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[PMID]:27988856
[Au] Autor:Patel AT; Akhani RC; Patel MJ; Dedania SR; Patel DH
[Ad] Endereço:Department of Biochemistry, P. D. Patel Institute of Applied Sciences, CHARUSAT, Changa, 388421, Gujarat, India.
[Ti] Título:Bioproduction of L-Aspartic Acid and Cinnamic Acid by L-Aspartate Ammonia Lyase from Pseudomonas aeruginosa PAO1.
[So] Source:Appl Biochem Biotechnol;182(2):792-803, 2017 Jun.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aspartase (L-aspartate ammonia lyase, EC 4.3.1.1) catalyses the reversible amination and deamination of L-aspartic acid to fumaric acid which can be used to produce important biochemical. In this study, we have explored the characteristics of aspartase from Pseudomonas aeruginosa PAO1 (PA-AspA). To overproduce PA-AspA, the 1425-bp gene was introduced in Escherichia coli BL21 and purified. A 51.0-kDa protein was observed as a homogenous purified protein on SDS-PAGE. The enzyme was optimally active at pH 8.0 and 35 °C. PA-AspA has retained 56% activity after 7 days of incubation at 35 °C, which displays the hyperthermostablility characteristics of the enzyme. PA-AspA is activated in the presence of metal ions and Mg2+ is found to be most effective. Among the substrates tested for specificity of PA-AspA, L-phenylalanine (38.35 ± 2.68) showed the highest specific activity followed by L-aspartic acid (31.21 ± 3.31) and fumarate (5.42 ± 2.94). K values for L-phenylalanine, L-aspartic acid and fumarate were 1.71 mM, 0.346 µM and 2 M, respectively. The catalytic efficiency (k /K ) for L-aspartic acid (14.18 s mM ) was higher than that for L-phenylalanine (4.65 s mM ). For bioconversion, from an initial concentration of 1000 mM of fumarate and 30 mM of L-phenylalanine, PA-AspA was found to convert 395.31 µM L-aspartic acid and 3.47 mM cinnamic acid, respectively.
[Mh] Termos MeSH primário: Aspartato Amônia-Liase/química
Ácido Aspártico/química
Proteínas de Bactérias/química
Cinamatos/química
Pseudomonas aeruginosa/enzimologia
[Mh] Termos MeSH secundário: Temperatura Alta
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cinnamates); 30KYC7MIAI (Aspartic Acid); EC 4.3.1.1 (Aspartate Ammonia-Lyase); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161219
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2362-7


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[PMID]:26777068
[Au] Autor:Hahlbrock A; Goesswein D; Künzel J; Wünsch D; Stauber RH
[Ad] Endereço:ENT Department, Molecular and Cellular Oncology, University Hospital of Mainz, Mainz, Germany. Electronic address: angelinahahlbrock@uni-mainz.de.
[Ti] Título:Threonine Aspartase1: An unexplored protease with relevance for oral oncology?
[So] Source:Oral Oncol;54:e10-2, 2016 Mar.
[Is] ISSN:1879-0593
[Cp] País de publicação:England
[La] Idioma:eng
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/enzimologia
Endopeptidases/metabolismo
Neoplasias Bucais/enzimologia
[Mh] Termos MeSH secundário: Aspartato Amônia-Liase/genética
Aspartato Amônia-Liase/metabolismo
Endopeptidases/genética
Seres Humanos
Treonina/genética
Treonina/metabolismo
[Pt] Tipo de publicação:LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
2ZD004190S (Threonine); EC 3.4.- (Endopeptidases); EC 3.4.22.- (taspase1, human); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160119
[St] Status:MEDLINE


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[PMID]:26657154
[Au] Autor:Wünsch D; Hahlbrock A; Jung S; Schirmeister T; van den Boom J; Schilling O; Knauer SK; Stauber RH
[Ad] Endereço:Molecular and Cellular Oncology, ENT/University Medical Center of Mainz, Mainz, Germany.
[Ti] Título:Taspase1: a 'misunderstood' protease with translational cancer relevance.
[So] Source:Oncogene;35(26):3351-64, 2016 Jun 30.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proteolysis is not only a critical requirement for life, but the executing enzymes also play important roles in numerous pathological conditions, including cancer. Therefore, targeting proteases is clearly relevant for improving cancer patient care. However, to effectively control proteases, a profound knowledge of their mechanistic function as well as their regulation and downstream signalling in health and disease is required. The highly conserved protease Threonine Aspartase1 (Taspase1) is overexpressed in numerous liquid and solid malignancies and was characterized as a 'non-oncogene addiction' protease. Although Taspase1 was shown to cleave various regulatory proteins in humans as well as leukaemia provoking mixed lineage leukaemia fusions, our knowledge on its detailed functions and the underlying mechanisms contributing to cancer is still incomplete. Despite superficial similarity to type 2 asparaginases as well as Ntn proteases, such as the proteasome, Taspase1-related research so far gives us the picture of a unique protease exhibiting special features. Moreover, neither effective genetic nor chemical inhibitors for this enzyme are available so far, thus hampering not only to further dissect Taspase1's pathobiological functions but also precluding the assessment of its clinical impact. Based on recent insights, we here critically review the current knowledge of Taspase1's structure-function relationship and its mechanistic relevance for tumorigenesis obtained from in vitro and in vivo cancer models. We provide a comprehensive overview of tumour entities for which Taspase1 might be of predictive and therapeutic value, and present the respective experimental evidence. To stimulate progress in the field, a comprehensive overview of Taspase1 targeting approaches is presented, including coverage of Taspase1-related patents. We conclude by discussing future inhibition strategies and relevant challenges, which need to be resolved by the field.
[Mh] Termos MeSH primário: Aspartato Amônia-Liase/metabolismo
Endopeptidases/metabolismo
Neoplasias/enzimologia
Treonina/metabolismo
Pesquisa Médica Translacional/métodos
[Mh] Termos MeSH secundário: Aspartato Amônia-Liase/antagonistas & inibidores
Aspartato Amônia-Liase/genética
Endopeptidases/genética
Inibidores Enzimáticos/química
Inibidores Enzimáticos/uso terapêutico
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Estrutura Molecular
Neoplasias/genética
Neoplasias/prevenção & controle
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 2ZD004190S (Threonine); EC 3.4.- (Endopeptidases); EC 3.4.22.- (taspase1, human); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2015.436


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[PMID]:26254042
[Au] Autor:Tajima T; Hamada M; Nakashimada Y; Kato J
[Ad] Endereço:Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1, Kagamiyama, Higashi-Hiroshima, 739-8530, Japan. ttajima@hiroshima-u.ac.jp.
[Ti] Título:Efficient aspartic acid production by a psychrophile-based simple biocatalyst.
[So] Source:J Ind Microbiol Biotechnol;42(10):1319-24, 2015 Oct.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We previously constructed a Psychrophile-based Simple bioCatalyst (PSCat) reaction system, in which psychrophilic metabolic enzymes are inactivated by heat treatment, and used it here to study the conversion of aspartic acid from fumaric acid mediated by the activity of aspartate ammonia-lyase (aspartase). In Escherichia coli, the biosynthesis of aspartic acid competes with that of L-malic acid produced from fumaric acid by fumarase. In this study, E. coli aspartase was expressed in psychrophilic Shewanella livingstonensis Ac10 heat treated at 50 °C for 15 min. The resultant PSCat could convert fumaric acid to aspartic acid without the formation of L-malic acid because of heat inactivation of psychrophilic fumarase activity. Furthermore, alginate-immobilized PSCat produced high yields of aspartic acid and could be re-used nine times. The results of our study suggest that PSCat can be applied in biotechnological production as a new approach to increase the yield of target compounds.
[Mh] Termos MeSH primário: Ácido Aspártico/biossíntese
Biocatálise
Shewanella/metabolismo
[Mh] Termos MeSH secundário: Aspartato Amônia-Liase/metabolismo
Biotecnologia/métodos
Estabilidade Enzimática
Reutilização de Equipamento
Escherichia coli/enzimologia
Escherichia coli/metabolismo
Fumarato Hidratase/metabolismo
Fumaratos/metabolismo
Temperatura Alta
Malatos/metabolismo
Shewanella/enzimologia
Shewanella/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fumarates); 0 (Malates); 30KYC7MIAI (Aspartic Acid); 817L1N4CKP (malic acid); 88XHZ13131 (fumaric acid); EC 4.2.1.2 (Fumarate Hydratase); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150809
[St] Status:MEDLINE
[do] DOI:10.1007/s10295-015-1669-7


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[PMID]:25386411
[Au] Autor:Wilharm G; Heider C
[Ad] Endereço:Project Group P2, Robert Koch-Institute Wernigerode, Germany.
[Ti] Título:Interrelationship between type three secretion system and metabolism in pathogenic bacteria.
[So] Source:Front Cell Infect Microbiol;4:150, 2014.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Before the advent of molecular biology methods, studies of pathogens were dominated by analyses of their metabolism. Development of molecular biology techniques then enabled the identification and functional characterisation of the fascinating toolbox of virulence factors. Increasing, genomic and proteomic approaches form the basis for a more systemic view on pathogens' functions in the context of infection. Re-emerging interest in the metabolism of pathogens and hosts further expands our view of infections. There is increasing evidence that virulence functions and metabolism of pathogens are extremely intertwined. Type three secretion systems (T3SSs) are major virulence determinants of many Gram-negative pathogens and it is the objective of this review to illustrate the intertwined relationship between T3SSs and the metabolism of the pathogens deploying them.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Fenômenos Fisiológicos Bacterianos
Sistemas de Secreção Bacterianos
Interações Hospedeiro-Patógeno
[Mh] Termos MeSH secundário: Aspartato Amônia-Liase/metabolismo
Bactérias/genética
Bactérias/patogenicidade
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Catálise
Ácidos Graxos/metabolismo
Plasmídeos/genética
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacterial Secretion Systems); 0 (Fatty Acids); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141112
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2014.00150


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[PMID]:24875395
[Au] Autor:Zhang J; Liu Y
[Ad] Endereço:Key Laboratory of Inorganic Chemistry in Universities of Shandong (Jining University), Qufu, Shandong 273155, China; Northwest Institute of Plateau Biology, Chinese Academy of Sciences, Xining, Qinghai 810001, China.
[Ti] Título:A QM/MM study of the catalytic mechanism of aspartate ammonia lyase.
[So] Source:J Mol Graph Model;51:113-9, 2014 Jun.
[Is] ISSN:1873-4243
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aspartate ammonia lyase (Asp) is one of three types of ammonia lyases specific for aspartate or its derivatives as substrates, which catalyzes the reversible reaction of l-aspartate to yield fumarate and ammonia. In this paper, the catalytic mechanism of Asp has been studied by using combined quantum-mechanical/molecular-mechanical (QM/MM) approach. The calculation results indicate that the overall reaction only contains two elementary steps. The first step is the abstraction of Cß proton of l-aspartate by Ser318, which is calculated to be rate limiting. The second step is the cleavage of CαN bond of l-aspartate to form fumarate and ammonia. Ser318 functions as the catalytic base, whereas His188 is a dispensable residue, but its protonation state can influence the active site structure and the existing form of leaving amino group, thereby influences the activity of the enzyme, which can well explain the pH dependence of enzymatic activity. Mutation of His188 to Ala only changes the active site structure and slightly elongates the distance of Cß proton of substrate with Ser318, causing the enzyme to remain significant but reduced activity.
[Mh] Termos MeSH primário: Aspartato Amônia-Liase/química
Proteínas de Bactérias/química
[Mh] Termos MeSH secundário: Ácido Aspártico/química
Bacillus/enzimologia
Biocatálise
Domínio Catalítico
Simulação por Computador
Ligações de Hidrogênio
Modelos Moleculares
Oxirredução
Ligação Proteica
Estrutura Secundária de Proteína
Teoria Quântica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 30KYC7MIAI (Aspartic Acid); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:140628
[Lr] Data última revisão:
140628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140531
[St] Status:MEDLINE


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[PMID]:24416937
[Au] Autor:Singh RS
[Ad] Endereço:Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala 147 002, India. rssingh11@lycos.com
[Ti] Título:A comparative study on cell disruption methods for release of aspartase from E. coli K-12.
[So] Source:Indian J Exp Biol;51(11):997-1003, 2013 Nov.
[Is] ISSN:0019-5189
[Cp] País de publicação:India
[La] Idioma:eng
[Ab] Resumo:Applicability of different mechanical cell disruption techniques namely sonication, bead milling and French press for the release of aspartase from E. coli K-12 was compared. Various operating parameters of each technique were optimized to obtain maximum aspartase release. The efficiency of aspartase release and cell disruption by all the methods was also compared under optimal conditions. The maximum release of aspartase (98.22%) and maximum cell breakage (84.25%) was observed using French press, while 92% of aspartase release was obtained by both sonication and bead milling. The order of cell disruption constant (k) for aspartase release by these methods was French press > bead milling > sonication. Disruption of cells using French press also demonstrated maximum protein release (14.12 mg/mL). The crude enzyme preparations can be further used for purification and its applications.
[Mh] Termos MeSH primário: Aspartato Amônia-Liase/metabolismo
Escherichia coli/enzimologia
[Mh] Termos MeSH secundário: Reatores Biológicos
Escherichia coli/citologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:140114
[Lr] Data última revisão:
140114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140115
[St] Status:MEDLINE


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[PMID]:23219690
[Au] Autor:Singh RS; Yadav M
[Ad] Endereço:Carbohydrate and Protein Biotechnology Laboratory, Department of Biotechnology, Punjabi University, Patiala, India. rssingh11@lycos.com
[Ti] Título:Enhanced production of recombinant aspartase of Aeromonas media NFB-5 in a stirred tank reactor.
[So] Source:Bioresour Technol;145:217-23, 2013 Oct.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aspartase gene (aspA) from Aeromonas media NFB-5 was cloned and expressed in Escherichia coli BL21 using pET21b(+) expression vector. Maximum production of aspartase was obtained at shake-flask after 5 h of IPTG (1.5 mM) induction at 37°C and by supplementing the media with KH2PO4 (0.3%, w/v) and K2HPO4 (0.3%, w/v). Further production was investigated at a laboratory scale stirred tank reactor using response surface methodology (RSM). Agitation (130-270 rpm), aeration (0.30-1.70 vvm) and IPTG induction time (3-7 h) was optimized. Optimal levels of agitation (250 rpm), aeration (1.25 vvm) and induction time (6h) were determined by statistical analysis of the experimental data. More than 7-fold increase in recombinant aspartase (1234 U/g wet weight) was observed than the parent strain (172 U/g wet wt). Homogenized immobilized permeabilized recombinant cells (566 mg/g wet cells) produced more L-aspartic acid as compared to permeabilized recombinant free cells (154 mg/g wet cells).
[Mh] Termos MeSH primário: Aeromonas/enzimologia
Aspartato Amônia-Liase/biossíntese
Aspartato Amônia-Liase/genética
Reatores Biológicos
Escherichia coli/metabolismo
Proteínas Recombinantes/biossíntese
[Mh] Termos MeSH secundário: Aeromonas/genética
Cromatografia Líquida de Alta Pressão
Clonagem Molecular
Fosfatos
Compostos de Potássio
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phosphates); 0 (Potassium Compounds); 0 (Recombinant Proteins); B7862WZ632 (potassium phosphate); EC 4.3.1.1 (Aspartate Ammonia-Lyase)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121211
[St] Status:MEDLINE


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[PMID]:22834890
[Au] Autor:de Villiers M; Puthan Veetil V; Raj H; de Villiers J; Poelarends GJ
[Ad] Endereço:Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Groningen, The Netherlands.
[Ti] Título:Catalytic mechanisms and biocatalytic applications of aspartate and methylaspartate ammonia lyases.
[So] Source:ACS Chem Biol;7(10):1618-28, 2012 Oct 19.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ammonia lyases catalyze the formation of α,ß-unsaturated bonds by the elimination of ammonia from their substrates. This conceptually straightforward reaction has been the emphasis of many studies, with the main focus on the catalytic mechanism of these enzymes and/or the use of these enzymes as catalysts for the synthesis of enantiomerically pure α-amino acids. In this Review aspartate ammonia lyase and 3-methylaspartate ammonia lyase, which represent two different enzyme superfamilies, are discussed in detail. In the past few years, the three-dimensional structures of these lyases in complex with their natural substrates have revealed the details of two elegant catalytic strategies. These strategies exploit similar deamination mechanisms that involve general-base catalyzed formation of an enzyme-stabilized enolate anion (aci-carboxylate) intermediate. Recent progress in the engineering and application of these enzymes to prepare enantiopure l-aspartic acid derivatives, which are highly valuable as tools for biological research and as chiral building blocks for pharmaceuticals and food additives, is also discussed.
[Mh] Termos MeSH primário: Amônia-Liases/metabolismo
Aspartato Amônia-Liase/metabolismo
[Mh] Termos MeSH secundário: Amônia/química
Amônia-Liases/química
Aspartato Amônia-Liase/química
Bactérias/enzimologia
Biocatálise
Domínio Catalítico
Modelos Moleculares
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
7664-41-7 (Ammonia); EC 4.3.1.- (Ammonia-Lyases); EC 4.3.1.1 (Aspartate Ammonia-Lyase); EC 4.3.1.2 (methylaspartate ammonia-lyase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:121019
[Lr] Data última revisão:
121019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120728
[St] Status:MEDLINE
[do] DOI:10.1021/cb3002792


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[PMID]:22551392
[Au] Autor:Puthan Veetil V; Fibriansah G; Raj H; Thunnissen AM; Poelarends GJ
[Ad] Endereço:Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
[Ti] Título:Aspartase/fumarase superfamily: a common catalytic strategy involving general base-catalyzed formation of a highly stabilized aci-carboxylate intermediate.
[So] Source:Biochemistry;51(21):4237-43, 2012 May 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Members of the aspartase/fumarase superfamily share a common tertiary and quaternary fold, as well as a similar active site architecture; the superfamily includes aspartase, fumarase, argininosuccinate lyase, adenylosuccinate lyase, δ-crystallin, and 3-carboxy-cis,cis-muconate lactonizing enzyme (CMLE). These enzymes all process succinyl-containing substrates, leading to the formation of fumarate as the common product (except for the CMLE-catalyzed reaction, which results in the formation of a lactone). In the past few years, X-ray crystallographic analysis of several superfamily members in complex with substrate, product, or substrate analogues has provided detailed insights into their substrate binding modes and catalytic mechanisms. This structural work, combined with earlier mechanistic studies, revealed that members of the aspartase/fumarase superfamily use a common catalytic strategy, which involves general base-catalyzed formation of a stabilized aci-carboxylate (or enediolate) intermediate and the participation of a highly flexible loop, containing the signature sequence GSSxxPxKxN (named the SS loop), in substrate binding and catalysis.
[Mh] Termos MeSH primário: Aspartato Amônia-Liase/química
Aspartato Amônia-Liase/metabolismo
Fumarato Hidratase/química
Fumarato Hidratase/metabolismo
[Mh] Termos MeSH secundário: Adenilossuccinato Liase/química
Adenilossuccinato Liase/genética
Adenilossuccinato Liase/metabolismo
Sequência de Aminoácidos
Argininossuccinato Liase/química
Argininossuccinato Liase/genética
Argininossuccinato Liase/metabolismo
Aspartato Amônia-Liase/genética
Catálise
Domínio Catalítico
Sequência Conservada
Escherichia coli/enzimologia
Escherichia coli/genética
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Fumarato Hidratase/genética
Seres Humanos
Liases Intramoleculares/química
Liases Intramoleculares/genética
Liases Intramoleculares/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Estrutura Quaternária de Proteína
Estrutura Terciária de Proteína
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
delta-Cristalinas/química
delta-Cristalinas/genética
delta-Cristalinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (delta-Crystallins); EC 4.2.1.2 (Fumarate Hydratase); EC 4.3.1.1 (Aspartate Ammonia-Lyase); EC 4.3.2.1 (Argininosuccinate Lyase); EC 4.3.2.2 (Adenylosuccinate Lyase); EC 5.5.- (Intramolecular Lyases); EC 5.5.1.5 (3-carboxy-cis-cis-muconate cyclase)
[Em] Mês de entrada:1207
[Cu] Atualização por classe:120529
[Lr] Data última revisão:
120529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120504
[St] Status:MEDLINE
[do] DOI:10.1021/bi300430j



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