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Pesquisa : D08.811.913.400.725.200 [Categoria DeCS]
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[PMID]:28092443
[Au] Autor:Stroek R; Ge Y; Talbot PD; Glok MK; Bernas KE; Thomson CM; Gould ER; Alphey MS; Liu H; Florence GJ; Naismith JH; da Silva RG
[Ad] Endereço:School of Engineering and Applied Science, Rotterdam University of Applied Science , G. J. de Jonghweg 4-6, 3015 GG Rotterdam, The Netherlands.
[Ti] Título:Kinetics and Structure of a Cold-Adapted Hetero-Octameric ATP Phosphoribosyltransferase.
[So] Source:Biochemistry;56(5):793-803, 2017 Feb 07.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Adenosine 5'-triphosphate phosphoribosyltransferase (ATPPRT) catalyzes the first step in histidine biosynthesis, the condensation of ATP and 5-phospho-α-d-ribosyl-1-pyrophosphate to generate N -(5-phospho-ß-d-ribosyl)-ATP and inorganic pyrophosphate. The enzyme is allosterically inhibited by histidine. Two forms of ATPPRT, encoded by the hisG gene, exist in nature, depending on the species. The long form, HisG , is a single polypeptide chain with catalytic and regulatory domains. The short form, HisG , lacks a regulatory domain and cannot bind histidine. HisG instead is found in complex with a regulatory protein, HisZ, constituting the ATPPRT holoenzyme. HisZ triggers HisG catalytic activity while rendering it sensitive to allosteric inhibition by histidine. Until recently, HisG was thought to be catalytically inactive without HisZ. Here, recombinant HisG and HisZ from the psychrophilic bacterium Psychrobacter arcticus were independently overexpressed and purified. The crystal structure of P. arcticus ATPPRT was determined at 2.34 Å resolution, revealing an equimolar HisG -HisZ hetero-octamer. Steady-state kinetics indicate that both the ATPPRT holoenzyme and HisG are catalytically active. Surprisingly, HisZ confers only a modest 2-4-fold increase in k . Reaction profiles for both enzymes cannot be distinguished by P nuclear magnetic resonance, indicating that the same reaction is catalyzed. The temperature dependence of k shows deviation from Arrhenius behavior at 308 K with the holoenzyme. Interestingly, such deviation is detected only at 313 K with HisG . Thermal denaturation by CD spectroscopy resulted in T 's of 312 and 316 K for HisZ and HisG , respectively, suggesting that HisZ renders the ATPPRT complex more thermolabile. This is the first characterization of a psychrophilic ATPPRT.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/química
Aminoacil-tRNA Sintetases/química
Proteínas de Bactérias/química
Histidina/química
Proteínas de Transporte de Monossacarídeos/química
Psychrobacter/enzimologia
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/genética
ATP Fosforribosiltransferase/metabolismo
Aclimatação
Trifosfato de Adenosina/análogos & derivados
Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Regulação Alostérica
Aminoacil-tRNA Sintetases/genética
Aminoacil-tRNA Sintetases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Temperatura Baixa
Cristalografia por Raios X
Difosfatos/química
Difosfatos/metabolismo
Estabilidade Enzimática
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Histidina/biossíntese
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
Modelos Moleculares
Proteínas de Transporte de Monossacarídeos/genética
Proteínas de Transporte de Monossacarídeos/metabolismo
Fosforribosil Pirofosfato/química
Fosforribosil Pirofosfato/metabolismo
Domínios Proteicos
Multimerização Proteica
Estrutura Secundária de Proteína
Psychrobacter/genética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Diphosphates); 0 (HisG protein, bacteria); 0 (Isoenzymes); 0 (Monosaccharide Transport Proteins); 0 (Recombinant Proteins); 1110-99-2 (phosphoribosyladenosine triphosphate); 4E862E7GRQ (diphosphoric acid); 4QD397987E (Histidine); 7540-64-9 (Phosphoribosyl Pyrophosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.4.2.17 (ATP Phosphoribosyltransferase); EC 6.1.1.- (Amino Acyl-tRNA Synthetases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01138


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[PMID]:27393206
[Au] Autor:Livingstone EK; Mittelstädt G; Given FM; Parker EJ
[Ad] Endereço:Department of Chemistry and Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand.
[Ti] Título:Independent catalysis of the short form HisG from Lactococcus lactis.
[So] Source:FEBS Lett;590(16):2603-10, 2016 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ATP-phosphoribosyltransferase (ATP-PRT) catalyses the first step of histidine biosynthesis. Two different forms of ATP-PRT have been described; the homo-hexameric long form, and the hetero-octameric short form. Lactococcus lactis possesses the short form ATP-PRT comprising four subunits of HisGS , the catalytic subunit, and four subunits of HisZ, a histidyl-tRNA synthetase paralogue. Previous studies have suggested that HisGS requires HisZ for catalysis. Here, we reveal that the dimeric HisGS does display ATP-PRT activity in the absence of HisZ. This result reflects the evolutionary relationship between the long and short form ATP-PRT, which acquired allosteric inhibition and enhanced catalysis via two divergent strategies.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/metabolismo
Aminoacil-tRNA Sintetases/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Isoformas de Proteínas/metabolismo
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/química
ATP Fosforribosiltransferase/genética
Sequência de Aminoácidos
Aminoacil-tRNA Sintetases/química
Aminoacil-tRNA Sintetases/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Catálise
Domínio Catalítico/genética
Histidina/química
Histidina/metabolismo
Lactococcus lactis/enzimologia
Proteínas de Transporte de Monossacarídeos/química
Proteínas de Transporte de Monossacarídeos/genética
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (HisG protein, bacteria); 0 (Monosaccharide Transport Proteins); 0 (Protein Isoforms); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase); EC 6.1.1.- (Amino Acyl-tRNA Synthetases); EC 6.1.1.- (HisZ protein, Lactococcus lactis)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160710
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12277


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[PMID]:27191057
[Au] Autor:Mittelstädt G; Moggré GJ; Panjikar S; Nazmi AR; Parker EJ
[Ad] Endereço:Maurice Wilkins Centre, Biomolecular Interaction Centre, Christchurch, 8140, New Zealand.
[Ti] Título:Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail.
[So] Source:Protein Sci;25(8):1492-506, 2016 08.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogenic ε-proteobacteria Campylobacter jejuni (CjeATP-PRT). This enzyme is a member of the long form (HisGL ) ATP-PRT and is allosterically inhibited by histidine, which binds to a remote regulatory domain, and competitively inhibited by AMP. In the crystalline form, CjeATP-PRT was found to adopt two distinctly different hexameric conformations, with an open homohexameric structure observed in the presence of substrate ATP, and a more compact closed form present when inhibitor histidine is bound. CjeATP-PRT was observed to adopt only a hexameric quaternary structure in solution, contradicting previous hypotheses favoring an allosteric mechanism driven by an oligomer equilibrium. Instead, this study supports the conclusion that the ATP-PRT long form hexamer is the active species; the tightening of this structure in response to remote histidine binding results in an inhibited enzyme.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/química
Monofosfato de Adenosina/química
Trifosfato de Adenosina/química
Proteínas de Bactérias/química
Campylobacter jejuni/química
Histidina/química
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/genética
ATP Fosforribosiltransferase/metabolismo
Regulação Alostérica
Sítio Alostérico
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Ligação Competitiva
Campylobacter jejuni/enzimologia
Campylobacter jejuni/genética
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Cinética
Modelos Moleculares
Mutação
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 415SHH325A (Adenosine Monophosphate); 4QD397987E (Histidine); 8L70Q75FXE (Adenosine Triphosphate); EC 2.4.2.17 (ATP Phosphoribosyltransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE
[do] DOI:10.1002/pro.2948


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[PMID]:25892668
[Au] Autor:Kulis-Horn RK; Persicke M; Kalinowski J
[Ad] Endereço:Microbial Genomics and Biotechnology, Center for Biotechnology, Bielefeld University, Universitätsstraße 27, 33615 Bielefeld, Germany.
[Ti] Título:Corynebacterium glutamicum ATP-phosphoribosyl transferases suitable for L-histidine production--Strategies for the elimination of feedback inhibition.
[So] Source:J Biotechnol;206:26-37, 2015 Jul 20.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:L-Histidine biosynthesis in Corynebacterium glutamicum is mainly regulated by L-histidine feedback inhibition of the ATP-phosphoribosyltransferase HisG that catalyzes the first step of the pathway. The elimination of this feedback inhibition is the first and most important step in the development of an L-histidine production strain. For this purpose, a combined approach of random mutagenesis and rational enzyme redesign was performed. Mutants spontaneously resistant to the toxic L-histidine analog ß-(2-thiazolyl)-DL-alanine (2-TA) revealed novel and unpredicted mutations in the C-terminal regulatory domain of HisG resulting in increased feedback resistance. Moreover, deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain resulted in a HisG variant that is still highly active even at L-histidine concentrations close to the solubility limit. Notably, the S143F mutation on its own provokes feedback deregulation, revealing for the first time an amino acid residue in the catalytic domain of HisG that is involved in the feedback regulatory mechanism. In addition, we investigated the effect of hisG mutations for L-histidine production on different levels. This comprised the analysis of different expression systems, including plasmid- and chromosome-based overexpression, as well as the importance of codon choice for HisG mutations. The combination of domain deletions, single amino acid exchanges, codon choice, and chromosome-based overexpression resulted in production strains accumulating around 0.5 g l(-1) L-histidine, demonstrating the added value of the different approaches.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/metabolismo
Corynebacterium glutamicum/genética
Retroalimentação Fisiológica/fisiologia
Histidina/metabolismo
Engenharia Metabólica/métodos
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/química
ATP Fosforribosiltransferase/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Corynebacterium glutamicum/enzimologia
Escherichia coli/genética
Redes e Vias Metabólicas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Mutação Silenciosa/genética
Mutação Silenciosa/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150525
[Lr] Data última revisão:
150525
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150421
[St] Status:MEDLINE


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[PMID]:23829416
[Au] Autor:Schendzielorz G; Dippong M; Grünberger A; Kohlheyer D; Yoshida A; Binder S; Nishiyama C; Nishiyama M; Bott M; Eggeling L
[Ad] Endereço:Institute of Bio- and Geosciences 1: Biotechnology, Forschungszentrum Jülich , D-52428 Jülich, Germany.
[Ti] Título:Taking control over control: use of product sensing in single cells to remove flux control at key enzymes in biosynthesis pathways.
[So] Source:ACS Synth Biol;3(1):21-9, 2014 Jan 17.
[Is] ISSN:2161-5063
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Enzymes initiating the biosynthesis of cellular building blocks are frequently inhibited by the end-product of the respective pathway. Here we present an approach to rapidly generate sets of enzymes overriding this control. It is based on the in vivo detection of the desired end-product in single cells using a genetically encoded sensor. The sensor transmits intracellular product concentrations into a graded optical output, thus enabling ultrahigh-throughput screens by FACS. We randomly mutagenized plasmid-encoded ArgB of Corynebacterium glutamicum and screened the library in a strain carrying the sensor pSenLys-Spc, which detects l-lysine, l-arginine and l-histidine. Six of the resulting N-acetyl-l-glutamate kinase proteins were further developed and characterized and found to be at least 20-fold less sensitive toward l-arginine inhibition than the wild-type enzyme. Overexpression of the mutein ArgB-K47H-V65A in C. glutamicumΔargR led to the accumulation of 34 mM l-arginine in the culture medium. We also screened mutant libraries of lysC-encoded aspartate kinase and hisG-encoded ATP phosphoribosyltransferase. We isolated 11 LysC muteins, enabling up to 45 mM l-lysine accumulation, and 13 HisG muteins, enabling up to 17 mM l-histidine accumulation. These results demonstrate that in vivo screening of enzyme libraries by using metabolite sensors is extremely well suited to identify high-performance muteins required for overproduction.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Corynebacterium glutamicum/metabolismo
Fosfotransferases (Aceptor do Grupo Carboxila)/metabolismo
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/genética
ATP Fosforribosiltransferase/metabolismo
Substituição de Aminoácidos
Arginina/química
Arginina/metabolismo
Aspartato Quinase/genética
Aspartato Quinase/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Corynebacterium glutamicum/enzimologia
Citometria de Fluxo
Histidina/química
Histidina/metabolismo
Cinética
Lisina/química
Lisina/metabolismo
Fosfotransferases (Aceptor do Grupo Carboxila)/química
Fosfotransferases (Aceptor do Grupo Carboxila)/genética
Plasmídeos/genética
Plasmídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 4QD397987E (Histidine); 94ZLA3W45F (Arginine); EC 2.4.2.17 (ATP Phosphoribosyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.4 (Aspartate Kinase); EC 2.7.2.8 (acetylglutamate kinase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:140808
[Lr] Data última revisão:
140808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130709
[St] Status:MEDLINE
[do] DOI:10.1021/sb400059y


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[PMID]:24111909
[Au] Autor:Lunardi J; Nunes JE; Bizarro CV; Basso LA; Santos DS; Machado P
[Ad] Endereço:Instituto Nacional de Ciência e Tecnologia em Tuberculose (INCT-TB), Centro de Pesquisas em Biologia Molecular e Funcional (CPBMF), Pontifícia Universidade Católica do Rio Grande do Sul (PUCRS), 90619-900, Porto Alegre, RS, Brazil. pablo.machado@pucrs.br.
[Ti] Título:Targeting the histidine pathway in Mycobacterium tuberculosis.
[So] Source:Curr Top Med Chem;13(22):2866-84, 2013.
[Is] ISSN:1873-4294
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Worldwide, tuberculosis is the leading cause of morbidity and mortality due to a single bacterial pathogen, Mycobacterium tuberculosis (Mtb). The increasing prevalence of this disease, the emergence of multi-, extensively, and totally drug-resistant strains, complicated by co-infection with the human immunodeficiency virus, and the length of tuberculosis chemotherapy have led to an urgent and continued need for the development of new and more effective antitubercular drugs. Within this context, the L-histidine biosynthetic pathway, which converts 5-phosphoribosyl 1-pyrophosphate to L-histidine in ten enzymatic steps, has been reported as a promising target of antimicrobial agents. This pathway is found in bacteria, archaebacteria, lower eukaryotes, and plants but is absent in mammals, making these enzymes highly attractive targets for the drug design of new antimycobacterial compounds with selective toxicity. Moreover, the biosynthesis of L-histidine has been described as essential for Mtb growth in vitro. Accordingly, a comprehensive overview of Mycobacterium tuberculosis histidine pathway enzymes as attractive targets for the development of new antimycobacterial agents is provided, mainly summarizing the previously reported inhibition data for Mtb or orthologous proteins.
[Mh] Termos MeSH primário: Antituberculosos/química
Antituberculosos/farmacologia
Enzimas/metabolismo
Histidina/metabolismo
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/metabolismo
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/química
ATP Fosforribosiltransferase/genética
ATP Fosforribosiltransferase/metabolismo
Aldose-Cetose Isomerases/genética
Aldose-Cetose Isomerases/metabolismo
Aminoidrolases/genética
Aminoidrolases/metabolismo
Desenho de Drogas
Enzimas/genética
Terapia de Alvo Molecular
Mycobacterium tuberculosis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Antitubercular Agents); 0 (Enzymes); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase); EC 3.5.1.- (imidazole glycerol phosphate synthase); EC 3.5.4.- (Aminohydrolases); EC 5.3.1.- (Aldose-Ketose Isomerases)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:131125
[Lr] Data última revisão:
131125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131012
[St] Status:MEDLINE


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[PMID]:23795473
[Au] Autor:Doroshenko VG; Lobanov AO; Fedorina EA
[Ti] Título:[The directed modification of Escherichia coli MG1655 to obtain histidine-producing mutants].
[So] Source:Prikl Biokhim Mikrobiol;49(2):149-54, 2013 Mar-Apr.
[Is] ISSN:0555-1099
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Strain MG 1655+hisGr hisL'-Delta, purR, which produces histidine with a weight yield of approximately 12% from glucose, was constructed through directed chromosomal modifications of the laboratory Escherichia coli strain MG 1655+, which has a known genome sequence. A feedback-resistant ATP-phosphoribosyl transferase encoded by the mutant hisGr (E271 K) was the main determinant of histidine production. A further increase in histidine production was achieved by the expression enhance of a mutant his operon containing hisGr through the deleting attenuator region (hisL'-Delta). An increase in the expression of the wildtype his operon did not result in histidine accumulation. Deletion of the transcriptional regulator gene purR increased the biomass produced and maintained the level of histidine production per cell under the fermentation conditions used.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/genética
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Histidina/biossíntese
Proteoma/genética
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/metabolismo
Sequência de Bases
Biomassa
Escherichia coli/crescimento & desenvolvimento
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Fermentação
Glucose/metabolismo
Engenharia Metabólica
Dados de Sequência Molecular
Mutação
Óperon
Proteoma/metabolismo
Proteínas Repressoras/deficiência
Proteínas Repressoras/genética
Deleção de Sequência
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Proteome); 0 (PurR protein, E coli); 0 (Repressor Proteins); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130626
[St] Status:MEDLINE


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[PMID]:23355034
[Au] Autor:Cheng Y; Zhou Y; Yang L; Zhang C; Xu Q; Xie X; Chen N
[Ad] Endereço:College of Biotechnology, Tianjin University of Science & Technology, Key Laboratory of Industrial Microbiology of Education Ministry, Tianjin 300457, China.
[Ti] Título:Modification of histidine biosynthesis pathway genes and the impact on production of L-histidine in Corynebacterium glutamicum.
[So] Source:Biotechnol Lett;35(5):735-41, 2013 May.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Histidine biosynthesis in Corynebacterium glutamicum is regulated not only by feedback inhibition by the first enzyme in the pathway, but also by repression control of the synthesis of the histidine enzymes. C. glutamicum histidine genes are located and transcribed in two unlinked loci, hisEG and hisDCB-orf1-orf2-hisHA-impA-hisFI. We constructed plasmid pK18hisDPtac to replace the native hisD promoter with the tac promoter, and overexpressed phosphoribosyl-ATP-pyrophosphohydrolase, encoded by hisE, and ATP-phosphoribosyltransferase, encoded by hisG. The L-histidine titer at 0.85 g l(-1) was 80 % greater in the transformed bacterium and production of byproducts, L-alanine and L-tryptophan, was significantly decreased. However, accumulation of glutamic acid increased by 58 % (2.8 g l(-1)). This study represents the first attempt to substitute the histidine biosynthesis pathway promoter in the chromosome with a stronger promoter to increase histidine production.
[Mh] Termos MeSH primário: Corynebacterium glutamicum/genética
Corynebacterium glutamicum/metabolismo
Histidina/biossíntese
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/genética
ATP Fosforribosiltransferase/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biotecnologia
Corynebacterium glutamicum/enzimologia
Fermentação
Histidina/genética
Redes e Vias Metabólicas
Plasmídeos/genética
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130129
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-013-1138-1


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[PMID]:22989207
[Au] Autor:Pedreño S; Pisco JP; Larrouy-Maumus G; Kelly G; de Carvalho LP
[Ad] Endereço:Mycobacterial Research Division, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
[Ti] Título:Mechanism of feedback allosteric inhibition of ATP phosphoribosyltransferase.
[So] Source:Biochemistry;51(40):8027-38, 2012 Oct 09.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MtATP-phosphoribosyltransferase catalyzes the first and committed step in l-histidine biosynthesis in Mycobacterium tuberculosis and is therefore subjected to allosteric feedback regulation. Because of its essentiality, this enzyme is being studied as a potential target for novel anti-infectives. To understand the basis for its regulation, we characterized the allosteric inhibition using gel filtration, steady-state and pre-steady-state kinetics, and the pH dependence of inhibition and binding. Gel filtration experiments indicate that MtATP-phosphoribosyltransferase is a hexamer in solution, in the presence or absence of l-histidine. Steady-state kinetic studies demonstrate that l-histidine inhibition is uncompetitive versus ATP and noncompetitive versus PRPP. At pH values close to neutrality, a K(ii) value of 4 µM was obtained for l-histidine. Pre-steady-state kinetic experiments indicate that chemistry is not rate-limiting for the overall reaction and that l-histidine inhibition is caused by trapping the enzyme in an inactive conformation. The pH dependence of binding, obtained by nuclear magnetic resonance, indicates that l-histidine binds better as the neutral α-amino group. The pH dependence of inhibition (K(ii)), on the contrary, indicates that l-histidine better inhibits MtATP-phosphoribosytransferase with a neutral imidazole and an ionized α-amino group. These results are combined into a model that accounts for the allosteric inhibition of MtATP-phosphoribosyltransferase.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/antagonistas & inibidores
Retroalimentação Fisiológica/fisiologia
Regulação Enzimológica da Expressão Gênica/fisiologia
Mycobacterium tuberculosis/enzimologia
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Histidina/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Estrutura Molecular
Mycobacterium tuberculosis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120920
[St] Status:MEDLINE
[do] DOI:10.1021/bi300808b


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[PMID]:22172596
[Au] Autor:Zhang Y; Shang X; Deng A; Chai X; Lai S; Zhang G; Wen T
[Ad] Endereço:Department of Industrial Microbiology and Biotechnology, Institute of Microbiology, Chinese Academy of Sciences, 100101 Beijing, China.
[Ti] Título:Genetic and biochemical characterization of Corynebacterium glutamicum ATP phosphoribosyltransferase and its three mutants resistant to feedback inhibition by histidine.
[So] Source:Biochimie;94(3):829-38, 2012 Mar.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:ATP phosphoribosyltransferase (ATP-PRT) catalyzes the condensation of ATP and PRPP at the first step of histidine biosynthesis and is regulated by a feedback inhibition from product histidine. Here, we report the genetic and biochemical characterization of such an enzyme, HisG(Cg), from Corynebacterium glutamicum, including site-directed mutagenesis of the histidine-binding site for the first time. Gene disruption and complementation experiments showed that HisG(Cg) is essential for histidine biosynthesis. HisG(Cg) activity was noncompetitively inhibited by histidine and the α-amino group of histidine were found to play an important role for its binding to HisG(Cg). Homology-based modeling predicted that four residues (N215, L231, T235 and A270) in the C-terminal domain of HisG(Cg) may affect the histidine inhibition. Mutating these residues in HisG(Cg) did not cause significant change in the specific activities of the enzyme but resulted in the generation of mutant ones resistant to histidine inhibition. Our data identified that the mutant N215K/L231F/T235A resists to histidine inhibition the most with 37-fold increase in K(i) value. As expected, overexpressing a hisG(Cg) gene containing N215K/L231F/T235A mutations in vivo promoted histidine accumulation to a final concentration of 0.15 ± 0.01 mM. Our results demonstrated that the polarity change of electrostatic potential of mutant protein surface prevents histidine from binding to the C-terminal domain of HisG(Cg), resulting in the release of allosteric inhibition. Considering that these residues were highly conserved in ATP-PRTs from different genera of Gram-positive bacteria the mechanism by histidine inhibition as exhibited in Corynebacterium glutamicum probably represents a ubiquitously inhibitory mechanism of ATP-PRTs by histidine.
[Mh] Termos MeSH primário: ATP Fosforribosiltransferase/metabolismo
Corynebacterium glutamicum/enzimologia
Histidina/metabolismo
Proteínas Mutantes/metabolismo
[Mh] Termos MeSH secundário: ATP Fosforribosiltransferase/genética
Mutagênese Sítio-Dirigida
Proteínas Mutantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mutant Proteins); 4QD397987E (Histidine); EC 2.4.2.17 (ATP Phosphoribosyltransferase)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111217
[St] Status:MEDLINE
[do] DOI:10.1016/j.biochi.2011.11.015



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