Base de dados : MEDLINE
Pesquisa : D08.811.913.477.700.525 [Categoria DeCS]
Referências encontradas : 6 [refinar]
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  1 / 6 MEDLINE  
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[PMID]:22595184
[Au] Autor:Han S; Auger C; Appanna VP; Lemire J; Castonguay Z; Akbarov E; Appanna VD
[Ad] Endereço:Department of Chemistry and Biochemistry, Laurentian University, Sudbury, Ontario, Canada.
[Ti] Título:A blue native polyacrylamide gel electrophoretic technology to probe the functional proteomics mediating nitrogen homeostasis in Pseudomonas fluorescens.
[So] Source:J Microbiol Methods;90(3):206-10, 2012 Sep.
[Is] ISSN:1872-8359
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:As glutamate and ammonia play a pivotal role in nitrogen homeostasis, their production is mediated by various enzymes that are widespread in living organisms. Here, we report on an effective electrophoretic method to monitor these enzymes. The in gel activity visualization is based on the interaction of the products, glutamate and ammonia, with glutamate dehydrogenase (GDH, EC: 1.4.1.2) in the presence of either phenazine methosulfate (PMS) or 2,6-dichloroindophenol (DCIP) and iodonitrotetrazolium (INT). The intensity of the activity bands was dependent on the amount of proteins loaded, the incubation time and the concentration of the respective substrates. The following enzymes were readily identified: glutaminase (EC: 3.5.1.2), alanine transaminase (EC: 2.6.1.2), aspartate transaminase (EC: 2.6.1.1), glycine transaminase (EC: 2.6.1.4), ornithine oxoacid aminotransferase (EC: 2.6.1.13), and carbamoyl phosphate synthase I (EC: 6.3.4.16). The specificity of the activity band was confirmed by high pressure liquid chromatography (HPLC) following incubation of the excised band with the corresponding substrates. These bands are amenable to further molecular characterization by a variety of analytical methods. This electrophoretic technology provides a powerful tool to screen these enzymes that contribute to nitrogen homeostasis in Pseudomonas fluorescens and possibly in other microbial systems.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Eletroforese em Gel de Poliacrilamida/métodos
Homeostase
Nitrogênio/metabolismo
Pseudomonas fluorescens/metabolismo
[Mh] Termos MeSH secundário: 2,6-Dicloroindofenol/química
Alanina Transaminase/química
Alanina Transaminase/isolamento & purificação
Alanina Transaminase/metabolismo
Amônia/química
Aspartato Aminotransferases/química
Aspartato Aminotransferases/isolamento & purificação
Aspartato Aminotransferases/metabolismo
Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/metabolismo
Carbamoil-Fosfato Sintase (Amônia)/química
Carbamoil-Fosfato Sintase (Amônia)/isolamento & purificação
Carbamoil-Fosfato Sintase (Amônia)/metabolismo
Ensaios Enzimáticos
Glutamato Desidrogenase/química
Ácido Glutâmico/química
Glutaminase/química
Glutaminase/isolamento & purificação
Glutaminase/metabolismo
Glicina Transaminase/química
Glicina Transaminase/isolamento & purificação
Glicina Transaminase/metabolismo
Metilfenazônio Metossulfato/química
Ornitina-Oxo-Ácido Transaminase/química
Ornitina-Oxo-Ácido Transaminase/isolamento & purificação
Ornitina-Oxo-Ácido Transaminase/metabolismo
Proteômica
Pseudomonas fluorescens/enzimologia
Sais de Tetrazólio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Tetrazolium Salts); 146-68-9 (iodonitrotetrazolium); 299-11-6 (Methylphenazonium Methosulfate); 3KX376GY7L (Glutamic Acid); 7664-41-7 (Ammonia); C35QN2Z58B (2,6-Dichloroindophenol); EC 1.4.1.2 (Glutamate Dehydrogenase); EC 2.6.1.1 (Aspartate Aminotransferases); EC 2.6.1.13 (Ornithine-Oxo-Acid Transaminase); EC 2.6.1.2 (Alanine Transaminase); EC 2.6.1.4 (Glycine Transaminase); EC 3.5.1.2 (Glutaminase); EC 6.3.4.16 (Carbamoyl-Phosphate Synthase (Ammonia)); N762921K75 (Nitrogen)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120519
[St] Status:MEDLINE
[do] DOI:10.1016/j.mimet.2012.05.006


  2 / 6 MEDLINE  
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[PMID]:20565126
[Au] Autor:French JB; Ealick SE
[Ad] Endereço:Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
[Ti] Título:Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway.
[So] Source:Biochemistry;49(29):5975-7, 2010 Jul 27.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many plants, fungi, and bacteria catabolize allantoin as a mechanism for nitrogen assimilation. Recent reports have shown that in plants and some bacteria the product of hydrolysis of allantoin by allantoinase is the unstable intermediate ureidoglycine. While this molecule can spontaneously decay, genetic analysis of some bacterial genomes indicates that an aminotransferase may be present in the pathway. Here we present evidence that Klebsiella pneumoniae HpxJ is an aminotransferase that preferentially converts ureidoglycine and an alpha-keto acid into oxalurate and the corresponding amino acid. We determined the crystal structure of HpxJ, allowing us to present an explanation for substrate specificity.
[Mh] Termos MeSH primário: Glicina Transaminase/química
Glicina/análogos & derivados
Klebsiella pneumoniae/enzimologia
Ureia/análogos & derivados
Ácido Úrico/metabolismo
[Mh] Termos MeSH secundário: Catálise
Glicina/metabolismo
Glicina Transaminase/genética
Conformação Proteica
Ureia/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ureidoglycine); 268B43MJ25 (Uric Acid); 8W8T17847W (Urea); EC 2.6.1.4 (Glycine Transaminase); TE7660XO1C (Glycine)
[Em] Mês de entrada:1008
[Cu] Atualização por classe:161122
[Lr] Data última revisão:
161122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100623
[St] Status:MEDLINE
[do] DOI:10.1021/bi1006755


  3 / 6 MEDLINE  
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[PMID]:20214682
[Au] Autor:Kameya M; Arai H; Ishii M; Igarashi Y
[Ad] Endereço:Department of Biotechnology, The University of Tokyo, Tokyo, Japan.
[Ti] Título:Purification of three aminotransferases from Hydrogenobacter thermophilus TK-6--novel types of alanine or glycine aminotransferase: enzymes and catalysis.
[So] Source:FEBS J;277(8):1876-85, 2010 Apr.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aminotransferases catalyse synthetic and degradative reactions of amino acids, and serve as a key linkage between central carbon and nitrogen metabolism in most organisms. In this study, three aminotransferases (AT1, AT2 and AT3) were purified and characterized from Hydrogenobacter thermophilus, a hydrogen-oxidizing chemolithoautotrophic bacterium, which has been reported to possess unique features in its carbon and nitrogen anabolism. AT1, AT2 and AT3 exhibited glutamate:oxaloacetate aminotransferase, glutamate:pyruvate aminotransferase and alanine:glyoxylate aminotransferase activities, respectively. In addition, both AT1 and AT2 catalysed a glutamate:glyoxylate aminotransferase reaction. Interestingly, phylogenetic analysis showed that AT2 belongs to aminotransferase family IV, whereas known glutamate:pyruvate aminotransferases and glutamate:glyoxylate aminotransferases are members of family Igamma. In contrast, AT3 was classified into family I, distant from eukaryotic alanine:glyoxylate aminotransferases which belong to family IV. Although Thermococcus litoralis alanine:glyoxylate aminotransferase is the sole known example of family I alanine:glyoxylate aminotransferases, it is indicated that this alanine:glyoxylate aminotransferase and AT3 are derived from distinct lineages within family I, because neither high sequence similarity nor putative substrate-binding residues are shared by these two enzymes. To our knowledge, this study is the first report of the primary structure of bacterial glutamate:glyoxylate aminotransferase and alanine:glyoxylate aminotransferase, and demonstrates the presence of novel types of aminotransferase phylogenetically distinct from known eukaryotic and archaeal isozymes.
[Mh] Termos MeSH primário: Alanina Transaminase/isolamento & purificação
Eucariotos/enzimologia
Glicina Transaminase/isolamento & purificação
Transaminases/isolamento & purificação
[Mh] Termos MeSH secundário: Alanina Transaminase/genética
Alanina Transaminase/metabolismo
Sequência de Aminoácidos
Catálise
Sequência Conservada
Glicina Transaminase/genética
Glicina Transaminase/metabolismo
Isoenzimas/genética
Isoenzimas/isolamento & purificação
Isoenzimas/metabolismo
Cinética
Modelos Biológicos
Dados de Sequência Molecular
Filogenia
Especificidade por Substrato/genética
Transaminases/genética
Transaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); EC 2.6.1.- (Transaminases); EC 2.6.1.2 (Alanine Transaminase); EC 2.6.1.4 (Glycine Transaminase)
[Em] Mês de entrada:1005
[Cu] Atualização por classe:100416
[Lr] Data última revisão:
100416
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100311
[St] Status:MEDLINE
[do] DOI:10.1111/j.1742-4658.2010.07604.x


  4 / 6 MEDLINE  
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[PMID]:12784618
[Au] Autor:Yamaguchi H; Ohtani M; Amachi S; Shinoyama H; Fujii T
[Ad] Endereço:Department of Bioresources Science, Graduate School of Science and Technology, Chiba University, 648 Matsudo, Matsudo-shi, Chiba 271-8510, Japan.
[Ti] Título:Some properties of glycine aminotransferase purified from Rhodopseudomonas palustris No. 7 concerning extracellular porphyrin production.
[So] Source:Biosci Biotechnol Biochem;67(4):783-9, 2003 Apr.
[Is] ISSN:0916-8451
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycine aminotransferase (EC 2.6.1.4; GlyAT) was presumed to be an enzyme concerning the supply of glycine for the extracellular porphyrin production by Rhodopseudomonas palustris No. 7. GlyAT was purified from strain No. 7 as an electrophoretically homogenous protein. The enzyme was a monomer protein with the molecular weight of about 42,000. From the absorption spectrum of the enzyme (350 nm, 410 nm), it was indicated that the enzyme had pyridoxal phosphate as a prosthetic group. The enzyme showed high substrate specificity for glutamate as an amino group donor. Apparent Kms for glutamate and glyoxylate were 6.20 mM and 3.75 mM, respectively. The Vmax and Kcat for glutamate were 66.8 mumol/min/mg protein and 46.8 s-1, respectively. The Vmax and Kcat for glyoxylate were 68.8 mumol/min/mg protein and 48.2 s-1. The optimum temperature and pH were 40-45 degrees C and 7.0-7.5, respectively. The enzyme activity lowered to about 50% in the presence of 15 mM ammonium chloride.
[Mh] Termos MeSH primário: Porfirinas/biossíntese
Rodopseudomonas/enzimologia
Transaminases/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/farmacologia
Glicina/biossíntese
Glicina/metabolismo
Glicina Transaminase
Glioxilatos/metabolismo
Concentração de Íons de Hidrogênio
Peso Molecular
Especificidade por Substrato
Temperatura Ambiente
Transaminases/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Glyoxylates); 0 (Porphyrins); EC 2.6.1.- (Transaminases); EC 2.6.1.4 (Glycine Transaminase); JQ39C92HH6 (glyoxylic acid); TE7660XO1C (Glycine)
[Em] Mês de entrada:0309
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030606
[St] Status:MEDLINE


  5 / 6 MEDLINE  
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[PMID]:10547044
[Au] Autor:Orzechowski S; Socha-Hanc J; Paszkowski A
[Ad] Endereço:Department of Biochemistry, Faculty of Agriculture, Warsaw Agricultural University, Warszawa, Poland.
[Ti] Título:Alanine aminotransferase and glycine aminotransferase from maize (Zea mays L.) leaves.
[So] Source:Acta Biochim Pol;46(2):447-57, 1999.
[Is] ISSN:0001-527X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Alanine aminotransferase (AlaAT, EC 2.6.1.2) and glycine aminotransferase (GlyAT, EC 2.6.1.4), two different enzymes catalyzing transamination reactions with L-alanine as the amino-acid substrate, were examined in maize in which alanine participates substantially in nitrogen transport. Preparative PAGE of a partially purified preparation of aminotransferases from maize leaves gave 6 fractions differing in electrophoretic mobility. The fastest migrating fraction I represents AlaAT specific for L-alanine as amino donor and 2-oxoglutarate as amino acceptor. The remaining fractions showed three aminotransferase activities: L-alanine-2-oxoglutarate, L-alanine-glyoxylate and L-glutamate-glyoxylate. By means of molecular sieving on Zorbax SE-250 two groups of enzymes were distinguished in the PAGE fractions: of about 100 kDa and 50 kDa. Molecular mass of 104 kDa was ascribed to AlaAT in fraction I, while the molecular mass of the three enzymatic activities in 3 fractions of the low electrophoretic mobility was about 50 kDa. The response of these fractions to: aminooxyacetate, 3-chloro-L-alanine and competing amino acids prompted us to suggest that five out of the six preparative PAGE fractions represented GlyAT isoforms, differing from each other by the L-glutamate-glyoxylate:L-alanine-glyoxylate:L-alanine-2-oxoglutarate activity ratio.
[Mh] Termos MeSH primário: Alanina Transaminase/metabolismo
Transaminases/metabolismo
Zea mays/enzimologia
[Mh] Termos MeSH secundário: Alanina Transaminase/química
Alanina Transaminase/isolamento & purificação
Eletroforese em Gel de Poliacrilamida
Glicina Transaminase
Peso Molecular
Folhas de Planta/enzimologia
Transaminases/química
Transaminases/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.6.1.- (Transaminases); EC 2.6.1.2 (Alanine Transaminase); EC 2.6.1.4 (Glycine Transaminase)
[Em] Mês de entrada:9911
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:991105
[St] Status:MEDLINE


  6 / 6 MEDLINE  
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[PMID]:3386016
[Au] Autor:Muramoto H
[Ti] Título:[Metabolism of guanidinoacetic acid and creatine in uremia].
[So] Source:Nihon Jinzo Gakkai Shi;30(2):117-28, 1988 Feb.
[Is] ISSN:0385-2385
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Mh] Termos MeSH primário: Creatina/sangue
Glicina/análogos & derivados
Uremia/metabolismo
[Mh] Termos MeSH secundário: Animais
Creatina/metabolismo
Feminino
Glicina/sangue
Glicina/metabolismo
Glicina Transaminase
Guanidinas/farmacologia
Seres Humanos
Rim/metabolismo
Masculino
Meia-Idade
Músculos/metabolismo
Pâncreas/metabolismo
Propionatos/farmacologia
Coelhos
Diálise Renal
Transaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Guanidines); 0 (Propionates); EC 2.6.1.- (Transaminases); EC 2.6.1.4 (Glycine Transaminase); GO52O1A04E (glycocyamine); MU72812GK0 (Creatine); TE7660XO1C (Glycine); UL1984YRKA (guanidinopropionic acid)
[Em] Mês de entrada:8808
[Cu] Atualização por classe:161123
[Lr] Data última revisão:
161123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:880201
[St] Status:MEDLINE



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