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[PMID]:27261771
[Au] Autor:Ruszkowski M; Dauter Z
[Ad] Endereço:Synchrotron Radiation Research Section of MCL, National Cancer Institute, Argonne, Illinois.
[Ti] Título:On methylene-bridged cysteine and lysine residues in proteins.
[So] Source:Protein Sci;25(9):1734-6, 2016 Sep.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cysteine residues ubiquitously stabilize tertiary and quaternary protein structure by formation of disulfide bridges. Here we investigate another linking interaction that involves sulfhydryl groups of cysteines, namely intra- and intermolecular methylene-bridges between cysteine and lysine residues. A number of crystal structures possessing such a linkage were identified in the Protein Data Bank. Inspection of the electron density maps and re-refinement of the nominated structures unequivocally confirmed the presence of Lys-CH2 -Cys bonds in several cases.
[Mh] Termos MeSH primário: Bases de Dados de Proteínas
Histidinol-Fosfatase/química
Medicago truncatula/enzimologia
Proteínas de Plantas/química
[Mh] Termos MeSH secundário: Cisteína/química
Lisina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); EC 3.1.3.15 (Histidinol-Phosphatase); K3Z4F929H6 (Lysine); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE
[do] DOI:10.1002/pro.2958


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[PMID]:26994138
[Au] Autor:Ruszkowski M; Dauter Z
[Ad] Endereço:From the Synchrotron Radiation Research Section of MCL, NCI, National Institutes of Health, Argonne, Illinois 60439 mruszkowski@anl.gov.
[Ti] Título:Structural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in Plants.
[So] Source:J Biol Chem;291(19):9960-73, 2016 May 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The penultimate enzyme in the histidine biosynthetic pathway catalyzes dephosphorylation of l-histidinol 1-phosphate (HOLP) into l-histidinol. The recently discovered in Arabidopsis thaliana plant-type histidinol phosphate phosphatase (HPP) shares no homology with the two other HPP superfamilies known previously in prokaryotes and resembles myo-inositol monophosphatases (IMPases). In this work, identification of an HPP enzyme from a model legume, Medicago truncatula (MtHPP) was based on the highest sequence identity to A. thaliana enzyme. Biochemical assays confirmed that MtHPP was able to cleave inorganic phosphate from HOLP but not from d-myo-inositol-1-phosphate, the main substrate of IMPases. Dimers of MtHPP, determined by size exclusion chromatography, in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys(158) and Cys(245) residues. Four high resolution crystal structures, namely complexes with HOLP (substrate), l-histidinol (product), and PO4 (3-) (by-product) as well as the structure showing the cross-linking between two MtHPP molecules, provide detailed structural information on the enzyme. Based on the crystal structures, the enzymatic reaction mechanism of IMPases is accustomed to fit the data for MtHPP. The enzymatic reaction, which requires Mg(2+) cations, is catalyzed mainly by amino acid residues from the N-terminal domain. The C-terminal domain, sharing little identity with IMPases, is responsible for the substrate specificity (i.e. allows the enzyme to distinguish between HOLP and d-myo-inositol-1-phosphate). Structural features, mainly the presence of a conserved Asp(246), allow MtHPP to bind HOLP specifically.
[Mh] Termos MeSH primário: Histidinol-Fosfatase/química
Medicago truncatula/enzimologia
Proteínas de Plantas/química
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Arabidopsis/genética
Cristalografia por Raios X
Histidina/biossíntese
Histidina/química
Histidina/genética
Histidinol-Fosfatase/genética
Histidinol-Fosfatase/metabolismo
Medicago truncatula/genética
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Estrutura Terciária de Proteína
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Plant Proteins); 4QD397987E (Histidine); EC 3.1.3.15 (Histidinol-Phosphatase)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170506
[Lr] Data última revisão:
170506
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160320
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.708727


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[PMID]:23728795
[Au] Autor:Yip SH; Matsumura I
[Ad] Endereço:Department of Biochemistry, Center for Fundamental and Applied Molecular Evolution, Rollins Research Center, Emory University School of Medicine, USA.
[Ti] Título:Substrate ambiguous enzymes within the Escherichia coli proteome offer different evolutionary solutions to the same problem.
[So] Source:Mol Biol Evol;30(9):2001-12, 2013 Sep.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many enzymes exhibit some catalytic promiscuity or substrate ambiguity. These weak activities do not affect the fitness of the organism under ordinary circumstances, but can serve as potential evolutionary precursors of new catalytic functions. We wondered whether different proteins with the same substrate ambiguous activity evolve differently under identical selection conditions. Patrick et al. (Patrick WM, Quandt EM, Swartzlander DB, Matsumura I. 2007. Multicopy suppression underpins metabolic evolvability. Mol Biol Evol. 24:2716-2722.) previously showed that three multicopy suppressors, gph, hisB, and ytjC, rescue ΔserB Escherichia coli cells from starvation on minimal media. We directed the evolution of variants of Gph, histidinol phosphatase (HisB), and YtjC that complemented ΔserB more efficiently, and characterized the effects of the amino acid changes, alone and in combination, upon the evolved phosphoserine phosphatase (PSP) activity. Gph and HisB are members of the HAD superfamily of hydrolases, but they adapted through different, kinetically distinguishable, biochemical mechanisms. All of the selected mutations, except N102T in YtjC, proved to be beneficial in isolation. They exhibited a pattern of antagonistic epistasis, as their effects in combination upon the kinetic parameters of the three proteins in reactions with phosphoserine were nonmultiplicative. The N102T mutation exhibited sign epistasis, as it was deleterious in isolation but beneficial in the context of other mutations. We also showed that the D57N mutation in the chromosomal copy of hisB is sufficient to suppress the ΔserB deletion. These results in combination show that proteomes can offer multiple mechanistic solutions to a molecular recognition problem.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Histidinol-Fosfatase/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Evolução Biológica
Epistasia Genética
Escherichia coli/enzimologia
Proteínas de Escherichia coli/genética
Genes Supressores
Teste de Complementação Genética
Histidinol-Fosfatase/genética
Cinética
Modelos Moleculares
Mutação
Monoéster Fosfórico Hidrolases/genética
Fosfosserina/metabolismo
Proteoma/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Proteome); 17885-08-4 (Phosphoserine); EC 3.1.3.15 (Histidinol-Phosphatase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.3 (phosphoserine phosphatase)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130604
[St] Status:MEDLINE
[do] DOI:10.1093/molbev/mst105


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[PMID]:23327428
[Au] Autor:Ghodge SV; Fedorov AA; Fedorov EV; Hillerich B; Seidel R; Almo SC; Raushel FM
[Ad] Endereço:Department of Chemistry, P.O. Box 30012, Texas A&M University, College Station, TX 77843-3012, USA.
[Ti] Título:Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins.
[So] Source:Biochemistry;52(6):1101-12, 2013 Feb 12.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:L-Histidinol phosphate phosphatase (HPP) catalyzes the hydrolysis of L-histidinol phosphate to L-histidinol and inorganic phosphate, the penultimate step in the biosynthesis of L-histidine. HPP from the polymerase and histidinol phosphatase (PHP) family of proteins possesses a trinuclear active site and a distorted (ß/α)(7)-barrel protein fold. This group of enzymes is closely related to the amidohydrolase superfamily of enzymes. The mechanism of phosphomonoester bond hydrolysis by the PHP family of HPP enzymes was addressed. Recombinant HPP from Lactococcus lactis subsp. lactis that was expressed in Escherichia coli contained a mixture of iron and zinc in the active site and had a catalytic efficiency of ~10(3) M(-1) s(-1). Expression of the protein under iron-free conditions resulted in the production of an enzyme with a 2 order of magnitude improvement in catalytic efficiency and a mixture of zinc and manganese in the active site. Solvent isotope and viscosity effects demonstrated that proton transfer steps and product dissociation steps are not rate-limiting. X-ray structures of HPP were determined with sulfate, L-histidinol phosphate, and a complex of L-histidinol and arsenate bound in the active site. These crystal structures and the catalytic properties of variants were used to identify the structural elements required for catalysis and substrate recognition by the HPP family of enzymes within the amidohydrolase superfamily.
[Mh] Termos MeSH primário: Arseniatos/metabolismo
Escherichia coli/enzimologia
Histidina/metabolismo
Histidinol-Fosfatase/química
Lactococcus lactis/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Catálise
Domínio Catalítico
Biologia Computacional
Cristalografia por Raios X
Escherichia coli/genética
Histidinol-Fosfatase/genética
Histidinol-Fosfatase/metabolismo
Concentração de Íons de Hidrogênio
Lactococcus lactis/genética
Modelos Moleculares
Dados de Sequência Molecular
Família Multigênica
Mutagênese Sítio-Dirigida
Mutação/genética
Proteínas Recombinantes
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arsenates); 0 (Recombinant Proteins); 4QD397987E (Histidine); EC 3.1.3.15 (Histidinol-Phosphatase); N7CIZ75ZPN (arsenic acid)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130119
[St] Status:MEDLINE
[do] DOI:10.1021/bi301496p


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[PMID]:21538547
[Au] Autor:Han GW; Ko J; Farr CL; Deller MC; Xu Q; Chiu HJ; Miller MD; Sefcikova J; Somarowthu S; Beuning PJ; Elsliger MA; Deacon AM; Godzik A; Lesley SA; Wilson IA; Ondrechen MJ
[Ad] Endereço:Joint Center for Structural Genomics, Scripps Research Institute, La Jolla, California 92037, USA.
[Ti] Título:Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity.
[So] Source:Proteins;79(7):2146-60, 2011 Jul.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The crystal structures of an unliganded and adenosine 5'-monophosphate (AMP) bound, metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis are reported at 2.4 and 1.94 Å, respectively. Functional characterization of this enzyme was guided by computational analysis and then confirmed by experiment. The structure consists of a polymerase and histidinol phosphatase (PHP, Pfam: PF02811) domain with a second domain (residues 105-178) inserted in the middle of the PHP sequence. The insert domain functions in binding AMP, but the precise function and substrate specificity of this domain are unknown. Initial bioinformatics analyses yielded multiple potential functional leads, with most of them suggesting DNA polymerase or DNA replication activity. Phylogenetic analysis indicated a potential DNA polymerase function that was somewhat supported by global structural comparisons identifying the closest structural match to the alpha subunit of DNA polymerase III. However, several other functional predictions, including phosphoesterase, could not be excluded. Theoretical microscopic anomalous titration curve shapes, a computational method for the prediction of active sites from protein 3D structures, identified potential reactive residues in YP_910028.1. Further analysis of the predicted active site and local comparison with its closest structure matches strongly suggested phosphoesterase activity, which was confirmed experimentally. Primer extension assays on both normal and mismatched DNA show neither extension nor degradation and provide evidence that YP_910028.1 has neither DNA polymerase activity nor DNA-proofreading activity. These results suggest that many of the sequence neighbors previously annotated as having DNA polymerase activity may actually be misannotated.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Bifidobacterium/enzimologia
Esterases/química
Esterases/metabolismo
[Mh] Termos MeSH secundário: 4-Nitrofenilfosfatase/química
4-Nitrofenilfosfatase/metabolismo
Difosfato de Adenosina/química
Difosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Sítios de Ligação
Domínio Catalítico
Simulação por Computador
Cristalografia
DNA Polimerase III/química
DNA Polimerase III/metabolismo
Histidinol-Fosfatase/química
Histidinol-Fosfatase/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Filogenia
Reprodutibilidade dos Testes
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Bacterial Proteins); 61D2G4IYVH (Adenosine Diphosphate); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (DNA polymerase III, alpha subunit); EC 3.1.- (Esterases); EC 3.1.3.15 (Histidinol-Phosphatase); EC 3.1.3.41 (4-Nitrophenylphosphatase)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110504
[St] Status:MEDLINE
[do] DOI:10.1002/prot.23035


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[PMID]:20050615
[Au] Autor:Wang L; Huang H; Nguyen HH; Allen KN; Mariano PS; Dunaway-Mariano D
[Ad] Endereço:Department of Chemistry and Chemical Biology, University of New Mexico, Albuquerque, New Mexico 87131, USA.
[Ti] Título:Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).
[So] Source:Biochemistry;49(6):1072-81, 2010 Feb 16.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:D-Glycero-d-manno-heptose-1,7-bisphosphate phosphatase (GmhB) is a member of the histidinol-phosphate phosphatase (HisB) subfamily of the haloalkanoic acid dehalogenase (HAD) enzyme superfamily. GmhB supports two divergent biochemical pathways in bacteria: the d-glycero-d-manno-heptose-1alpha-GDP pathway (in S-layer glycoprotein biosynthesis) and the l-glycero-d-manno-heptose-1beta-ADP pathway (in lipid A biosynthesis). Herein, we report the comparative analysis of substrate recognition in selected GmhB orthologs. The substrate specificity of the l-glycero-d-manno-heptose-1beta-ADP pathway GmhB from Escherichia coli K-12 was evaluated using hexose and heptose bisphosphates, histidinol phosphate, and common organophosphate metabolites. Only d-glycero-d-manno-heptose 1beta,7-bisphosphate (k(cat)/K(m) = 7 x 10(6) M(-1) s(-1)) and d-glycero-d-manno-heptose 1alpha,7-bisphosphate (k(cat)/K(m) = 7 x 10(4) M(-1) s(-1)) displayed physiologically significant substrate activity. (31)P NMR analysis demonstrated that E. coli GmhB selectively removes the C(7) phosphate. Steady-state kinetic inhibition studies showed that d-glycero-d-manno-heptose 1beta-phosphate (K(is) = 60 microM, and K(ii) = 150 microM) and histidinol phosphate (K(is) = 1 mM, and K(ii) = 6 mM), while not hydrolyzed, do in fact bind to E. coli GmhB, which leads to the conclusion that nonproductive binding contributes to substrate discrimination. High catalytic efficiency and a narrow substrate range are characteristic of a well-evolved metabolic enzyme, and as such, E. coli GmhB is set apart from most HAD phosphatases (which are typically inefficient and promiscuous). The specialization of the biochemical function of GmhB was examined by measuring the kinetic constants for hydrolysis of the alpha- and beta-anomers of d-glycero-d-manno-heptose 1beta,7-bisphosphate catalyzed by the GmhB orthologs of the l-glycero-d-manno-heptose 1beta-ADP pathways operative in Bordetella bronchiseptica and Mesorhizobium loti and by the GmhB of the d-glycero-d-manno-heptose 1alpha-GDP pathway operative in Bacteroides thetaiotaomicron. The results show that although each of these representatives possesses physiologically significant catalytic activity toward both anomers, each displays substantial anomeric specificity. Like E. coli GmhB, B. bronchiseptica GmhB and M. loti GmhB prefer the beta-anomer, whereas B. thetaiotaomicron GmhB is selective for the alpha-anomer. By determining the anomeric configuration of the physiological substrate (d-glycero-d-manno-heptose 1,7-bisphosphate) for each of the four GmhB orthologs, we discovered that the anomeric specificity of GmhB correlates with that of the pathway kinase. The conclusion drawn from this finding is that the evolution of the ancestor to GmhB in the HisB subfamily provided for specialization toward two distinct biochemical functions.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
Hidrolases/química
Família Multigênica
Monoéster Fosfórico Hidrolases/química
[Mh] Termos MeSH secundário: Alphaproteobacteria/enzimologia
Bacteroides/enzimologia
Bordetella bronchiseptica/enzimologia
Catálise
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Heptoses/química
Heptoses/genética
Histidinol-Fosfatase/química
Histidinol-Fosfatase/genética
Hidrolases/genética
Monoéster Fosfórico Hidrolases/genética
Especificidade por Substrato/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Heptoses); 4305-74-2 (glycero-manno-heptose); EC 3.- (Hydrolases); EC 3.1.3.- (D,D-heptose 1,7-bisphosphate phosphatase, E coli); EC 3.1.3.15 (Histidinol-Phosphatase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.8.1.2 (2-haloacid dehalogenase); EC 3.8.1.5 (haloalkane dehalogenase)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100107
[St] Status:MEDLINE
[do] DOI:10.1021/bi902018y


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[PMID]:20050614
[Au] Autor:Nguyen HH; Wang L; Huang H; Peisach E; Dunaway-Mariano D; Allen KN
[Ad] Endereço:Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2394, USA.
[Ti] Título:Structural determinants of substrate recognition in the HAD superfamily member D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB) .
[So] Source:Biochemistry;49(6):1082-92, 2010 Feb 16.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The haloalkanoic acid dehalogenase (HAD) enzyme superfamily is the largest family of phosphohydrolases. In HAD members, the structural elements that provide the binding interactions that support substrate specificity are separated from those that orchestrate catalysis. For most HAD phosphatases, a cap domain functions in substrate recognition. However, for the HAD phosphatases that lack a cap domain, an alternate strategy for substrate selection must be operative. One such HAD phosphatase, GmhB of the HisB subfamily, was selected for structure-function analysis. Herein, the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg(2+) and orthophosphate (1.8 A resolution), and in a complex with Mg(2+) and d-glycero-d-manno-heptose 1beta,7-bisphosphate (2.2 A resolution) were determined, in addition to the structure of Bordetella bronchiseptica GmhB bound to Mg(2+) and orthophosphate (1.7 A resolution). The structures show that in place of a cap domain, the GmhB catalytic site is elaborated by three peptide inserts or loops that pack to form a concave, semicircular surface around the substrate leaving group. Structure-guided kinetic analysis of site-directed mutants was conducted in parallel with a bioinformatics study of sequence diversification within the HisB subfamily to identify loop residues that serve as substrate recognition elements and that distinguish GmhB from its subfamily counterpart, the histidinol-phosphate phosphatase domain of HisB. We show that GmhB and the histidinol-phosphate phosphatase domain use the same design of three substrate recognition loops inserted into the cap domain yet, through selective residue usage on the loops, have achieved unique substrate specificity and thus novel biochemical function.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
Hidrolases/química
Família Multigênica
Monoéster Fosfórico Hidrolases/química
[Mh] Termos MeSH secundário: Apoenzimas/química
Apoenzimas/genética
Bordetella bronchiseptica/enzimologia
Bordetella bronchiseptica/genética
Cristalografia por Raios X
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Histidinol-Fosfatase/química
Histidinol-Fosfatase/genética
Hidrolases/genética
Mutagênese Sítio-Dirigida
Monoéster Fosfórico Hidrolases/genética
Ligação Proteica/genética
Estrutura Terciária de Proteína/genética
Especificidade por Substrato/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Apoenzymes); 0 (Escherichia coli Proteins); EC 3.- (Hydrolases); EC 3.1.3.- (D,D-heptose 1,7-bisphosphate phosphatase, E coli); EC 3.1.3.15 (Histidinol-Phosphatase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.8.1.- (haloalcohol dehalogenase)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100107
[St] Status:MEDLINE
[do] DOI:10.1021/bi902019q


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[PMID]:20023146
[Au] Autor:Petersen LN; Marineo S; Mandalà S; Davids F; Sewell BT; Ingle RA
[Ad] Endereço:Department of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa.
[Ti] Título:The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.
[So] Source:Plant Physiol;152(3):1186-96, 2010 Mar.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Histidina/biossíntese
Histidinol-Fosfatase/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
DNA Bacteriano/genética
DNA de Plantas/genética
Regulação da Expressão Gênica de Plantas
Teste de Complementação Genética
Histidinol/metabolismo
Histidinol-Fosfatase/genética
Modelos Moleculares
Mutagênese Insercional
Mutação
Fosforilação
Filogenia
Estrutura Terciária de Proteína
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (DNA, Bacterial); 0 (DNA, Plant); 0 (Recombinant Fusion Proteins); 0 (T-DNA); 4QD397987E (Histidine); 501-28-0 (Histidinol); EC 3.1.3.15 (Histidinol-Phosphatase)
[Em] Mês de entrada:1006
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:091222
[St] Status:MEDLINE
[do] DOI:10.1104/pp.109.150805


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[PMID]:19407379
[Au] Autor:Jung HI; Lee HS; An YJ; Cho Y; Lee JH; Kang SG; Cha SS
[Ad] Endereço:Marine and Extreme Genome Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea.
[Ti] Título:Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1.
[So] Source:Acta Crystallogr Sect F Struct Biol Cryst Commun;65(Pt 5):472-4, 2009 May 01.
[Is] ISSN:1744-3091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The TON_0887 gene product from Thermococcus onnurineus NA1 is a 240-residue protein that has histidinol-phosphate phosphatase (HolPase) activity. According to analysis of its primary structure, the TON_0887 gene product is a monofunctional HolPase that belongs to the DDDD superfamily. This contrasts with the generally accepted classification that bifunctional HolPases belong to the DDDD superfamily. The TON_0887 gene product was purified and crystallized at 295 K. A 2.2 A resolution data set was collected using synchrotron radiation. The TON-HolPase crystals belonged to space group P222(1), with unit-cell parameters a = 40.88, b = 46.89, c = 148.03 A. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 48.3%.
[Mh] Termos MeSH primário: Histidinol-Fosfatase/química
Thermococcus/enzimologia
[Mh] Termos MeSH secundário: Cristalização
Cristalografia por Raios X
Histidinol-Fosfatase/genética
Histidinol-Fosfatase/metabolismo
Thermococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.1.3.15 (Histidinol-Phosphatase)
[Em] Mês de entrada:0906
[Cu] Atualização por classe:141209
[Lr] Data última revisão:
141209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090502
[St] Status:MEDLINE
[do] DOI:10.1107/S1744309109010732


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[PMID]:19211662
[Au] Autor:Nakane S; Nakagawa N; Kuramitsu S; Masui R
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
[Ti] Título:Characterization of DNA polymerase X from Thermus thermophilus HB8 reveals the POLXc and PHP domains are both required for 3'-5' exonuclease activity.
[So] Source:Nucleic Acids Res;37(6):2037-52, 2009 Apr.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The X-family DNA polymerases (PolXs) comprise a highly conserved DNA polymerase family found in all kingdoms. Mammalian PolXs are known to be involved in several DNA-processing pathways including repair, but the cellular functions of bacterial PolXs are less known. Many bacterial PolXs have a polymerase and histidinol phosphatase (PHP) domain at their C-termini in addition to a PolX core (POLXc) domain, and possess 3'-5' exonuclease activity. Although both domains are highly conserved in bacteria, their molecular functions, especially for a PHP domain, are unknown. We found Thermus thermophilus HB8 PolX (ttPolX) has Mg(2+)/Mn(2+)-dependent DNA/RNA polymerase, Mn(2+)-dependent 3'-5' exonuclease and DNA-binding activities. We identified the domains of ttPolX by limited proteolysis and characterized their biochemical activities. The POLXc domain was responsible for the polymerase and DNA-binding activities but exonuclease activity was not detected for either domain. However, the POLXc and PHP domains interacted with each other and a mixture of the two domains had Mn(2+)-dependent 3'-5' exonuclease activity. Moreover, site-directed mutagenesis revealed catalytically important residues in the PHP domain for the 3'-5' exonuclease activity. Our findings provide a molecular insight into the functional domain organization of bacterial PolXs, especially the requirement of the PHP domain for 3'-5' exonuclease activity.
[Mh] Termos MeSH primário: DNA Polimerase Dirigida por DNA/química
Exodesoxirribonucleases/química
Thermus thermophilus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
DNA/metabolismo
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/metabolismo
Exodesoxirribonucleases/metabolismo
Histidinol-Fosfatase/química
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Domínios e Motivos de Interação entre Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.7.7.- (DNA polymerase X); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.3.15 (Histidinol-Phosphatase)
[Em] Mês de entrada:0904
[Cu] Atualização por classe:141210
[Lr] Data última revisão:
141210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090213
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkp064



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