Base de dados : MEDLINE
Pesquisa : D08.811.682.047.820.200 [Categoria DeCS]
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[PMID]:26059458
[Au] Autor:Wang D; Zhou J; Chen C; Wei D; Shi J; Jiang B; Liu P; Hao J
[Ad] Endereço:Lab of Biorefinery, Shanghai Advanced Research Institute, Chinese Academy of Sciences, No. 99 Haike Road, Pudong, Shanghai, 201210, People's Republic of China.
[Ti] Título:R-acetoin accumulation and dissimilation in Klebsiella pneumoniae.
[So] Source:J Ind Microbiol Biotechnol;42(8):1105-15, 2015 Aug.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Klebsiella pneumoniae is a 2,3-butanediol producer, and R-acetoin is an intermediate of 2,3-butanediol production. R-acetoin accumulation and dissimilation in K. pneumoniae was studied here. A budC mutant, which has lost 2,3-butanediol dehydrogenase activity, accumulated high levels of R-acetoin in culture broth. However, after glucose was exhausted, the accumulated R-acetoin could be reused by the cells as a carbon source. Acetoin dehydrogenase enzyme system, encoded by acoABCD, was responsible for R-acetoin dissimilation. acoABCD mutants lost the ability to grow on acetoin as the sole carbon source, and the acetoin accumulated could not be dissimilated. However, in the presence of another carbon source, the acetoin accumulated in broth of acoABCD mutants was converted to 2,3-butanediol. Parameters of R-acetoin production by budC mutants were optimized in batch culture. Aerobic culture and mildly acidic conditions (pH 6-6.5) favored R-acetoin accumulation. At the optimized conditions, in fed-batch fermentation, 62.3 g/L R-acetoin was produced by budC and acoABCD double mutant in 57 h culture, with an optical purity of 98.0 %, and a substrate conversion ratio of 28.7 %.
[Mh] Termos MeSH primário: Acetoína/metabolismo
Klebsiella pneumoniae/enzimologia
Klebsiella pneumoniae/genética
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/genética
Acetoína Desidrogenase/metabolismo
Técnicas de Cultura Celular por Lotes
Butileno Glicóis/metabolismo
Carbono/química
Meios de Cultura/química
Escherichia coli/enzimologia
Escherichia coli/genética
Fermentação
Concentração de Íons de Hidrogênio
Plasmídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Butylene Glycols); 0 (Culture Media); 45427ZB5IJ (2,3-butylene glycol); 7440-44-0 (Carbon); BG4D34CO2H (Acetoin); EC 1.1.1.- (Acetoin Dehydrogenase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150611
[St] Status:MEDLINE
[do] DOI:10.1007/s10295-015-1638-1


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[PMID]:25272750
[Au] Autor:Kang ZH; Ren CC; Zhang JL; Dong JG; Li X; Wei XJ
[Ti] Título:Purification and cloning of nicosulfuron-degrading enzymes from Bacillus subtilis YB1.
[So] Source:Prikl Biokhim Mikrobiol;50(1):39-43, 2014 Jan-Feb.
[Is] ISSN:0555-1099
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:The nicosulfuron-degrading enzymes from Bacillus subtilis strain YB1 were purified and their genes were cloned. The proteins of bacterial culture filtrate were precipitated with ammonium sulfate or acetone. The extracellular proteins concentrated by acetone were purified from DEAE-Sepharose Fast Flow chromatography. The four protein peaks eluted from DEAE-column were separated and purified by native PAGE. Three components (P1-1, P3-2, P4-3) had nicosulfuron-degrading activity, and component P4-3 degradated 57.5% of this compound. The molecular weights of the components were 33.5, 54.8 and 37.0 kDa, respectively. The amino acid sequences of nicosulfuron-degrading enzymes from B. subtilis YB1 were determined by MALDI-TOF-MS, indicating these enzymes as manganese ABC transporter, vegetative catalase 1 and acetoin dehydrogenase E1, respectively. Using PCR amplification, genes 918, 1428, 1026 bp in size were detected for the enzymes studied.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/isolamento & purificação
Acetoína Desidrogenase/isolamento & purificação
Bacillus subtilis/química
Proteínas de Bactérias/isolamento & purificação
Catalase/isolamento & purificação
Piridinas/química
Compostos de Sulfonilureia/química
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/química
Transportadores de Cassetes de Ligação de ATP/genética
Acetoína Desidrogenase/química
Acetoína Desidrogenase/genética
Bacillus subtilis/enzimologia
Bacillus subtilis/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biodegradação Ambiental
Catalase/química
Catalase/genética
Cromatografia por Troca Iônica
Clonagem Molecular
Poluentes Ambientais/química
Escherichia coli/genética
Escherichia coli/metabolismo
Herbicidas/química
Peso Molecular
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Environmental Pollutants); 0 (Herbicides); 0 (Pyridines); 0 (Recombinant Proteins); 0 (Sulfonylurea Compounds); CG297D9264 (nicosulfuron); EC 1.1.1.- (Acetoin Dehydrogenase); EC 1.11.1.6 (Catalase)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:141002
[Lr] Data última revisão:
141002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141003
[St] Status:MEDLINE


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[PMID]:24614328
[Au] Autor:Gao X; Xu N; Li S; Liu L
[Ad] Endereço:State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China; Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, China; Laboratory of Food Microbial-Manufacturing Engineering, Jiangnan Univ
[Ti] Título:Metabolic engineering of Candida glabrata for diacetyl production.
[So] Source:PLoS One;9(3):e89854, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, Candida glabrata, an efficient pyruvate-producing strain, was metabolically engineered for the production of the food ingredient diacetyl. A diacetyl biosynthetic pathway was reconstructed based on genetic modifications and medium optimization. The former included (i) channeling carbon flux into the diacetyl biosynthetic pathway by amplification of acetolactate synthase, (ii) elimination of the branched pathway of α-acetolactate by deleting the ILV5 gene, and (iii) restriction of diacetyl degradation by deleting the BDH gene. The resultant strain showed an almost 1∶1 co-production of α-acetolactate and diacetyl (0.95 g L(-1)). Furthermore, addition of Fe3+ to the medium enhanced the conversion of α-acetolactate to diacetyl and resulted in a two-fold increase in diacetyl production (2.1 g L(-1)). In addition, increased carbon flux was further channeled into diacetyl biosynthetic pathway and a titer of 4.7 g L(-1) of diacetyl was achieved by altering the vitamin level in the flask culture. Thus, this study illustrates that C. glabrata could be tailored as an attractive platform for enhanced biosynthesis of beneficial products from pyruvate by metabolic engineering strategies.
[Mh] Termos MeSH primário: Candida glabrata/metabolismo
Diacetil/metabolismo
Engenharia Metabólica/métodos
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/metabolismo
Acetolactato Sintase/metabolismo
Oxirredutases do Álcool/metabolismo
Candida glabrata/crescimento & desenvolvimento
Ciclo do Carbono/efeitos dos fármacos
Meios de Cultura
Descarboxilação/efeitos dos fármacos
Fermentação/efeitos dos fármacos
Deleção de Genes
Ferro/farmacologia
Lactatos/metabolismo
Redes e Vias Metabólicas/efeitos dos fármacos
NAD/metabolismo
Niacina/farmacologia
Ácido Pirúvico/metabolismo
Tiamina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); 0 (Lactates); 0U46U6E8UK (NAD); 2679MF687A (Niacin); 535-17-1 (alpha-acetolactate); 8558G7RUTR (Pyruvic Acid); E1UOL152H7 (Iron); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (Acetoin Dehydrogenase); EC 1.1.1.4 (butanediol dehydrogenase); EC 2.2.1.6 (Acetolactate Synthase); K324J5K4HM (Diacetyl); X66NSO3N35 (Thiamine)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:140311
[Lr] Data última revisão:
140311
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140312
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0089854


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[PMID]:23568047
[Au] Autor:Wang Z; Song Q; Yu M; Wang Y; Xiong B; Zhang Y; Zheng J; Ying X
[Ad] Endereço:College of Biological and Environmental Engineering, Zhejiang University of Technology, 18 Chaowang Road, Hangzhou, Zhejiang, 310014, China.
[Ti] Título:Characterization of a stereospecific acetoin(diacetyl) reductase from Rhodococcus erythropolis WZ010 and its application for the synthesis of (2S,3S)-2,3-butanediol.
[So] Source:Appl Microbiol Biotechnol;98(2):641-50, 2014 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Rhodococcus erythropolis WZ010 was capable of producing optically pure (2S,3S)-2,3-butanediol in alcoholic fermentation. The gene encoding an acetoin(diacetyl) reductase from R. erythropolis WZ010 (ReADR) was cloned, overexpressed in Escherichia coli, and subsequently purified by Ni-affinity chromatography. ReADR in the native form appeared to be a homodimer with a calculated subunit size of 26,864, belonging to the family of the short-chain dehydrogenase/reductases. The enzyme accepted a broad range of substrates including aliphatic and aryl alcohols, aldehydes, and ketones. It exhibited remarkable tolerance to dimethyl sulfoxide (DMSO) and retained 53.6 % of the initial activity after 4 h incubation with 30 % (v/v) DMSO. The enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2S,3S)-2,3-butanediol via (S)-acetoin. The optimal pH and temperature for diacetyl reduction were pH 7.0 and 30 °C, whereas those for (2S,3S)-2,3-butanediol oxidation were pH 9.5 and 25 °C. Under the optimized conditions, the activity of diacetyl reduction was 11.9-fold higher than that of (2S,3S)-2,3-butanediol oxidation. Kinetic parameters of the enzyme showed lower K(m) values and higher catalytic efficiency for diacetyl and NADH in comparison to those for (2S,3S)-2,3-butanediol and NAD⁺, suggesting its physiological role in favor of (2S,3S)-2,3-butanediol formation. Interestingly, the enzyme showed higher catalytic efficiency for (S)-1-phenylethanol oxidation than that for acetophenone reduction. ReADR-catalyzed asymmetric reduction of diacetyl was coupled with stereoselective oxidation of 1-phenylethanol, which simultaneously formed both (2S,3S)-2,3-butanediol and (R)-1-phenylethanol in great conversions and enantiomeric excess values.
[Mh] Termos MeSH primário: Acetoína Desidrogenase/metabolismo
Butileno Glicóis/metabolismo
Rhodococcus/enzimologia
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/química
Acetoína Desidrogenase/genética
Acetoína Desidrogenase/isolamento & purificação
Cromatografia de Afinidade
Clonagem Molecular
DNA Bacteriano/química
DNA Bacteriano/genética
Estabilidade Enzimática
Escherichia coli/genética
Expressão Gênica
Concentração de Íons de Hidrogênio
Cinética
Dados de Sequência Molecular
Peso Molecular
Multimerização Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Rhodococcus/genética
Análise de Sequência de DNA
Estereoisomerismo
Especificidade por Substrato
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Butylene Glycols); 0 (DNA, Bacterial); 0 (Recombinant Proteins); 45427ZB5IJ (2,3-butylene glycol); EC 1.1.1.- (Acetoin Dehydrogenase)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130410
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-013-4870-5


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[PMID]:23701367
[Au] Autor:Gao J; Xu YY; Li FW; Ding G
[Ad] Endereço:Schol of Chemical and Biological Engineering, Yancheng Institute of Technology, Yancheng, China.
[Ti] Título:Production of S-acetoin from diacetyl by Escherichia coli transformant cells that express the diacetyl reductase gene of Paenibacillus polymyxa ZJ-9.
[So] Source:Lett Appl Microbiol;57(4):274-81, 2013 Oct.
[Is] ISSN:1472-765X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: S-acetoin (S-AC) is an important four-carbon chiral compound that has unique industrial applications in the asymmetric synthesis of valuable chiral specialty chemicals. However, previous studies showed that the usually low yield and optical purity of S-AC as well as the very high substrate cost have hindered the application of this compound. In the current work, a gene encoding diacetyl reductase (DAR) from a Paenibacillus polymyxa strain ZJ-9 was cloned and expressed in Escherichia coli. Whole cells of the recombinant E. coli were used to produce S-AC from diacetyl (DA). Under optimal conditions, S-AC with high optical purity (purity >99·9%) was obtained with a yield of 13·5 ± 0·24 and 39·4 ± 0·38 g l(-1) under batch and fed-batch culture conditions, respectively. This process featured the biotransformation of DA into S-AC using whole cells of engineered E. coli. The result is a considerable increase in the yield and optical purity of S-AC, which in turn facilitated the practical application of the compound. SIGNIFICANCE AND IMPACT OF THE STUDY: This study demonstrated a highly efficient new method to produce S-acetoin with higher than 99·9% optical purity from diacetyl using whole cells of engineered Escherichia coli. It will therefore decrease the production cost of S-acetoin and highlight its application in asymmetric synthesis of highly valuable chiral compounds.
[Mh] Termos MeSH primário: Acetoína Desidrogenase/genética
Acetoína/metabolismo
Proteínas de Bactérias/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Paenibacillus/enzimologia
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/metabolismo
Proteínas de Bactérias/metabolismo
Diacetil/metabolismo
Expressão Gênica
Engenharia Genética
Paenibacillus/genética
Transformação Bacteriana
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); BG4D34CO2H (Acetoin); EC 1.1.1.- (Acetoin Dehydrogenase); K324J5K4HM (Diacetyl)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:130930
[Lr] Data última revisão:
130930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130525
[St] Status:MEDLINE
[do] DOI:10.1111/lam.12107


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[PMID]:20171216
[Au] Autor:Payne KA; Hough DW; Danson MJ
[Ad] Endereço:Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath, UK.
[Ti] Título:Discovery of a putative acetoin dehydrogenase complex in the hyperthermophilic archaeon Sulfolobus solfataricus.
[So] Source:FEBS Lett;584(6):1231-4, 2010 Mar 19.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Like many other aerobic archaea, the hyperthermophile Sulfolobus solfataricus possesses a gene cluster encoding components of a putative 2-oxoacid dehydrogenase complex. In the current paper, we have cloned and expressed the first two genes of this cluster and demonstrate that the protein products form an alpha(2)beta(2) hetero-tetramer possessing the catalytic activity characteristic of the first component enzyme of an acetoin dehydrogenase multienzyme complex. This represents the first report of an acetoin multienzyme complex in archaea, and contrasts with the branched-chain 2-oxoacid dehydrogenase complex activities characterised in two other archaea, Thermoplasma acidophilum and Haloferax volcanii.
[Mh] Termos MeSH primário: Acetoína Desidrogenase/isolamento & purificação
Complexos Multienzimáticos/isolamento & purificação
Sulfolobus solfataricus/enzimologia
[Mh] Termos MeSH secundário: Acetoína/metabolismo
Acetoína Desidrogenase/genética
Acetoína Desidrogenase/metabolismo
Archaea/química
Archaea/enzimologia
Archaea/genética
Sequência de Bases
Clonagem Molecular
Temperatura Alta
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Família Multigênica
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Especificidade por Substrato
Sulfolobus solfataricus/química
Sulfolobus solfataricus/genética
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Multienzyme Complexes); 0 (Recombinant Proteins); BG4D34CO2H (Acetoin); EC 1.1.1.- (Acetoin Dehydrogenase)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100223
[St] Status:MEDLINE
[do] DOI:10.1016/j.febslet.2010.02.037


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[PMID]:17139509
[Au] Autor:An HY; Tsuda H; Miyamoto T
[Ad] Endereço:The Graduate School of Natural Science and Technology, Okayama University, Tsushima, Okayama, 700-8530, Japan.
[Ti] Título:Expression of citrate permease gene of plasmid pCM1 isolated from Lactococcus lactis subsp. lactis biovar diacetylactis NIAI N-7 in Lactobacillus casei L-49-4.
[So] Source:Appl Microbiol Biotechnol;74(3):609-16, 2007 Mar.
[Is] ISSN:0175-7598
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Recombinant vector pJLECit (8,232 bp) was constructed using citrate permease gene contained in the 3,919-bp fragment of plasmid pCM1 (8,280 bp) isolated from Lactococcus lactis subsp. lactis biovar diacetylactis NIAI N-7, repA and ori from pLU1, and pMB1 ori and the erythromycin resistance gene from pJIR418. Lactobacillus casei L-49-4 (plasmid-free mutant of strain L-49) harboring the constructed pJLECit converted citrate into diacetyl/acetoin. Citrate uptake rate of resting cells was the highest at pH 5.5 and 10 mM citrate concentration. Diacetyl formation activity by the cell-free extracts of Lb. casei L-49-4 (pJLECit) grown in de Man-Rogosa-Sharpe (MRS) broth was higher than that of cells grown in MRS broth without citrate. On the other hand, diacetyl reductase activity of cells grown in MRS broth was lower than that of cells grown in MRS broth without citrate.
[Mh] Termos MeSH primário: Proteínas de Bactérias/biossíntese
Expressão Gênica
Lactobacillus casei/genética
Lactococcus lactis/enzimologia
Transportadores de Ânions Orgânicos/biossíntese
[Mh] Termos MeSH secundário: Acetoína/metabolismo
Acetoína Desidrogenase/análise
Proteínas de Bactérias/genética
Ácido Cítrico/metabolismo
Clonagem Molecular
Meios de Cultura
DNA Helicases/genética
Diacetil/metabolismo
Vetores Genéticos
Concentração de Íons de Hidrogênio
Lactobacillus casei/metabolismo
Lactococcus lactis/genética
Metiltransferases/genética
Transportadores de Ânions Orgânicos/genética
Plasmídeos/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Culture Media); 0 (Organic Anion Transporters); 0 (Recombinant Proteins); 2968PHW8QP (Citric Acid); 77000-09-0 (citP protein, Lactococcus lactis); BG4D34CO2H (Acetoin); EC 1.1.1.- (Acetoin Dehydrogenase); EC 2.1.1.- (ErmTR protein, bacteria); EC 2.1.1.- (Methyltransferases); EC 3.6.4.- (DNA Helicases); K324J5K4HM (Diacetyl)
[Em] Mês de entrada:0706
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061202
[St] Status:MEDLINE


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[PMID]:17030441
[Au] Autor:van Bergen B; Strasser R; Cyr N; Sheppard JD; Jardim A
[Ad] Endereço:Department of Bioresource Engineering, Macdonald Campus of McGill University, 21 111 Lakeshore Road, Ste-Anne-de-Bellevue, Quebec, Canada H9X 3V9.
[Ti] Título:Alpha,beta-dicarbonyl reduction by Saccharomyces D-arabinose dehydrogenase.
[So] Source:Biochim Biophys Acta;1760(11):1636-45, 2006 Nov.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:An alpha,beta-dicarbonyl reductase activity was purified from Saccharomyces cerevisiae and identified as the cytosolic enzyme D-Arabinose dehydrogenase (ARA1) by MALDI-TOF/TOF. Size exclusion chromatography analysis of recombinant Ara1p revealed that this protein formed a homodimer. Ara1p catalyzed the reduction of the reactive alpha,beta-dicarbonyl compounds methylglyoxal, diacetyl, and pentanedione in a NADPH dependant manner. Ara1p had apparent Km values of approximately 14 mM, 7 mM and 4 mM for methylglyoxal, diacetyl and pentanedione respectively, with corresponding turnover rates of 4.4, 6.9 and 5.9 s(-1) at pH 7.0. pH profiling showed that Ara1p had a pH optimum of 4.5 for the diacetyl reduction reaction. Ara1p also catalyzed the NADP+ dependant oxidation of acetoin; however this back reaction only occurred at alkaline pH values. That Ara1p was important for degradation of alpha,beta-dicarbonyl substrates was further supported by the observation that ara1-Delta knockout yeast mutants exhibited a decreased growth rate phenotype in media containing diacetyl.
[Mh] Termos MeSH primário: Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/química
Proteínas de Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/enzimologia
Desidrogenase do Álcool de Açúcar/química
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/química
Acetoína Desidrogenase/isolamento & purificação
Sequência de Aminoácidos
Diacetil/química
Diacetil/metabolismo
Cinética
Espectrometria de Massas
Dados de Sequência Molecular
Oxirredução
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/genética
Oxirredutases Atuantes sobre Doadores de Grupos Aldeído ou Oxo/metabolismo
Aldeído Pirúvico/química
Aldeído Pirúvico/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
Desidrogenase do Álcool de Açúcar/genética
Desidrogenase do Álcool de Açúcar/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ara1 protein, S cerevisiae); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 722KLD7415 (Pyruvaldehyde); EC 1.1.- (Sugar Alcohol Dehydrogenases); EC 1.1.1.- (Acetoin Dehydrogenase); EC 1.1.1.116 (D-arabinose dehydrogenase); EC 1.2.- (Oxidoreductases Acting on Aldehyde or Oxo Group Donors); K324J5K4HM (Diacetyl)
[Em] Mês de entrada:0701
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:061013
[St] Status:MEDLINE


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[PMID]:15548307
[Au] Autor:Ui S; Takusagawa Y; Sato T; Ohtsuki T; Mimura A; Ohkuma M; Kudo T
[Ad] Endereço:Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Yamanashi University, Kofu, Yamanashi, Japan. ui@ab11.yamanashi.ac.jp
[Ti] Título:Production of L-2,3-butanediol by a new pathway constructed in Escherichia coli.
[So] Source:Lett Appl Microbiol;39(6):533-7, 2004.
[Is] ISSN:0266-8254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: A metabolic pathway for L-2,3-butanediol (BD) as the main product has not yet been found. To rectify this situation, we attempted to produce L-BD from diacetyl (DA) by producing simultaneous expression of diacetyl reductase (DAR) and L-2,3-butanediol dehydrogenase (BDH) using transgenic bacteria, Escherichia coli JM109/pBUD-comb. METHODS AND RESULTS: The meso-BDH of Klebsiella pneumoniae was used for its DAR activity to convert DA to L-acetoin (AC) and the L-BDH of Brevibacterium saccharolyticum was used to reduce L-AC to L-BD. The respective gene coding each enzyme was connected in tandem to the MCS of pFLAG-CTC (pBUD-comb). The divided addition of DA as a source, addition of 2% glucose, and the combination of static and shaking culture was effective for the production. CONCLUSIONS: L-BD (2200 mg l(-1)) was generated from 3000 mg l(-1) added of DA, which corresponded to a 73% conversion rate. Meso-BD as a by-product was mixed by 2% at most. SIGNIFICANCE AND IMPACT OF THE STUDY: An enzyme system for converting DA to L-BD was constructed with a view to using DA-producing bacteria in the future.
[Mh] Termos MeSH primário: Butileno Glicóis/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
[Mh] Termos MeSH secundário: Acetoína Desidrogenase/genética
Acetoína Desidrogenase/metabolismo
Oxirredutases do Álcool/genética
Oxirredutases do Álcool/metabolismo
Proteínas de Bactérias/genética
Brevibacterium/enzimologia
Brevibacterium/genética
Clonagem Molecular
Diacetil/metabolismo
Fermentação
Vetores Genéticos
Cinética
Klebsiella pneumoniae/enzimologia
Klebsiella pneumoniae/genética
Plasmídeos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Estereoisomerismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Butylene Glycols); 0 (Recombinant Proteins); 45427ZB5IJ (2,3-butylene glycol); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (Acetoin Dehydrogenase); EC 1.1.1.4 (butanediol dehydrogenase); K324J5K4HM (Diacetyl)
[Em] Mês de entrada:0501
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:041119
[St] Status:MEDLINE


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[PMID]:12514009
[Au] Autor:Rattray FP; Myling-Petersen D; Larsen D; Nilsson D
[Ad] Endereço:Department of Genomics and Strain Development, Chr. Hansen A/S., DK-2970 Hørsholm, Denmark. FergalPatrick.Rattray@dk.chr-hansen.com
[Ti] Título:Plasmid-encoded diacetyl (acetoin) reductase in Leuconostoc pseudomesenteroides.
[So] Source:Appl Environ Microbiol;69(1):304-11, 2003 Jan.
[Is] ISSN:0099-2240
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A plasmid-borne diacetyl (acetoin) reductase (butA) from Leuconostoc pseudomesenteroides CHCC2114 was sequenced and cloned. Nucleotide sequence analysis revealed an open reading frame encoding a protein of 257 amino acids which had high identity at the amino acid level to diacetyl (acetoin) reductases reported previously. Downstream of the butA gene of L. pseudomesenteroides, but coding in the opposite orientation, a putative DNA recombinase was identified. A two-step PCR approach was used to construct FPR02, a butA mutant of the wild-type strain, CHCC2114. FPR02 had significantly reduced diacetyl (acetoin) reductase activity with NADH as coenzyme, but not with NADPH as coenzyme, suggesting the presence of another diacetyl (acetoin)-reducing activity in L. pseudomesenteroides. Plasmid-curing experiments demonstrated that the butA gene is carried on a 20-kb plasmid in L. pseudomesenteroides.
[Mh] Termos MeSH primário: Acetoína Desidrogenase/genética
Acetoína Desidrogenase/metabolismo
Leuconostoc/enzimologia
Plasmídeos/genética
[Mh] Termos MeSH secundário: Clonagem Molecular
Escherichia coli/enzimologia
Escherichia coli/genética
Deleção de Genes
Leuconostoc/genética
Dados de Sequência Molecular
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.1.- (Acetoin Dehydrogenase)
[Em] Mês de entrada:0303
[Cu] Atualização por classe:170219
[Lr] Data última revisão:
170219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030107
[St] Status:MEDLINE



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