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[PMID]:26422920
[Au] Autor:Avdiyuk KV; Varbanets LD
[Ti] Título:[THE EFFECT OF METAL IONES AND SPECIFIC CHEMICAL REAGENTS ON THE ACTIVITY OF ASPERGILLUS FLAVUS VAR. ORYZAE AND BACILLUS SUBTILIS α-AMYLASES].
[So] Source:Mikrobiol Z;77(4):15-24, 2015 Jul-Aug.
[Is] ISSN:1028-0987
[Cp] País de publicação:Ukraine
[La] Idioma:ukr
[Ab] Resumo:The effect of cations and anions on the activity of Aspergillus flavus var. oryzae and Bacillus subtilis α-amylases showed that the tested enzymes are sensitive to most of cations and resistant to anions. The most significant inhibitory effects on the activity of A. flavus var. oryzae α-amylase have been demonstrated by Al3+ and Fe3+ ions, while on the activity of B. subtilis α-amylase - Hg2+, Cu2+ and Fe3+ ions. Inactivation of A. flavus var. oryzae and B. subtilis α-amylases in the presence of EGTA is indicated on the presence within their structure of metal ions. An important role in the enzymatic catalysis of both enzymes play carboxyl groups as evidenced by their inhibition of 1-[3-(dimethylamino)propyl]-3-ethylcarbodiimide methiodide. Inhibition of B. subtilis α-amylase by p-chloromercuribenzoate, N-ethylmaleimide and sodium sulfite is indicated on the probable involvement of the sulfhydryl groups in the functioning of the enzyme. Unlike most studied glycosidases the tested enzymes do not contain histidine imidazole group in the active center.
[Mh] Termos MeSH primário: Aspergillus flavus/química
Bacillus subtilis/química
Proteínas de Bactérias/química
Proteínas Fúngicas/química
alfa-Amilases/química
[Mh] Termos MeSH secundário: Alumínio/química
Aspergillus flavus/enzimologia
Bacillus subtilis/enzimologia
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/isolamento & purificação
Biocatálise
Carbodi-Imidas/química
Domínio Catalítico
Cátions
Cobre/química
Ácido Egtázico/química
Ensaios Enzimáticos
Etilmaleimida/química
Proteínas Fúngicas/antagonistas & inibidores
Proteínas Fúngicas/isolamento & purificação
Ferro/química
Cinética
Mercúrio/química
Sulfitos/química
alfa-Amilases/antagonistas & inibidores
alfa-Amilases/isolamento & purificação
Ácido p-Cloromercurobenzoico/química
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Carbodiimides); 0 (Cations); 0 (Fungal Proteins); 0 (Sulfites); 526U7A2651 (Egtazic Acid); 59-85-8 (p-Chloromercuribenzoic Acid); 789U1901C5 (Copper); CPD4NFA903 (Aluminum); E1UOL152H7 (Iron); EC 3.2.1.1 (alpha-Amylases); FXS1BY2PGL (Mercury); O3C74ACM9V (Ethylmaleimide); VTK01UQK3G (sodium sulfite)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:151123
[Lr] Data última revisão:
151123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151002
[St] Status:MEDLINE


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[PMID]:24971741
[Au] Autor:Wang L; Yuan L; Wang H; Liu X; Li X; Chen H
[Ad] Endereço:The Key Lab of Health Chemistry and Molecular Diagnosis of Suzhou, Department of Polymer Science and Engineering, College of Chemistry, Chemical Engineering and Materials Science, Soochow University , 199 Ren'ai Road, Suzhou, 215123, P. R. China.
[Ti] Título:New strategy for reversible modulation of protein activity through site-specific conjugation of small molecule and polymer.
[So] Source:Bioconjug Chem;25(7):1252-60, 2014 Jul 16.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A new strategy for accurate and reversible modulation of protein activity via simple conjugation of the sulfhydryl modifier and polymer with the introduced Cys residue in protein was developed in this study. With Escherichia coli inorganic pyrophosphatase (PPase) as a model protein, we used site-directed mutagenesis to generate a mutant PPase (PPC) with a substituted Cys residue at the specific Lys-148 site, which is within a conserved sequence near the active site and exposed to the surface of the PPC for chemical reaction. The site-specific conjugation of the mutated Cys residue in PPC with sulfhydryl modifier p-chloromercuribenzoate (PCMB) and pyridyl disulfide-functionalized poly(2-hydroxyethyl methacrylate) (pHEMA) resulted in obvious decrease or complete loss of the catalytic activity of PPC, due to the conformational change of PPC. Compared with the effect of small molecule modification (PCMB), the pHEMA conjugation led to greater inhibitory effect on protein activity due to the significant change of the tertiary structure of PPC after conjugation. Moreover, the protein activity can be restored to different extents by the treatment with different amount of reductive reagents, which can result in the dissociation between PPC and PCMB or pHEMA to recover the protein conformation. This study provides a new strategy for efficient control of protein activity at different levels by site-specific conjugation of a small molecule and polymer.
[Mh] Termos MeSH primário: Escherichia coli/enzimologia
Metacrilatos/metabolismo
Poli-Hidroxietil Metacrilato/metabolismo
Polímeros/metabolismo
Pirofosfatases/metabolismo
Compostos de Sulfidrila/metabolismo
Ácido p-Cloromercurobenzoico/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cinética
Metacrilatos/química
Mutagênese Sítio-Dirigida
Mutação/genética
Poli-Hidroxietil Metacrilato/química
Polímeros/química
Conformação Proteica
Pirofosfatases/química
Pirofosfatases/genética
Compostos de Sulfidrila/química
Ácido p-Cloromercurobenzoico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Methacrylates); 0 (Polymers); 0 (Sulfhydryl Compounds); 25249-16-5 (Polyhydroxyethyl Methacrylate); 59-85-8 (p-Chloromercuribenzoic Acid); 6E1I4IV47V (hydroxyethyl methacrylate); EC 3.6.1.- (Pyrophosphatases)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:140716
[Lr] Data última revisão:
140716
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140628
[St] Status:MEDLINE
[do] DOI:10.1021/bc5000934


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[PMID]:24355101
[Au] Autor:Marshall AC; Shaltout HA; Pirro NT; Rose JC; Diz DI; Chappell MC
[Ad] Endereço:Hypertension and Vascular Research Center, Wake Forest School of Medicine, Winston Salem, NC, United States.
[Ti] Título:Enhanced activity of an angiotensin-(1-7) neuropeptidase in glucocorticoid-induced fetal programming.
[So] Source:Peptides;52:74-81, 2014 Feb.
[Is] ISSN:1873-5169
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously identified angiotensin converting enzyme (ACE) and an endopeptidase activity that degraded angiotensin-(1-7) [Ang-(1-7)] to Ang-(1-5) and Ang-(1-4), respectively, in the cerebrospinal fluid (CSF) of 6-month old male sheep. The present study undertook a more comprehensive analysis of the CSF peptidase that converts Ang-(1-7) to Ang-(1-4) in control and in utero betamethasone-exposed sheep (BMX). Characterization of the Ang-(1-7) peptidase revealed that the thiol agents 4-aminophenylmercuric acetate (APMA) and p-chloromercuribenzoic acid (PCMB), as well as the metallo-chelators o-phenanthroline and EDTA essentially abolished the enzyme activity. Additional inhibitors for serine, aspartyl, and cysteine proteases, as well as selective inhibitors against the endopeptidases neprilysin, neurolysin, prolyl and thimet oligopeptidases did not attenuate enzymatic activity. Competition studies against the peptidase revealed similar IC50s for Ang-(1-7) (5µM) and Ang II (3µM), but lower values for Ala(1)-Ang-(1-7) and Ang-(2-7) of 1.8 and 2.0µM, respectively. In contrast, bradykinin exhibited a 6-fold higher IC50 (32µM) than Ang-(1-7) while neurotensin was a poor competitor. Mean arterial pressure (78±1 vs. 94±2mmHg, N=4-5, P<0.01) and Ang-(1-7) peptidase activity (14.2±1 vs 32±1.5fmol/min/ml CSF, N=5, P<0.01) were higher in the BMX group, and enzyme activity inversely correlated with Ang-(1-7) content in CSF. Lower Ang-(1-7) expression in brain is linked to baroreflex impairment in hypertension and aging, thus, increased activity of an Ang-(1-7) peptidase may contribute to lower CSF Ang-(1-7) levels, elevated blood pressure and impaired reflex function in this model of fetal programming.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Angiotensina I
Barorreflexo/fisiologia
Hipertensão/metabolismo
Fragmentos de Peptídeos
Peptidil Dipeptidase A
[Mh] Termos MeSH secundário: Angiotensina I/química
Angiotensina I/metabolismo
Animais
Ácido Edético/química
Masculino
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/metabolismo
Peptidil Dipeptidase A/química
Peptidil Dipeptidase A/metabolismo
Fenantrolinas/química
Acetato de Fenilmercúrio/análogos & derivados
Acetato de Fenilmercúrio/química
Ovinos
Especificidade por Substrato/fisiologia
Ácido p-Cloromercurobenzoico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Fragments); 0 (Phenanthrolines); 59-85-8 (p-Chloromercuribenzoic Acid); 6283-24-5 (4-aminophenylmercuriacetate); 9041-90-1 (Angiotensin I); 9G34HU7RV0 (Edetic Acid); EC 3.4.15.1 (Peptidyl-Dipeptidase A); IJ3FUK8MOF (angiotensin I (1-7)); OSX88361UX (Phenylmercuric Acetate); W4X6ZO7939 (1,10-phenanthroline)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131221
[St] Status:MEDLINE


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[PMID]:23591260
[Au] Autor:Thomas PW; Spicer T; Cammarata M; Brodbelt JS; Hodder P; Fast W
[Ad] Endereço:Division of Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX 78712, USA.
[Ti] Título:An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screening.
[So] Source:Bioorg Med Chem;21(11):3138-46, 2013 Jun 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Due to the global threat of antibiotic resistance mediated by New Delhi metallo-beta-lactamase-1 (NDM-1) and the lack of structurally diverse inhibitors reported for this enzyme, we developed screening and counter-screening assays for manual and automated formats. The manual assay is a trans-well absorbance-based endpoint assay in 96-well plates and has a Z' factor of 0.8. The automated assay is an epi-absorbance endpoint assay in 384-well plates, has a Z' factor of ≥0.8, good signal/baseline ratios (>3.8), and is likely scalable for high-throughput screening (HTS). A TEM-1-based counter-screen is also presented to eliminate false positives due to assay interference or off-target activities. A pilot screen of a pharmacologically characterized compound library identified two thiol-modifying compounds as authentic NDM-1 inhibitors: p-chloromecuribenzoate (p-CMB) and nitroprusside. Recombinant NDM-1 has one Cys residue that serves as a conserved active-site primary zinc ligand and is selectively modified by p-CMB as confirmed by LC-MS/MS. However a C208D mutation results in an enzyme that maintains almost full lactamase activity, yet is completely resistant to the inhibitor. These results predict that covalent targeting of the conserved active-site Cys residue may have drawbacks as a drug design strategy.
[Mh] Termos MeSH primário: Antibacterianos/química
Nitroprussiato/química
Zinco/química
Inibidores de beta-Lactamases
Ácido p-Cloromercurobenzoico/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cisteína/química
Cisteína/genética
Enterobacteriaceae/química
Enterobacteriaceae/enzimologia
Enterobacteriaceae/genética
Ensaios de Triagem em Larga Escala
Testes de Sensibilidade Microbiana
Mutação
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Espectrometria de Massas em Tandem
Resistência beta-Lactâmica
beta-Lactamases/química
beta-Lactamases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Recombinant Proteins); 0 (beta-Lactamase Inhibitors); 169D1260KM (Nitroprusside); 59-85-8 (p-Chloromercuribenzoic Acid); EC 3.5.2.6 (beta-Lactamases); EC 3.5.2.6 (beta-lactamase NDM-1); J41CSQ7QDS (Zinc); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130418
[St] Status:MEDLINE


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[PMID]:23511333
[Au] Autor:Santos KL; Vento MA; Wright JW; Speth RC
[Ad] Endereço:Pharmaceutical Sciences Department, College of Pharmacy, Nova Southeastern University, Fort Lauderdale, FL 33328, United States.
[Ti] Título:The effects of para-chloromercuribenzoic acid and different oxidative and sulfhydryl agents on a novel, non-AT1, non-AT2 angiotensin binding site identified as neurolysin.
[So] Source:Regul Pept;184:104-14, 2013 Jun 10.
[Is] ISSN:1873-1686
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A novel, non-AT1, non-AT2 brain binding site for angiotensin peptides that is unmasked by p-chloromercuribenzoate (PCMB) has been identified as a membrane associated variant of neurolysin. The ability of different organic and inorganic oxidative and sulfhydryl reactive agents to unmask or inhibit 125I-Sar1Ile8 angiotensin II (SI-Ang II) binding to this site was presently examined. In tissue membranes from homogenates of rat brain and testis incubated in assay buffer containing losartan (10 µM) and PD123319 (10 µM) plus 100 µM PCMB, 5 of the 39 compounds tested inhibited 125I-SI Ang II binding in brain and testis. Mersalyl acid, mercuric chloride (HgCl2) and silver nitrate (AgNO3) most potently inhibited 125I-SI Ang II binding with IC50s ~1-20 µM. This HgCl2 inhibition was independent of any interaction of HgCl2 with angiotensin II (Ang II) based on the lack of effect of HgCl2 on the dipsogenic effects of intracerebroventricularly administered Ang II and 125I-SI Ang II binding to AT1 receptors in the liver. Among sulfhydryl reagents, cysteamine and reduced glutathione (GSH), but not oxidized glutathione (GSSG) up to 1mM, inhibited PCMB-unmasked 125I-SI Ang II binding in brain and testis. Thimerosal and 4-hydroxymercuribenzoate moderately inhibited PCMB-unmasked 125I-SI Ang II binding in brain and testis at 100 µM; however, they also unmasked non-AT1, non-AT2 binding independent of PCMB. 4-Hydroxybenzoic acid did not promote 125 I-SI Ang II binding to this binding site indicating that only specific organomercurial compounds can unmask the binding site. The common denominator for all of these interacting substances is the ability to bind to protein cysteine sulfur. Comparison of cysteines between neurolysin and the closely related enzyme thimet oligopeptidase revealed an unconserved cysteine (cys650, based on the full length variant) in the proposed ligand binding channel (Brown et al., 2001) [45] near the active site of neurolysin. It is proposed that the mercuric ion in PCMB and closely related organomercurial compounds binds to cys650, while the acidic anion forms an ionic bond with a nearby arginine or lysine along the channel to effect a conformational change in neurolysin that promotes Ang II binding.
[Mh] Termos MeSH primário: Angiotensinas/metabolismo
Metaloendopeptidases/química
Compostos de Sulfidrila/farmacologia
Ácido p-Cloromercurobenzoico/farmacologia
[Mh] Termos MeSH secundário: Angiotensina I/química
Angiotensina I/metabolismo
Angiotensina II/química
Angiotensina II/metabolismo
Angiotensinas/antagonistas & inibidores
Angiotensinas/química
Animais
Sítios de Ligação
Losartan/farmacologia
Masculino
Metaloendopeptidases/metabolismo
Oxirredução
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Angiotensins); 0 (Sulfhydryl Compounds); 11128-99-7 (Angiotensin II); 59-85-8 (p-Chloromercuribenzoic Acid); 9041-90-1 (Angiotensin I); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.16 (neurolysin); JMS50MPO89 (Losartan)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130321
[St] Status:MEDLINE


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[PMID]:23412923
[Au] Autor:Swindle JD; Santos KL; Speth RC
[Ad] Endereço:Farquhar College of Arts and Sciences, Nova Southeastern University, Fort Lauderdale, FL, 33314, USA.
[Ti] Título:Pharmacological characterization of a novel non-AT1, non-AT2 angiotensin binding site identified as neurolysin.
[So] Source:Endocrine;44(2):525-31, 2013 Oct.
[Is] ISSN:1559-0100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The discovery of a novel non-AT1, non-AT2 binding site for angiotensins in the rodent brain and testis that is unmasked by the organomercurial compound para-chloromercuribenzoic acid (PCMB) has catalyzed efforts to purify and characterize this protein. We recently reported that this protein is neurolysin and now report upon the specificity of this binding site for various neuropeptides. Competition binding assays in rat brain and testis used (125)I-Sar(1), Ile(8) angiotensin II (Ang II) as the radioligand in the presence of saturating concentrations of AT1 and AT2 receptor antagonists and 100 µM parachloromercuribenzoate. Primary screening of 36 peptides and other compounds at 10 µM concentration revealed seven peptides that inhibited specific binding >50 %: ghrelin, Tyr(1) S36057 (a melanin-concentrating hormone receptor ligand), orphanin FQ and its congeners (Tyr(1) and Tyr(14)), Dynorphin A (1-8), and Ang (1-9). The selective neurolysin inhibitor Proline-Isoleucine dipeptide was inactive at 1 mM. These results suggest that the ability of PCMB to unmask high affinity binding of Ang II to neurolysin is a pharmacological effect and that neurolysin may significantly affect the activity of the renin-angiotensin system.
[Mh] Termos MeSH primário: Angiotensina II/metabolismo
Metaloendopeptidases/metabolismo
Ácido p-Cloromercurobenzoico/farmacologia
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/efeitos dos fármacos
Ligação Competitiva/efeitos dos fármacos
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Masculino
Metaloendopeptidases/química
Metaloendopeptidases/isolamento & purificação
Biblioteca de Peptídeos
Ligação Proteica/efeitos dos fármacos
Ratos
Ratos Sprague-Dawley
Receptores de Angiotensina/metabolismo
Testículo/efeitos dos fármacos
Testículo/metabolismo
Ácido p-Cloromercurobenzoico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Peptide Library); 0 (Receptors, Angiotensin); 11128-99-7 (Angiotensin II); 59-85-8 (p-Chloromercuribenzoic Acid); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.16 (neurolysin)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130216
[St] Status:MEDLINE
[do] DOI:10.1007/s12020-013-9898-x


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[PMID]:23123479
[Au] Autor:Yamaguchi T; Iwata Y; Miura S; Kawada K
[Ad] Endereço:Department of Chemistry, Faculty of Science, Fukuoka University, Fukuoka 814­0180, Japan. takeo@fukuoka-u.ac.jp
[Ti] Título:Reinvestigation of drugs and chemicals as aquaporin-1 inhibitors using pressure-induced hemolysis in human erythrocytes.
[So] Source:Biol Pharm Bull;35(11):2088-91, 2012.
[Is] ISSN:1347-5215
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Recently, we have found that pressure-induced hemolysis is enhanced by inhibiting water transport via aquaporin-1 (AQP1), as seen in p-chloromercuribenzoate (pCMB)-treated erythrocytes. So, using this method we reinvestigated the functions as AQP1 inhibitors of drugs and chemicals such as acetazolamide, sodium nitroprusside, tetraethylammonium ions (TEA(+)), and dimethylsulfoxide (DMSO). The values of hemolysis at 200 MPa were almost unaffected by acetazolamide or sodium nitroprusside, decreased by TEA(+), and increased significantly by DMSO. Furthermore, the erythrocytes were exposed to pCMB in the presence of TEA(+) or DMSO. The enhancement effect of pCMB on pressure-induced hemolysis was unaffected by TEA(+) but attenuated by DMSO. Taken together, these results suggest that, of drugs and chemicals examined here, DMSO only is an AQP1 inhibitor, but the effect of DMSO is small compared with pCMB.
[Mh] Termos MeSH primário: Aquaporina 1/antagonistas & inibidores
Dimetil Sulfóxido/farmacologia
Eritrócitos/efeitos dos fármacos
Hemólise/efeitos dos fármacos
[Mh] Termos MeSH secundário: Acetazolamida/farmacologia
Células Cultivadas
Eritrócitos/fisiologia
Seres Humanos
Nitroprussiato/farmacologia
Pressão
Tetraetilamônio/farmacologia
Ácido p-Cloromercurobenzoico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
146410-94-8 (Aquaporin 1); 169D1260KM (Nitroprusside); 59-85-8 (p-Chloromercuribenzoic Acid); 66-40-0 (Tetraethylammonium); O3FX965V0I (Acetazolamide); YOW8V9698H (Dimethyl Sulfoxide)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121106
[St] Status:MEDLINE


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[PMID]:23088096
[Au] Autor:Gudzenko OV; Varbanets' LD
[Ti] Título:[Investigation of functional groups of Cryptococcus albidus alpha-L-rhamnosidase].
[So] Source:Mikrobiol Z;74(4):19-28, 2012 Jul-Aug.
[Is] ISSN:1028-0987
[Cp] País de publicação:Ukraine
[La] Idioma:ukr
[Ab] Resumo:The effect of cations, anions and specific chemical reagents: 1-[3-(dimethylamino)propyl]-3-ethylcarbodimide methiodide, EDTA, o-phenantroline, dithiotreitol, L-cysteine, beta-mercaptoethanol, p-chlormercurybenzoate (p-ChMB), N-ethylmaleimide on the alpha-L-rhamnosidase activity of Cryptococcus albidus has been investigated. The essential role of Ag+ which inhibits the alpha-L-rhamnosidase activity by 72.5% was shown. Rhamnose at 1-5 mM protect the enzyme from the negative effect of Ag(+). It was expected that carboxyl group of C-terminal aminoacid and imidazole group of histidine would participate in the catalytic action of alpha-L-rhamnosidase on the basis of inhibition and kinetic analysis.
[Mh] Termos MeSH primário: Cryptococcus/enzimologia
Proteínas Fúngicas/química
Glicosídeo Hidrolases/química
Ramnose/química
Prata/química
[Mh] Termos MeSH secundário: Biocatálise
Cátions Monovalentes
Cryptococcus/química
Cisteína/química
Ditiotreitol/química
Ácido Edético/química
Etildimetilaminopropil Carbodi-Imida/análogos & derivados
Etildimetilaminopropil Carbodi-Imida/química
Etilmaleimida/química
Proteínas Fúngicas/isolamento & purificação
Proteínas Fúngicas/metabolismo
Glicosídeo Hidrolases/isolamento & purificação
Glicosídeo Hidrolases/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Mercaptoetanol/química
Fenantrolinas/química
Especificidade por Substrato
Ácido p-Cloromercurobenzoico/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations, Monovalent); 0 (Fungal Proteins); 0 (Phenanthrolines); 3M4G523W1G (Silver); 59-85-8 (p-Chloromercuribenzoic Acid); 60-24-2 (Mercaptoethanol); 73U5123RNT (1-ethyl-3-(3-(dimethylamino)propyl)carbodiimide methiodide); 9G34HU7RV0 (Edetic Acid); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.40 (alpha-L-rhamnosidase); K848JZ4886 (Cysteine); O3C74ACM9V (Ethylmaleimide); QN34XC755A (Rhamnose); RJ5OZG6I4A (Ethyldimethylaminopropyl Carbodiimide); T8ID5YZU6Y (Dithiothreitol); W4X6ZO7939 (1,10-phenanthroline)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121024
[St] Status:MEDLINE


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[PMID]:21897027
[Au] Autor:Mitsukura K; Suzuki M; Shinoda S; Kuramoto T; Yoshida T; Nagasawa T
[Ad] Endereço:Department of Biomolecular Science, Faculty of Engineering, Gifu University. mitukura@gifu-u.ac.jp
[Ti] Título:Purification and characterization of a novel (R)-imine reductase from Streptomyces sp. GF3587.
[So] Source:Biosci Biotechnol Biochem;75(9):1778-82, 2011.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The (R)-imine reductase (RIR) of Streptomyces sp. GF3587 was purified and characterized. It was found to be a NADPH-dependent enzyme, and was found to be a homodimer consisting of 32 kDa subunits. Enzymatic reduction of 10 mM 2-methyl-1-pyrroline (2-MPN) resulted in the formation of 9.8 mM (R)-2-methylpyrrolidine ((R)-2-MP) with 99% e.e. The enzyme showed not only reduction activity for 2-MPN at neutral pH (6.5-8.0), but also oxidation activity for (R)-2-MP under alkaline pH (10-11.5) conditions. It appeared to be a sulfhydryl enzyme based on the sensitivity to sulfhydryl specific inhibitors. It was very specific to 2-MPN as substrate.
[Mh] Termos MeSH primário: Iminas/metabolismo
Oxirredutases/metabolismo
Subunidades Proteicas/química
Pirróis/metabolismo
Pirrolidinas/metabolismo
Streptomyces/enzimologia
[Mh] Termos MeSH secundário: Cromatografia em Gel
Dimerização
Eletroforese em Gel de Poliacrilamida
Concentração de Íons de Hidrogênio
Cinética
Metilação
Peso Molecular
NADP/metabolismo
Oxirredutases/antagonistas & inibidores
Oxirredutases/química
Oxirredutases/isolamento & purificação
Streptomyces/química
Especificidade por Substrato
Reagentes de Sulfidrila/farmacologia
Ácido p-Cloromercurobenzoico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-methylpyrrolidine); 0 (Imines); 0 (Protein Subunits); 0 (Pyrroles); 0 (Pyrrolidines); 0 (Sulfhydryl Reagents); 28350-87-0 (pyrroline); 53-59-8 (NADP); 59-85-8 (p-Chloromercuribenzoic Acid); EC 1.- (Oxidoreductases)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:110928
[Lr] Data última revisão:
110928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110908
[St] Status:MEDLINE


  10 / 387 MEDLINE  
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[PMID]:20861168
[Au] Autor:Rashid M; Arumugam TV; Karamyan VT
[Ad] Endereço:Department of Pharmaceutical Sciences and Vascular Drug Research Center, School of Pharmacy, Texas Tech University Health Sciences Center, Amarillo, Texas 79106, USA.
[Ti] Título:Association of the novel non-AT1, non-AT2 angiotensin binding site with neuronal cell death.
[So] Source:J Pharmacol Exp Ther;335(3):754-61, 2010 Dec.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have discovered a non-AT(1), non-AT(2) angiotensin binding site in rodent and human brain membranes, which, based on its pharmacological/biochemical properties and tissue distribution, is different from angiotensin receptors and key proteases processing angiotensins. In this study, the novel angiotensin binding site was localized to a specific brain cell type by using radioligand receptor binding assays. Our results indicate that the novel binding site is expressed in mouse primary cortical neuronal membranes but not in primary cortical astroglial and bEnd.3 brain capillary endothelial cell membranes. Whole-cell binding assays in neurons showed that the binding site faces the outer side of the plasma membrane. Consistent with our previous observations, the novel binding site was unmasked by the sulfhydryl reagent p-chloromercuribenzoate. This effect had a bell-shaped curve and was reversed by reduced glutathione, indicating that the function of the binding site might be regulated by the redox state of the environment. Density of the novel binding site measured by saturation binding assays was significantly increased in neuronal membranes of cells challenged in four in vitro models of cell death (oxygen-glucose deprivation, sodium azide-induced hypoxia, N-methyl-D-aspartate neurotoxicity, and hydrogen peroxide neurotoxicity). In addition, our in vivo data from developing mouse brains showed that the density of the novel angiotensin binding site changes similarly to the pattern of neuronal death in maturating brain. This is the first time that evidence is provided on the association of the novel angiotensin binding site with neuronal death, and future studies directed toward understanding of the functions of this protein are warranted.
[Mh] Termos MeSH primário: Neurônios/citologia
Neurônios/metabolismo
Receptores de Angiotensina/metabolismo
[Mh] Termos MeSH secundário: 1-Sarcosina-8-Isoleucina Angiotensina II/metabolismo
4-Cloromercuriobenzenossulfonato/farmacologia
Angiotensina II/metabolismo
Bloqueadores do Receptor Tipo 1 de Angiotensina II/farmacologia
Bloqueadores do Receptor Tipo 2 de Angiotensina II/farmacologia
Animais
Morte Celular/efeitos dos fármacos
Morte Celular/fisiologia
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Córtex Cerebral/citologia
Córtex Cerebral/metabolismo
Feminino
Glutationa/farmacologia
Dissulfeto de Glutationa/farmacologia
Cinética
Camundongos
Camundongos Endogâmicos
Neurônios/efeitos dos fármacos
Prosencéfalo/citologia
Prosencéfalo/embriologia
Prosencéfalo/crescimento & desenvolvimento
Prosencéfalo/metabolismo
Ligação Proteica/efeitos dos fármacos
Ligação Proteica/fisiologia
Receptores de Superfície Celular/antagonistas & inibidores
Receptores de Superfície Celular/metabolismo
Frações Subcelulares/efeitos dos fármacos
Frações Subcelulares/metabolismo
Temperatura Ambiente
Ácido p-Cloromercurobenzoico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Angiotensin II Type 1 Receptor Blockers); 0 (Angiotensin II Type 2 Receptor Blockers); 0 (Receptors, Angiotensin); 0 (Receptors, Cell Surface); 11128-99-7 (Angiotensin II); 59-85-8 (p-Chloromercuribenzoic Acid); 5YIN07W42H (4-Chloromercuribenzenesulfonate); 9088-01-1 (1-Sarcosine-8-Isoleucine Angiotensin II); GAN16C9B8O (Glutathione); ULW86O013H (Glutathione Disulfide)
[Em] Mês de entrada:1102
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100924
[St] Status:MEDLINE
[do] DOI:10.1124/jpet.110.171439



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