Bifosfatase/química
Leishmania major/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Coenzimas
Cristalografia por Raios X
Inibidores Enzimáticos
Seres Humanos
Cinética
Manganês/metabolismo
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Enzyme Inhibitors); 415SHH325A (Adenosine Monophosphate); 42Z2K6ZL8P (Manganese); EC 3.1.3.11 (Fructose-Bisphosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171022
[Lr] Data última revisão:
171022
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE


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[PMID]:28847921
[Au] Autor:Jiang T; Guo X; Yan J; Zhang Y; Wang Y; Zhang M; Sheng B; Ma C; Xu P; Gao C
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
[Ti] Título:A Bacterial Multidomain NAD-Independent d-Lactate Dehydrogenase Utilizes Flavin Adenine Dinucleotide and Fe-S Clusters as Cofactors and Quinone as an Electron Acceptor for d-Lactate Oxidization.
[So] Source:J Bacteriol;199(22), 2017 Nov 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial membrane-associated NAD-independent d-lactate dehydrogenase (Fe-S d-iLDH) oxidizes d-lactate into pyruvate. A sequence analysis of the enzyme reveals that it contains an Fe-S oxidoreductase domain in addition to a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain, which differs from other typical d-iLDHs. Fe-S d-iLDH from KT2440 was purified as a His-tagged protein and characterized in detail. This monomeric enzyme exhibited activities with l-lactate and several d-2-hydroxyacids. Quinone was shown to be the preferred electron acceptor of the enzyme. The two domains of the enzyme were then heterologously expressed and purified separately. The Fe-S cluster-binding motifs predicted by sequence alignment were preliminarily verified by site-directed mutagenesis of the Fe-S oxidoreductase domain. The FAD-containing dehydrogenase domain retained 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S d-iLDH. Compared to the intact enzyme, the FAD-containing dehydrogenase domain showed increased catalytic efficiency with cytochrome as the electron acceptor, but it completely lost the ability to use coenzyme Q Additionally, the FAD-containing dehydrogenase domain was no longer associated with the cell membrane, and it could not support the utilization of d-lactate as a carbon source. Based on the results obtained, we conclude that the Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by Fe-S d-iLDH, and it helps the enzyme associate with the cell membrane. These functions make the Fe-S oxidoreductase domain crucial for the d-lactate utilization function of Fe-S d-iLDH. Lactate metabolism plays versatile roles in most domains of life. Lactate utilization processes depend on certain enzymes to oxidize lactate to pyruvate. In recent years, novel bacterial lactate-oxidizing enzymes have been continually reported, including the unique NAD-independent d-lactate dehydrogenase that contains an Fe-S oxidoreductase domain besides the typical flavin-containing domain (Fe-S d-iLDH). Although Fe-S d-iLDH is widely distributed among bacterial species, the investigation of it is insufficient. Fe-S d-iLDH from KT2440, which is the major d-lactate-oxidizing enzyme for the strain, might be a representative of this type of enzyme. A study of it will be helpful in understanding the detailed mechanisms underlying the lactate utilization processes.
[Mh] Termos MeSH primário: Flavina-Adenina Dinucleotídeo/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Lactato Desidrogenases/genética
Lactato Desidrogenases/metabolismo
Ácido Láctico/metabolismo
Quinonas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Coenzimas
Citocromos c/metabolismo
Elétrons
Lactato Desidrogenases/isolamento & purificação
Mutagênese Sítio-Dirigida
NAD/metabolismo
Oxirredução
Pseudomonas putida/enzimologia
Ubiquinona/análogos & derivados
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Iron-Sulfur Proteins); 0 (Quinones); 0U46U6E8UK (NAD); 1339-63-5 (Ubiquinone); 146-14-5 (Flavin-Adenine Dinucleotide); 33X04XA5AT (Lactic Acid); 9007-43-6 (Cytochromes c); EC 1.1.- (Lactate Dehydrogenases); EC 1.1.1.28 (D-lactate dehydrogenase); EJ27X76M46 (coenzyme Q10)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE


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[PMID]:28832942
[Au] Autor:Marpani F; Sárossy Z; Pinelo M; Meyer AS
[Ad] Endereço:Department of Chemical and Biochemical Engineering, Center for BioProcess Engineering, Technical University of Denmark, Kgs. Lyngby, Denmark.
[Ti] Título:Kinetics based reaction optimization of enzyme catalyzed reduction of formaldehyde to methanol with synchronous cofactor regeneration.
[So] Source:Biotechnol Bioeng;114(12):2762-2770, 2017 Dec.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enzymatic reduction of carbon dioxide (CO ) to methanol (CH OH) can be accomplished using a designed set-up of three oxidoreductases utilizing reduced pyridine nucleotide (NADH) as cofactor for the reducing equivalents electron supply. For this enzyme system to function efficiently a balanced regeneration of the reducing equivalents during reaction is required. Herein, we report the optimization of the enzymatic conversion of formaldehyde (CHOH) to CH OH by alcohol dehydrogenase, the final step of the enzymatic redox reaction of CO to CH OH, with kinetically synchronous enzymatic cofactor regeneration using either glucose dehydrogenase (System I) or xylose dehydrogenase (System II). A mathematical model of the enzyme kinetics was employed to identify the best reaction set-up for attaining optimal cofactor recycling rate and enzyme utilization efficiency. Targeted process optimization experiments were conducted to verify the kinetically modeled results. Repetitive reaction cycles were shown to enhance the yield of CH OH, increase the total turnover number (TTN) and the biocatalytic productivity rate (BPR) value for both system I and II whilst minimizing the exposure of the enzymes to high concentrations of CHOH. System II was found to be superior to System I with a yield of 8 mM CH OH, a TTN of 160 and BPR of 24 µmol CH OH/U · h during 6 hr of reaction. The study demonstrates that an optimal reaction set-up could be designed from rational kinetics modeling to maximize the yield of CH OH, whilst simultaneously optimizing cofactor recycling and enzyme utilization efficiency.
[Mh] Termos MeSH primário: Álcool Desidrogenase/química
Oxirredutases do Álcool/química
Coenzimas/química
Formaldeído/química
Glucose 1-Desidrogenase/química
Metanol/síntese química
Modelos Químicos
[Mh] Termos MeSH secundário: Catálise
Simulação por Computador
Ativação Enzimática
Cinética
Metanol/isolamento & purificação
Oxirredução
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 1HG84L3525 (Formaldehyde); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.1.175 (D-xylose dehydrogenase); EC 1.1.1.47 (Glucose 1-Dehydrogenase); Y4S76JWI15 (Methanol)
[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:170824
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26405


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[PMID]:28819009
[Au] Autor:Stach L; Freemont PS
[Ad] Endereço:Section of Structural Biology, Department of Medicine, Imperial College London, London, U.K.
[Ti] Título:The AAA+ ATPase p97, a cellular multitool.
[So] Source:Biochem J;474(17):2953-2976, 2017 Aug 17.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The AAA+ (ATPases associated with diverse cellular activities) ATPase p97 is essential to a wide range of cellular functions, including endoplasmic reticulum-associated degradation, membrane fusion, NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) activation and chromatin-associated processes, which are regulated by ubiquitination. p97 acts downstream from ubiquitin signaling events and utilizes the energy from ATP hydrolysis to extract its substrate proteins from cellular structures or multiprotein complexes. A multitude of p97 cofactors have evolved which are essential to p97 function. Ubiquitin-interacting domains and p97-binding domains combine to form bi-functional cofactors, whose complexes with p97 enable the enzyme to interact with a wide range of ubiquitinated substrates. A set of mutations in p97 have been shown to cause the multisystem proteinopathy inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia. In addition, p97 inhibition has been identified as a promising approach to provoke proteotoxic stress in tumors. In this review, we will describe the cellular processes governed by p97, how the cofactors interact with both p97 and its ubiquitinated substrates, p97 enzymology and the current status in developing p97 inhibitors for cancer therapy.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/fisiologia
Modelos Biológicos
Proteínas Nucleares/fisiologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/antagonistas & inibidores
Adenosina Trifosfatases/química
Regulação Alostérica/efeitos dos fármacos
Animais
Antineoplásicos/química
Antineoplásicos/farmacologia
Sítios de Ligação
Montagem e Desmontagem da Cromatina/efeitos dos fármacos
Coenzimas/química
Coenzimas/metabolismo
Drogas em Investigação/química
Drogas em Investigação/farmacologia
Degradação Associada com o Retículo Endoplasmático/efeitos dos fármacos
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Seres Humanos
Fusão de Membrana/efeitos dos fármacos
Conformação Molecular
Subunidade p50 de NF-kappa B/agonistas
Subunidade p50 de NF-kappa B/metabolismo
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/química
Conformação Proteica
Ubiquitinação/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Coenzymes); 0 (Drugs, Investigational); 0 (Enzyme Inhibitors); 0 (NF-kappa B p50 Subunit); 0 (NFKB1 protein, human); 0 (Nuclear Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (p97 ATPase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160783



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