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[PMID]:26879543
[Au] Autor:Hatori Y; Yan Y; Schmidt K; Furukawa E; Hasan NM; Yang N; Liu CN; Sockanathan S; Lutsenko S
[Ad] Endereço:Department of Physiology, Johns Hopkins University, School of Medicine, 725 N. Wolfe street, Baltimore, 21205 Maryland, USA.
[Ti] Título:Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway.
[So] Source:Nat Commun;7:10640, 2016 Feb 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Brain development requires a fine-tuned copper homoeostasis. Copper deficiency or excess results in severe neuro-pathologies. We demonstrate that upon neuronal differentiation, cellular demand for copper increases, especially within the secretory pathway. Copper flow to this compartment is facilitated through transcriptional and metabolic regulation. Quantitative real-time imaging revealed a gradual change in the oxidation state of cytosolic glutathione upon neuronal differentiation. Transition from a broad range of redox states to a uniformly reducing cytosol facilitates reduction of the copper chaperone Atox1, liberating its metal-binding site. Concomitantly, expression of Atox1 and its partner, a copper transporter ATP7A, is upregulated. These events produce a higher flux of copper through the secretory pathway that balances copper in the cytosol and increases supply of the cofactor to copper-dependent enzymes, expression of which is elevated in differentiated neurons. Direct link between glutathione oxidation and copper compartmentalization allows for rapid metabolic adjustments essential for normal neuronal function.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Amidina-Liases/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Cobre/metabolismo
Glutationa/metabolismo
Metalochaperonas/metabolismo
Oxigenases de Função Mista/metabolismo
Neurogênese
Neurônios/metabolismo
Oxirredução
Via Secretória
[Mh] Termos MeSH secundário: Animais
Embrião de Galinha
ATPases Transportadoras de Cobre
Citosol
Eletroporação
Dissulfeto de Glutationa/metabolismo
Células HEK293
Seres Humanos
Immunoblotting
NADP/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Espectrofotometria Atômica
Medula Espinal/citologia
Medula Espinal/embriologia
Medula Espinal/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (ATOX1 protein, human); 0 (Cation Transport Proteins); 0 (Metallochaperones); 53-59-8 (NADP); 789U1901C5 (Copper); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (PAM protein, human); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.3.54 (ATP7A protein, human); EC 3.6.3.54 (Copper-transporting ATPases); EC 4.3.2.- (Amidine-Lyases); GAN16C9B8O (Glutathione); ULW86O013H (Glutathione Disulfide)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160217
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms10640


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[PMID]:26667899
[Au] Autor:Kumar D; Mains RE; Eipper BA
[Ad] Endereço:Departments of Molecular Biology and BiophysicsUniversity of Connecticut Health Center, Farmington, Connecticut, USA.
[Ti] Título:60 YEARS OF POMC: From POMC and α-MSH to PAM, molecular oxygen, copper, and vitamin C.
[So] Source:J Mol Endocrinol;56(4):T63-76, 2016 May.
[Is] ISSN:1479-6813
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A critical role for peptide C-terminal amidation was apparent when the first bioactive peptides were identified. The conversion of POMC into adrenocorticotropic hormone and then into α-melanocyte-stimulating hormone, an amidated peptide, provided a model system for identifying the amidating enzyme. Peptidylglycine α-amidating monooxygenase (PAM), the only enzyme that catalyzes this modification, is essential; mice lacking PAM survive only until mid-gestation. Purification and cloning led to the discovery that the amidation of peptidylglycine substrates proceeds in two steps: peptidylglycine α-hydroxylating monooxygenase catalyzes the copper- and ascorbate-dependent α-hydroxylation of the peptidylglycine substrate; peptidyl-α-hydroxyglycine α-amidating lyase cleaves the N-C bond, producing amidated product and glyoxylate. Both enzymes are contained in the luminal domain of PAM, a type 1 integral membrane protein. The structures of both catalytic cores have been determined, revealing how they interact with metals, molecular oxygen, and substrate to catalyze both reactions. Although not essential for activity, the intrinsically disordered cytosolic domain is essential for PAM trafficking. A phylogenetic survey led to the identification of bifunctional membrane PAM in Chlamydomonas, a unicellular eukaryote. Accumulating evidence points to a role for PAM in copper homeostasis and in retrograde signaling from the lumen of the secretory pathway to the nucleus. The discovery of PAM in cilia, cellular antennae that sense and respond to environmental stimuli, suggests that much remains to be learned about this ancient protein.
[Mh] Termos MeSH primário: Amidina-Liases/metabolismo
Ácido Ascórbico/metabolismo
Cobre/metabolismo
Oxigênio/metabolismo
Pró-Opiomelanocortina/metabolismo
alfa-MSH/metabolismo
[Mh] Termos MeSH secundário: Processamento Alternativo
Amidina-Liases/química
Amidina-Liases/genética
Animais
Cílios/metabolismo
Evolução Molecular
Técnicas de Inativação de Genes
Genótipo
Seres Humanos
Oxigenases de Função Mista/química
Oxigenases de Função Mista/genética
Oxigenases de Função Mista/metabolismo
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Obesidade/etiologia
Obesidade/metabolismo
Pró-Opiomelanocortina/química
Domínios e Motivos de Interação entre Proteínas
Proteólise
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Multienzyme Complexes); 581-05-5 (alpha-MSH); 66796-54-1 (Pro-Opiomelanocortin); 789U1901C5 (Copper); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (peptidylglycine monooxygenase); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.5 (peptidylamidoglycolate lyase); PQ6CK8PD0R (Ascorbic Acid); S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151216
[St] Status:MEDLINE
[do] DOI:10.1530/JME-15-0266


  3 / 69 MEDLINE  
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[PMID]:26614892
[Au] Autor:Zielinski M; Wójtowicz-Krawiec A; Mikiewicz D; Kesik-Brodacka M; Cecuda-Adamczewska V; Marciniak-Rusek A; Sokolowska I; Lukasiewicz N; Gurba L; Odrowaz-Sypniewski M; Baran P; Plucienniczak G; Plucienniczak A; Borowicz P; Szewczyk B
[Ad] Endereço:Institute of Biotechnology and Antibiotics, Staroscinska 5, Warszawa 02-516, Poland. Electronic address: marcinzielinski2@wp.pl.
[Ti] Título:Expression of recombinant human bifunctional peptidylglycine α-amidating monooxygenase in CHO cells and its use for insulin analogue modification.
[So] Source:Protein Expr Purif;119:102-9, 2016 Mar.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The availability of catalytically active peptidylglycine α-amidating monooxygenase (PAM) should provide the means to examine its potential use for the chemienzymatic synthesis of bioactive peptides for the purpose of pharmacological studies. Hypoglycemic activity is one of the most important features of insulin derivatives. Insulin glargine amide was found to show a time/effect profile which is distinctly more flat and thus more advantageous than insulin glargine itself. The aim of the study was to obtain recombinant PAM and use it for insulin analogue amidation. We stably expressed a recombinant PAM in CHO dhfr-cells in culture. Recombinant PAM was partially purified by fractional ammonium sulphate precipitation and ion-exchange chromatography. The enzyme was used to modify glycine-extended A22(G)-B31(K)-B32(R) human insulin analogue (GKR). Alpha-amidated insulin was analyzed by HPLC and mass spectrometry. Hypoglycemic activity of amidated and non-amidated insulin was compared. The pharmacodynamic effect was based on glucose concentration measurement in Wistar rats with hyperglycemia induced by streptozotocin. The overall glycemic profile up to 36 h was evaluated after subcutaneous single dosing at a range of 2.5-7.5 U/kg b.w. The experiment on rats confirmed with a statistical significance (P < 0.05) hypoglycemic activity of GKR-NH2 in comparison to a control group receiving 0.9% NaCl. Characteristics for GKR-NH2 profile was a rather fast beginning of action (0.5-2.0 h) and quite prolonged return to initial values. GKR-NH2 is a candidate for a hypoglycemic drug product in diabetes care. In addition, this work also provides a valuable alternative method for preparing any other recombinant bioactive peptides with C-terminal amidation.
[Mh] Termos MeSH primário: Amidina-Liases/biossíntese
Hipoglicemiantes/química
Insulina/análogos & derivados
Insulina/química
Oxigenases de Função Mista/biossíntese
Proteínas Recombinantes/biossíntese
[Mh] Termos MeSH secundário: Amidina-Liases/química
Amidina-Liases/isolamento & purificação
Animais
Glicemia
Células CHO
Cromatografia em Gel
Cromatografia Líquida de Alta Pressão
Cricetinae
Cricetulus
Diabetes Mellitus Experimental/tratamento farmacológico
Avaliação Pré-Clínica de Medicamentos
Feminino
Hipoglicemiantes/farmacologia
Insulina/farmacologia
Masculino
Oxigenases de Função Mista/química
Oxigenases de Função Mista/isolamento & purificação
Ratos Wistar
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Hypoglycemic Agents); 0 (Insulin); 0 (Recombinant Proteins); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (PAM protein, human); EC 4.3.2.- (Amidine-Lyases)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151129
[St] Status:MEDLINE


  4 / 69 MEDLINE  
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[PMID]:25020232
[Au] Autor:Shin I; Han K; Rhee S
[Ad] Endereço:Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Korea.
[Ti] Título:Structural insights into the substrate specificity of (s)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase.
[So] Source:J Mol Biol;426(17):3028-40, 2014 Aug 26.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In plants, the ureide pathway is a metabolic route that converts the ring nitrogen atoms of purine into ammonia via sequential enzymatic reactions, playing an important role in nitrogen recovery. In the final step of the pathway, (S)-ureidoglycolate amidohydrolase (UAH) catalyzes the conversion of (S)-ureidoglycolate into glyoxylate and releases two molecules of ammonia as by-products. UAH is homologous in structure and sequence with allantoate amidohydrolase (AAH), an upstream enzyme in the pathway with a similar function as that of an amidase but with a different substrate. Both enzymes exhibit strict substrate specificity and catalyze reactions in a concerted manner, resulting in purine degradation. Here, we report three crystal structures of Arabidopsis thaliana UAH (bound with substrate, reaction intermediate, and product) and a structure of Escherichia coli AAH complexed with allantoate. Structural analyses of UAH revealed a distinct binding mode for each ligand in a bimetal reaction center with the active site in a closed conformation. The ligand directly participates in the coordination shell of two metal ions and is stabilized by the surrounding residues. In contrast, AAH, which exhibits a substrate-binding site similar to that of UAH, requires a larger active site due to the additional ureido group in allantoate. Structural analyses and mutagenesis revealed that both enzymes undergo an open-to-closed conformational transition in response to ligand binding and that the active-site size and the interaction environment in UAH and AAH are determinants of the substrate specificities of these two structurally homologous enzymes.
[Mh] Termos MeSH primário: Amidina-Liases/química
Arabidopsis/enzimologia
Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
Ureo-Hidrolases/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Complexos de Coordenação/química
Cristalografia por Raios X
Glioxilatos/química
Hidrólise
Cinética
Modelos Moleculares
Ligação Proteica
Homologia Estrutural de Proteína
Especificidade por Substrato
Ureia/análogos & derivados
Ureia/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coordination Complexes); 0 (Escherichia coli Proteins); 0 (Glyoxylates); 02WGT7SHWJ (allantoic acid); 8W8T17847W (Urea); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.- (allantoate amidohydrolase); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.3 (ureidoglycollate lyase); JQ39C92HH6 (glyoxylic acid)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140715
[St] Status:MEDLINE


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[PMID]:24464100
[Au] Autor:Steinthorsdottir V; Thorleifsson G; Sulem P; Helgason H; Grarup N; Sigurdsson A; Helgadottir HT; Johannsdottir H; Magnusson OT; Gudjonsson SA; Justesen JM; Harder MN; Jørgensen ME; Christensen C; Brandslund I; Sandbæk A; Lauritzen T; Vestergaard H; Linneberg A; Jørgensen T; Hansen T; Daneshpour MS; Fallah MS; Hreidarsson AB; Sigurdsson G; Azizi F; Benediktsson R; Masson G; Helgason A; Kong A; Gudbjartsson DF; Pedersen O; Thorsteinsdottir U; Stefansson K
[Ad] Endereço:deCODE Genetics/Amgen, Inc., Reykjavik, Iceland.
[Ti] Título:Identification of low-frequency and rare sequence variants associated with elevated or reduced risk of type 2 diabetes.
[So] Source:Nat Genet;46(3):294-8, 2014 Mar.
[Is] ISSN:1546-1718
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Through whole-genome sequencing of 2,630 Icelanders and imputation into 11,114 Icelandic cases and 267,140 controls followed by testing in Danish and Iranian samples, we discovered 4 previously unreported variants affecting risk of type 2 diabetes (T2D). A low-frequency (1.47%) variant in intron 1 of CCND2, rs76895963[G], reduces risk of T2D by half (odds ratio (OR) = 0.53, P = 5.0 × 10(-21)) and is correlated with increased CCND2 expression. Notably, this variant is also associated with both greater height and higher body mass index (1.17 cm per allele, P = 5.5 × 10(-12) and 0.56 kg/m(2) per allele, P = 6.5 × 10(-7), respectively). In addition, two missense variants in PAM, encoding p.Asp563Gly (frequency of 4.98%) and p.Ser539Trp (frequency of 0.65%), confer moderately higher risk of T2D (OR = 1.23, P = 3.9 × 10(-10) and OR = 1.47, P = 1.7 × 10(-5), respectively), and a rare (0.20%) frameshift variant in PDX1, encoding p.Gly218Alafs*12, associates with high risk of T2D (OR = 2.27, P = 7.3 × 10(-7)).
[Mh] Termos MeSH primário: Amidina-Liases/genética
Ciclina D2/genética
Diabetes Mellitus Tipo 2/genética
Variação Genética
Proteínas de Homeodomínio/genética
Oxigenases de Função Mista/genética
Transativadores/genética
[Mh] Termos MeSH secundário: Estatura/genética
Peso Corporal/genética
Estudos de Casos e Controles
Dinamarca
Diabetes Mellitus Tipo 2/patologia
Feminino
Frequência do Gene
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Seres Humanos
Islândia
Irã (Geográfico)
Masculino
Polimorfismo de Nucleotídeo Único
Fatores de Risco
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CCND2 protein, human); 0 (Cyclin D2); 0 (Homeodomain Proteins); 0 (Trans-Activators); 0 (pancreatic and duodenal homeobox 1 protein); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (PAM protein, human); EC 4.3.2.- (Amidine-Lyases)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:170603
[Lr] Data última revisão:
170603
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140128
[St] Status:MEDLINE
[do] DOI:10.1038/ng.2882


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[PMID]:24107613
[Au] Autor:Percudani R; Carnevali D; Puggioni V
[Ad] Endereço:Department of Life Sciences, Laboratory of Biochemistry, Molecular Biology and Bioinformatics, University of Parma, Italy.
[Ti] Título:Ureidoglycolate hydrolase, amidohydrolase, lyase: how errors in biological databases are incorporated in scientific papers and vice versa.
[So] Source:Database (Oxford);2013:bat071, 2013.
[Is] ISSN:1758-0463
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An opaque biochemical definition, an insufficient functional characterization, an interpolated database description, and a beautiful 3D structure with a wrong reaction. All these are elements of an exemplar case of misannotation in biological databases and confusion in the scientific literature concerning genes and enzymes acting on ureidoglycolate, an intermediate of purine catabolism. Here we show biochemical evidence for the relocation of genes assigned to EC 3.5.3.19 (ureidoglycolate hydrolase, releasing ammonia), such as allA of Escherichia coli or DAL3 of Saccharomyces cerevisiae, to EC 4.3.2.3 (ureidoglycolate lyase, releasing urea). The EC 3.5.3.19 should be more appropriately named ureidoglycolate amidohydrolase and include genes equivalent to UAH of Arabidopsis thaliana. The distinction between ammonia- or urea-releasing activities from ureidoglycolate is relevant for the understanding of nitrogen metabolism in various organisms and of virulence factors in certain pathogens rather than a nomenclature problem. We trace the original fault in database annotation and provide a rationale for its incorporation and persistence in the scientific literature. Notwithstanding the technological distance, yet not surprising for the constancy of human nature, error categories and mechanisms established in the study of the work of amanuensis monks still apply to the modern curation of biological databases.
[Mh] Termos MeSH primário: Amidina-Liases/metabolismo
Aminoidrolases/metabolismo
Bases de Dados como Assunto
Publicações
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Biocatálise
Escherichia coli/enzimologia
Glicolatos/química
Glicolatos/metabolismo
Seres Humanos
Nitrogênio/metabolismo
Saccharomyces cerevisiae/enzimologia
Terminologia como Assunto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycolates); EC 3.5.4.- (Aminohydrolases); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.3 (ureidoglycollate lyase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131011
[St] Status:MEDLINE
[do] DOI:10.1093/database/bat071


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[PMID]:23583291
[Au] Autor:Wise HZ; Hung CY; Whiston E; Taylor JW; Cole GT
[Ad] Endereço:Department of Biology and South Texas Center for Emerging Infectious Diseases, University of Texas at San Antonio, San Antonio, TX 78249, USA.
[Ti] Título:Extracellular ammonia at sites of pulmonary infection with Coccidioides posadasii contributes to severity of the respiratory disease.
[So] Source:Microb Pathog;59-60:19-28, 2013 Jun-Jul.
[Is] ISSN:1096-1208
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Coccidioides is the causative agent of a potentially life-threatening respiratory disease of humans. A feature of this mycosis is that pH measurements of the microenvironment of pulmonary abscesses are consistently alkaline due to ammonia production during the parasitic cycle. We previously showed that enzymatically active urease is partly responsible for elevated concentrations of extracellular ammonia at sites of lung infection and contributes to both localized host tissue damage and exacerbation of the respiratory disease in BALB/c mice. Disruption of the urease gene (URE) of Coccidioides posadasii only partially reduced the amount of ammonia detected during in vitro growth of the parasitic phase, suggesting that other ammonia-producing pathways exist that may also contribute to the virulence of this pathogen. Ureidoglycolate hydrolase (Ugh) expressed by bacteria, fungi and higher plants catalyzes the hydrolysis of ureidoglycolate to yield glyoxylate and the release CO2 and ammonia. This enzymatic pathway is absent in mice and humans. Ureidoglycolate hydrolase gene deletions were conducted in a wild type (WT) isolate of C. posadasii as well as the previously generated Δure knock-out strain. Restorations of UGH in the mutant stains were performed to generate and evaluate the respective revertants. The double mutant revealed a marked decrease in the amount of extracellular ammonia without loss of reproductive competence in vitro compared to both the WT and Δure parental strains. BALB/c mice challenged intranasally with the Δugh/Δure mutant showed 90% survival after 30 days, decreased fungal burden, and well-organized pulmonary granulomas. We conclude that loss of both Ugh and Ure activity significantly reduced the virulence of this fungal pathogen.
[Mh] Termos MeSH primário: Amidina-Liases/metabolismo
Amônia/metabolismo
Coccidioides/metabolismo
Coccidioides/patogenicidade
Coccidioidomicose/patologia
Pneumopatias Fúngicas/patologia
Urease/metabolismo
[Mh] Termos MeSH secundário: Amidina-Liases/genética
Animais
Coccidioides/enzimologia
Coccidioides/genética
Coccidioidomicose/microbiologia
Modelos Animais de Doenças
Técnicas de Inativação de Genes
Seres Humanos
Pneumopatias Fúngicas/microbiologia
Camundongos
Camundongos Endogâmicos BALB C
Análise de Sobrevida
Urease/genética
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
7664-41-7 (Ammonia); EC 3.5.1.5 (Urease); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.3 (ureidoglycollate lyase)
[Em] Mês de entrada:1311
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130416
[St] Status:MEDLINE


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[PMID]:23263489
[Au] Autor:Huyghe JR; Jackson AU; Fogarty MP; Buchkovich ML; Stancáková A; Stringham HM; Sim X; Yang L; Fuchsberger C; Cederberg H; Chines PS; Teslovich TM; Romm JM; Ling H; McMullen I; Ingersoll R; Pugh EW; Doheny KF; Neale BM; Daly MJ; Kuusisto J; Scott LJ; Kang HM; Collins FS; Abecasis GR; Watanabe RM; Boehnke M; Laakso M; Mohlke KL
[Ad] Endereço:Center for Statistical Genetics, Department of Biostatistics, University of Michigan, Ann Arbor, Michigan, USA.
[Ti] Título:Exome array analysis identifies new loci and low-frequency variants influencing insulin processing and secretion.
[So] Source:Nat Genet;45(2):197-201, 2013 Feb.
[Is] ISSN:1546-1718
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Insulin secretion has a crucial role in glucose homeostasis, and failure to secrete sufficient insulin is a hallmark of type 2 diabetes. Genome-wide association studies (GWAS) have identified loci contributing to insulin processing and secretion; however, a substantial fraction of the genetic contribution remains undefined. To examine low-frequency (minor allele frequency (MAF) 0.5-5%) and rare (MAF < 0.5%) nonsynonymous variants, we analyzed exome array data in 8,229 nondiabetic Finnish males using the Illumina HumanExome Beadchip. We identified low-frequency coding variants associated with fasting proinsulin concentrations at the SGSM2 and MADD GWAS loci and three new genes with low-frequency variants associated with fasting proinsulin or insulinogenic index: TBC1D30, KANK1 and PAM. We also show that the interpretation of single-variant and gene-based tests needs to consider the effects of noncoding SNPs both nearby and megabases away. This study demonstrates that exome array genotyping is a valuable approach to identify low-frequency variants that contribute to complex traits.
[Mh] Termos MeSH primário: Exoma/genética
Variação Genética
Insulina/genética
Insulina/secreção
[Mh] Termos MeSH secundário: Amidina-Liases/genética
Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte/genética
Jejum/sangue
Finlândia
Frequência do Gene
Genética Populacional
Genótipo
Fatores de Troca do Nucleotídeo Guanina/genética
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Masculino
Oxigenases de Função Mista/genética
Anotação de Sequência Molecular
Proinsulina/sangue
Proteínas Supressoras de Tumor/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 (Death Domain Receptor Signaling Adaptor Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Insulin); 0 (Intracellular Signaling Peptides and Proteins); 0 (KANK1 protein, human); 0 (MADD protein, human); 0 (SGSM2 protein, human); 0 (Tumor Suppressor Proteins); 9035-68-1 (Proinsulin); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (PAM protein, human); EC 4.3.2.- (Amidine-Lyases)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:161209
[Lr] Data última revisão:
161209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121225
[St] Status:MEDLINE
[do] DOI:10.1038/ng.2507


  9 / 69 MEDLINE  
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[PMID]:22496439
[Au] Autor:Attenborough RM; Hayward DC; Kitahara MV; Miller DJ; Ball EE
[Ad] Endereço:Evolution, Ecology and Genetics, Research School of Biology, Australian National University, Canberra, ACT 0200, Australia.
[Ti] Título:A "neural" enzyme in nonbilaterian animals and algae: preneural origins for peptidylglycine α-amidating monooxygenase.
[So] Source:Mol Biol Evol;29(10):3095-109, 2012 Oct.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secreted peptides, produced by enzymatic processing of larger precursor molecules, are found throughout the animal kingdom and play important regulatory roles as neurotransmitters and hormones. Many require a carboxy-terminal modification, involving the conversion of a glycine residue into an α-amide, for their biological activity. Two sequential enzymatic activities catalyze this conversion: a monooxygenase (peptidylglycine α-hydroxylating monooxygenase or PHM) and an amidating lyase (peptidyl-α-hydroxyglycine α-amidating lyase or PAL). In vertebrates, these activities reside in a single polypeptide known as peptidylglycine α-amidating monooxygenase (PAM), which has been extensively studied in the context of neuropeptide modification. Bifunctional PAMs have been reported from some invertebrates, but the phylogenetic distribution of PAMs and their evolutionary relationship to PALs and PHMs is unclear. Here, we report sequence and expression data for two PAMs from the coral Acropora millepora (Anthozoa, Cnidaria), as well as providing a comprehensive survey of the available sequence data from other organisms. These analyses indicate that bifunctional PAMs predate the origins of the nervous and endocrine systems, consistent with the idea that within the Metazoa their ancestral function may have been to amidate epitheliopeptides. More surprisingly, the phylogenomic survey also revealed the presence of PAMs in green algae (but not in higher plants or fungi), implying that the bifunctional enzyme either predates the plant/animal divergence and has subsequently been lost in a number of lineages or perhaps that convergent evolution or lateral gene transfer has occurred. This finding is consistent with recent discoveries that other molecules once thought of as "neural" predate nervous systems.
[Mh] Termos MeSH primário: Antozoários/enzimologia
Clorófitas/enzimologia
Oxigenases de Função Mista/genética
Complexos Multienzimáticos/genética
Neurônios/enzimologia
[Mh] Termos MeSH secundário: Processamento Alternativo/genética
Amidina-Liases/química
Amidina-Liases/metabolismo
Sequência de Aminoácidos
Animais
Antozoários/genética
Biocatálise
Evolução Molecular
Regulação Enzimológica da Expressão Gênica
Oxigenases de Função Mista/química
Oxigenases de Função Mista/metabolismo
Dados de Sequência Molecular
Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
Filogenia
Estrutura Terciária de Proteína
Homologia de Sequência de Aminoácidos
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Multienzyme Complexes); EC 1.- (Mixed Function Oxygenases); EC 1.14.17.3 (peptidylglycine monooxygenase); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.5 (peptidylamidoglycolate lyase)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:120926
[Lr] Data última revisão:
120926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120413
[St] Status:MEDLINE


  10 / 69 MEDLINE  
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Texto completo
[PMID]:20813786
[Au] Autor:Muñoz A; Bannenberg GL; Montero O; Cabello-Díaz JM; Piedras P; Pineda M
[Ad] Endereço:Departamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CSIC), E-28049 Madrid, Spain.
[Ti] Título:An alternative pathway for ureide usage in legumes: enzymatic formation of a ureidoglycolate adduct in Cicer arietinum and Phaseolus vulgaris.
[So] Source:J Exp Bot;62(1):307-18, 2011 Jan.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ureidoglycolate is an intermediate in the degradation of the ureides, allantoin and allantoate, found in many organisms. In some leguminous plant species these compounds are used to transport recently fixed nitrogen in the root nodules to the aerial parts of the plant. In the present study, it was demonstrated that purified ureidoglycolases from chickpea (Cicer arietinum) and French bean (Phaseolus vulgaris) do not produce glyoxylate, and can use phenylhydrazine as a substrate with K(m) values of 4.0 mM and 8.5 mM, respectively. Furthermore, these enzymes catalyse the transfer of the ureidoglycolyl group to phenylhydrazine to produce ureidoglycolyl phenylhydrazide, which degrades non-enzymatically to glyoxylate phenylhydrazone and urea. This supports their former classification as ureidoglycolate urea-lyases. The enzymatic reaction catalysed by the characterized ureidoglycolases uncovered here can be viewed as a novel type of phenylhydrazine ureidoglycolyl transferase. The implications of these findings for ureide metabolism in legume nitrogen metabolism are discussed.
[Mh] Termos MeSH primário: Amidina-Liases/metabolismo
Cicer/metabolismo
Glicolatos/metabolismo
Phaseolus/metabolismo
Proteínas de Plantas/metabolismo
Ureia/metabolismo
[Mh] Termos MeSH secundário: Amidina-Liases/genética
Cicer/enzimologia
Cicer/genética
Redes e Vias Metabólicas
Nitrogênio/metabolismo
Phaseolus/enzimologia
Phaseolus/genética
Proteínas de Plantas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glycolates); 0 (Plant Proteins); 0WT12SX38S (glycolic acid); 8W8T17847W (Urea); EC 4.3.2.- (Amidine-Lyases); EC 4.3.2.3 (ureidoglycollate lyase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1103
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100904
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/erq268



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