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  1 / 202 MEDLINE  
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[PMID]:27987384
[Au] Autor:Tramonti A; Milano T; Nardella C; di Salvo ML; Pascarella S; Contestabile R
[Ad] Endereço:Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Rome, Italy.
[Ti] Título:Salmonella typhimurium PtsJ is a novel MocR-like transcriptional repressor involved in regulating the vitamin B salvage pathway.
[So] Source:FEBS J;284(3):466-484, 2017 Feb.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The vitamin B salvage pathway, involving pyridoxine 5'-phosphate oxidase (PNPOx) and pyridoxal kinase (PLK), recycles B vitamers from nutrients and protein turnover to produce pyridoxal 5'-phosphate (PLP), the catalytically active form of the vitamin. Regulation of this pathway, widespread in living organisms including humans and many bacteria, is very important to vitamin B homeostasis but poorly understood. Although some information is available on the enzymatic regulation of PNPOx and PLK, little is known on their regulation at the transcriptional level. In the present work, we identified a new MocR-like regulator, PtsJ from Salmonella typhimurium, which controls the expression of the pdxK gene encoding one of the two PLKs expressed in this organism (PLK1). Analysis of pdxK expression in a ptsJ knockout strain demonstrated that PtsJ acts as a transcriptional repressor. This is the first case of a MocR-like regulator acting as repressor of its target gene. Expression and purification of PtsJ allowed a detailed characterisation of its effector and DNA-binding properties. PLP is the only B vitamer acting as effector molecule for PtsJ. A DNA-binding region composed of four repeated nucleotide sequences is responsible for binding of PtsJ to its target promoter. Analysis of binding stoichiometry revealed that protein subunits/DNA molar ratio varies from 4 : 1 to 2 : 1, depending on the presence or absence of PLP. Structural characteristics of DNA transcriptional factor-binding sites suggest that PtsJ binds DNA according to a different model with respect to other characterised members of the MocR subgroup.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Regulação Bacteriana da Expressão Gênica
Piridoxal Quinase/química
Piridoxaminafosfato Oxidase/química
Proteínas Repressoras/química
Salmonella typhimurium/metabolismo
Vitamina B 6/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Clonagem Molecular
DNA Bacteriano/química
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Modelos Moleculares
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Piridoxal Quinase/genética
Piridoxal Quinase/metabolismo
Fosfato de Piridoxal/química
Fosfato de Piridoxal/metabolismo
Piridoxaminafosfato Oxidase/genética
Piridoxaminafosfato Oxidase/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Salmonella typhimurium/química
Alinhamento de Sequência
Homologia Estrutural de Proteína
Transcrição Genética
Vitamina B 6/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Recombinant Proteins); 0 (Repressor Proteins); 5V5IOJ8338 (Pyridoxal Phosphate); 8059-24-3 (Vitamin B 6); EC 1.4.3.5 (Pyridoxaminephosphate Oxidase); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1111/febs.13994


  2 / 202 MEDLINE  
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[PMID]:27425248
[Au] Autor:Kim MI; Hong M
[Ad] Endereço:Division of Biological Science and Technology, Yonsei University, Wonju, Republic of Korea.
[Ti] Título:Crystal structure and catalytic mechanism of pyridoxal kinase from Pseudomonas aeruginosa.
[So] Source:Biochem Biophys Res Commun;478(1):300-306, 2016 09 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyridoxal kinase is a ubiquitous enzyme essential for pyridoxal 5'-phosphate (PLP) homeostasis since PLP is required for the catalytic activity of a variety of PLP-dependent enzymes involved in amino acid, lipid, and sugar metabolism as well as neurotransmitter biosynthesis. Previously, two catalytic mechanisms were proposed with regard to Pdx kinases, in which either the aspartate or the cysteine residue is involved as a catalytic residue. Because the Pdx kinase of Pseudomonas aeruginosa (PaPdxK) contains both residues, the catalytic mechanism of PaPdxK remains elusive. To elucidate the substrate-recognition and catalytic mechanisms of PaPdxK, the crystal structure of PaPdxK was determined at a 2.0 Å resolution. The PaPdxK structure possesses a channel that can accommodate substrates and a metallic cofactor. Our structure-based biochemical and mutational analyses in combination with modeling studies suggest that PaPdxK catalysis is mediated by an acid-base mechanism through the catalytic acid Asp225 and a helical dipole moment.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Magnésio/química
Pseudomonas aeruginosa/enzimologia
Piridoxal Quinase/química
Piridoxal Quinase/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Catálise
Ativação Enzimática
Simulação de Acoplamento Molecular
Ligação Proteica
Conformação Proteica
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.35 (Pyridoxal Kinase); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171127
[Lr] Data última revisão:
171127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160719
[St] Status:MEDLINE


  3 / 202 MEDLINE  
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[PMID]:26831303
[Au] Autor:Moreno-Navarrete JM; Jove M; Ortega F; Xifra G; Ricart W; Obis È; Pamplona R; Portero-Otin M; Fernández-Real JM
[Ad] Endereço:Department of Diabetes, Endocrinology and Nutrition, Institut d'Investigació Biomèdica de Girona (IdIBGi), Hospital of Girona 'Dr Josep Trueta', Carretera de França s/n, 17007, Girona, Spain.
[Ti] Título:Metabolomics uncovers the role of adipose tissue PDXK in adipogenesis and systemic insulin sensitivity.
[So] Source:Diabetologia;59(4):822-32, 2016 Apr.
[Is] ISSN:1432-0428
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:AIMS/HYPOTHESIS: We aimed to investigate the potential mechanisms involved in the compromised adipogenesis of visceral (VAT) vs subcutaneous adipose tissue (SAT) using comparative metabolomics. Based on the differentially identified metabolites, we focused on the relationship between the active form of vitamin B6 (pyridoxal 5-phosphate [PLP]), known to be generated through pyridoxal kinase (PDXK), and adipogenesis. METHODS: Non-targeted metabolomics analyses were performed in paired VAT and SAT (n = 14, discovery cohort). PDXK gene expression was evaluated in two validation cohorts of paired SAT and VAT samples in relation to obesity status and insulin sensitivity, and mechanistically after weight loss in vivo and in 3T3-L1 cells in vitro. RESULTS: Comparative metabolomics showed that PLP was significantly decreased in VAT vs SAT. Concordantly, PDXK mRNA levels were significantly decreased in VAT vs SAT, specifically in adipocytes. The decrease was specially marked in obese individuals. PDXK mRNA levels showed a strong association with adipogenic, lipid-droplet-related and lipogenic genes. At a functional level, systemic insulin sensitivity positively associated with PDXK expression, and surgically-induced weight loss (improving insulin sensitivity) led to increased SAT PDXK mRNA levels in parallel with adipogenic genes. In human pre-adipocytes, PDXK mRNA levels increased during adipocyte differentiation and after administration of peroxisome proliferator-activated receptor-γ agonists, and decreased under inflammatory stimuli. Mechanistic studies in 3T3-L1 cells showed that PLP administration resulted in increased adipogenic mRNA markers during early adipogenesis, whereas the PLP antagonist 4-deoxypyridoxine exerted opposite effects. CONCLUSIONS/INTERPRETATION: Overall, these results support the notion that in situ production of PLP is required for physiological adipogenesis.
[Mh] Termos MeSH primário: Tecido Adiposo/metabolismo
Metabolômica/métodos
Piridoxal Quinase/metabolismo
[Mh] Termos MeSH secundário: Células 3T3-L1
Adipócitos/metabolismo
Adipogenia/genética
Adipogenia/fisiologia
Adulto
Animais
Feminino
Seres Humanos
Resistência à Insulina
Gordura Intra-Abdominal/metabolismo
Masculino
Camundongos
Meia-Idade
Obesidade/metabolismo
Gordura Subcutânea/metabolismo
Vitamina B 6/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
8059-24-3 (Vitamin B 6); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160203
[St] Status:MEDLINE
[do] DOI:10.1007/s00125-016-3863-1


  4 / 202 MEDLINE  
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[PMID]:26780217
[Au] Autor:Huang S; Yang H; Yao L; Zhang J; Huang L
[Ad] Endereço:School of Tea and Food Science, Anhui Agricultural University, Hefei 230036, People's Republic of China; Center for Cell and Gene Therapy, Takara Bio Inc., Seta 3-4-1, Otsu, Shiga 520-2193, Japan.
[Ti] Título:Effect of exogenous hormones on transcription levels of pyridoxal 5'-phosphate biosynthetic enzymes in the silkworm (Bombyx mori).
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;194-195:20-4, 2016 Apr-May.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Vitamin B6 includes 6 pyridine derivatives, among which pyridoxal 5'-phosphate is a coenzyme for over 140 enzymes. Animals acquire their vitamin B6 from food. Through a salvage pathway, pyridoxal 5'-phosphate is synthesized from pyridoxal, pyridoxine or pyridoxamine, in a series of reactions catalyzed by pyridoxal kinase and pyridoxine 5'-phosphate oxidase. The regulation of pyridoxal 5'-phospahte biosynthesis and pyridoxal 5'-phospahte homeostasis are at the center of study for vitamin B6 nutrition. How pyridoxal 5'-phosphate biosynthesis is regulated by hormones has not been reported so far. Our previous studies have shown that pyridoxal 5'-phosphate level in silkworm larva displays cyclic developmental changes. In the current study, effects of exogenous juvenile hormone and molting hormone on the transcription level of genes coding for the enzymes involved in the biosynthesis of pyridoxal 5'-phospahte were examined. Results show that pyridoxal kinase and pyridoxine 5'-phosphate oxidase are regulated at the transcription level by development and are responsive to hormones. Molting hormone stimulates the expression of genes coding for pyridoxal kinase and pyridoxine 5'-phosphate oxidase, and juvenile hormone appears to work against molting hormone. Whether pyridoxal 5'-phosphate biosynthesis is regulated by hormones in general is an important issue for further studies.
[Mh] Termos MeSH primário: Bombyx/fisiologia
Hormônios de Inseto/fisiologia
Proteínas de Insetos/metabolismo
Piridoxal Quinase/metabolismo
Fosfato de Piridoxal/biossíntese
Piridoxaminafosfato Oxidase/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Bombyx/efeitos dos fármacos
Bombyx/crescimento & desenvolvimento
China
Ecdisterona/antagonistas & inibidores
Ecdisterona/farmacologia
Ecdisterona/fisiologia
Corpo Adiposo/efeitos dos fármacos
Corpo Adiposo/crescimento & desenvolvimento
Corpo Adiposo/fisiologia
Regulação da Expressão Gênica no Desenvolvimento/efeitos dos fármacos
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Genes de Insetos/efeitos dos fármacos
Antagonistas de Hormônios/farmacologia
Hormônios de Inseto/antagonistas & inibidores
Hormônios de Inseto/farmacologia
Proteínas de Insetos/agonistas
Proteínas de Insetos/antagonistas & inibidores
Proteínas de Insetos/genética
Hormônios Juvenis/farmacologia
Hormônios Juvenis/fisiologia
Cinética
Larva/efeitos dos fármacos
Larva/crescimento & desenvolvimento
Larva/fisiologia
Piridoxal Quinase/antagonistas & inibidores
Piridoxal Quinase/química
Piridoxal Quinase/genética
Piridoxaminafosfato Oxidase/química
Piridoxaminafosfato Oxidase/genética
RNA Mensageiro/metabolismo
Glândulas Salivares/efeitos dos fármacos
Glândulas Salivares/crescimento & desenvolvimento
Glândulas Salivares/fisiologia
Sesquiterpenos/farmacologia
Transcrição Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hormone Antagonists); 0 (Insect Hormones); 0 (Insect Proteins); 0 (Juvenile Hormones); 0 (RNA, Messenger); 0 (Sesquiterpenes); 5289-74-7 (Ecdysterone); 5V5IOJ8338 (Pyridoxal Phosphate); B74U6BJ6J5 (juvenile hormone III); EC 1.4.3.5 (Pyridoxaminephosphate Oxidase); EC 2.7.1.35 (Pyridoxal Kinase)
[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


  5 / 202 MEDLINE  
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[PMID]:26092494
[Au] Autor:Kobayashi D; Yoshimura T; Johno A; Ishikawa M; Sasaki K; Wada K
[Ad] Endereço:Department of Food and Chemical Toxicology, School of Pharmaceutical Sciences, Health Sciences University of Hokkaido, Hokkaido, Japan.
[Ti] Título:Decrease in pyridoxal-5'-phosphate concentration and increase in pyridoxal concentration in rat plasma by 4'-O-methylpyridoxine administration.
[So] Source:Nutr Res;35(7):637-42, 2015 Jul.
[Is] ISSN:1879-0739
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Food poisoning from Ginkgo biloba seeds can cause epilepsy because of a decrease in γ-aminobutyric acid (GABA) concentrations in the brain. We previously demonstrated that 4'-O-methylpyridoxine (MPN) is responsible for this observed toxicity of G biloba seeds; however, the mechanism for the decrease in GABA and plasma concentration profile of MPN has not been clarified. Our hypothesis is that MPN induces a decrease in vitamin B6 concentrations, resulting in a decrease in GABA concentration. This study aimed to characterize the plasma concentration profile of MPN and intrinsic vitamin B6 concentrations (pyridoxal [PL], PL-5'-phosphate [PLP], and 4-pyridoxic acid) using a rat model. Plasma concentrations of B6 vitamers after intravenous MPN administration (5 mg/kg) were determined using high-performance liquid chromatography with a fluorescence detector. The half-life of MPN (0.91 ± 0.05 hours) was shorter in rats than the previously reported value in humans. We found a significant decrease in the plasma concentration of PLP, an active form of vitamin B6, after MPN administration. We also observed an increase in plasma PL and 4-pyridoxic acid concentrations; the increase in PL concentration may be caused by either metabolism of MPN to PL or by MPN-mediated inhibition of PL kinase. The present study is the first in vivo study showing relatively rapid elimination of MPN in rats and a decrease in plasma PLP concentration caused by MPN.
[Mh] Termos MeSH primário: Encéfalo/efeitos dos fármacos
Ginkgo biloba/química
Piridoxal Quinase/antagonistas & inibidores
Fosfato de Piridoxal/sangue
Piridoxina/análogos & derivados
Deficiência de Vitamina B 6/sangue
Ácido gama-Aminobutírico/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Modelos Animais de Doenças
Doenças Transmitidas por Alimentos/metabolismo
Ginkgo biloba/efeitos adversos
Seres Humanos
Masculino
Piridoxal/sangue
Fosfato de Piridoxal/deficiência
Ácido Piridóxico/sangue
Piridoxina/efeitos adversos
Piridoxina/sangue
Ratos Wistar
Sementes
Complexo Vitamínico B/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (4'-O-methylpyridoxine); 12001-76-2 (Vitamin B Complex); 3THM379K8A (Pyridoxal); 56-12-2 (gamma-Aminobutyric Acid); 5K18793O8D (Pyridoxic Acid); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.7.1.35 (Pyridoxal Kinase); KV2JZ1BI6Z (Pyridoxine)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150718
[Lr] Data última revisão:
150718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150621
[St] Status:MEDLINE


  6 / 202 MEDLINE  
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[PMID]:25655354
[Au] Autor:di Salvo ML; Nogués I; Parroni A; Tramonti A; Milano T; Pascarella S; Contestabile R
[Ad] Endereço:Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", "Sapienza" Università di Roma, Piazzale Aldo Moro 5, 00185 Roma, Italy.
[Ti] Título:On the mechanism of Escherichia coli pyridoxal kinase inhibition by pyridoxal and pyridoxal 5'-phosphate.
[So] Source:Biochim Biophys Acta;1854(9):1160-6, 2015 Sep.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pyridoxal 5'-phosphate (PLP), the catalytically active form of vitamin B6, plays a crucial role in several cellular processes. In most organisms, PLP is recycled from nutrients and degraded B6-enzymes in a salvage pathway that involves pyridoxal kinase (PLK), pyridoxine phosphate oxidase and phosphatase activities. Regulation of the salvage pathway is poorly understood. Escherichia coli possesses two distinct pyridoxal kinases, PLK1, which is the focus of the present work, and PLK2. From previous studies dating back to thirty years ago, pyridoxal (PL) was shown to inhibit E. coli PLK1 forming a covalent link with the enzyme. This inhibition was proposed to play a regulative role in vitamin B6 metabolism, although its details had never been clarified. Recently, we have shown that also PLP produced during PLK1 catalytic cycle acts as an inhibitor, forming a Schiff base with Lys229, without being released in the solvent. The question arises as to which is the actual inhibition mechanism by PL and PLP. In the present work, we demonstrated that also PL binds to Lys229 as a Schiff base. However, the isolated covalent PLK1-PL complex is not inactive but, in the presence of ATP, is able to catalyse the single turnover production of PLP, which binds tightly to the enzyme and is ultimately responsible for its inactivation. The inactivation mechanism mediated by Lys229 may play a physiological role in controlling cellular levels of PLP. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications.
[Mh] Termos MeSH primário: Escherichia coli/enzimologia
Piridoxal Quinase/antagonistas & inibidores
Fosfato de Piridoxal/farmacologia
Piridoxal/farmacologia
[Mh] Termos MeSH secundário: Catálise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
3THM379K8A (Pyridoxal); 5V5IOJ8338 (Pyridoxal Phosphate); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150207
[St] Status:MEDLINE


  7 / 202 MEDLINE  
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[PMID]:25421565
[Au] Autor:Liao S; Bitoun JP; Nguyen AH; Bozner D; Yao X; Wen ZT
[Ad] Endereço:Department of Oral and Craniofacial Biology, Louisiana State University Health Sciences Center, New Orleans, LA, USA.
[Ti] Título:Deficiency of PdxR in Streptococcus mutans affects vitamin B6 metabolism, acid tolerance response and biofilm formation.
[So] Source:Mol Oral Microbiol;30(4):255-68, 2015 Aug.
[Is] ISSN:2041-1014
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Streptococcus mutans, a key etiological agent of the human dental caries, lives primarily on the tooth surface in tenacious biofilms. The SMU864 locus, designated pdxR, is predicted to encode a member of the novel MocR/GabR family proteins, which are featured with a winged helix DNA-binding N-terminal domain and a C-terminal domain highly homologous to the pyridoxal phosphate-dependent aspartate aminotransferases. A pdxR-deficient mutant, TW296, was constructed using allelic exchange. PdxR deficiency in S. mutans had little effect on cell morphology and growth when grown in brain heart infusion. However, when compared with its parent strain, UA159, the PdxR-deficient mutant displayed major defects in acid tolerance response and formed significantly fewer biofilms (P < 0.01). When analyzed by real-time polymerase chain reaction, PdxR deficiency was found to drastically reduce expression of an apparent operon encoding a pyridoxal kinase (SMU865) and a pyridoxal permease (SMU866) of the salvage pathway of vitamin B6 biosynthesis. In addition, PdxR deficiency also altered the expression of genes for ClpL protease, glucosyltransferase B and adhesin SpaP, which are known to play important roles in stress tolerance and biofilm formation. Consistently, PdxR-deficiency affected the growth of the deficient mutant when grown in defined medium with and without vitamin B6 . Further studies revealed that although S. mutans is known to require vitamin B6 to grow in defined medium, B6 vitamers, especially pyridoxal, were strongly inhibitory at millimolar concentrations, against S. mutans growth and biofilm formation. Our results suggest that PdxR in S. mutans plays an important role in regulation of vitamin B6 metabolism, acid tolerance response and biofilm formation.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Biofilmes/crescimento & desenvolvimento
Streptococcus mutans/genética
Streptococcus mutans/metabolismo
Fatores de Transcrição/genética
Vitamina B 6/metabolismo
[Mh] Termos MeSH secundário: Adesinas Bacterianas/genética
Aminoácidos/metabolismo
Biofilmes/efeitos dos fármacos
Meios de Cultura/química
Regulação Bacteriana da Expressão Gênica
Glucosiltransferases/genética
Seres Humanos
Mutação
Óperon
Piridoxal/farmacologia
Piridoxal Quinase/genética
Reação em Cadeia da Polimerase em Tempo Real
Streptococcus mutans/efeitos dos fármacos
Streptococcus mutans/crescimento & desenvolvimento
Estresse Fisiológico/genética
Transaminases/genética
Fatores de Transcrição/metabolismo
Vitamina B 6/biossíntese
Vitamina B 6/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Amino Acids); 0 (Bacterial Proteins); 0 (Culture Media); 0 (Transcription Factors); 3THM379K8A (Pyridoxal); 8059-24-3 (Vitamin B 6); EC 2.4.1.- (1,3-alpha-D-glucan synthase); EC 2.4.1.- (Glucosyltransferases); EC 2.6.1.- (Transaminases); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:D
[Da] Data de entrada para processamento:141126
[St] Status:MEDLINE
[do] DOI:10.1111/omi.12090


  8 / 202 MEDLINE  
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[PMID]:24899377
[Au] Autor:Elsinghorst PW; di Salvo ML; Parroni A; Contestabile R
[Ad] Endereço:Pharmaceutical Chemistry I, Pharmaceutical Institute , University of Bonn, Bonn , Germany and.
[Ti] Título:Inhibition of human pyridoxal kinase by 2-acetyl-4-((1R,2S,3R)-1,2,3,4-tetrahydroxybutyl)imidazole (THI).
[So] Source:J Enzyme Inhib Med Chem;30(2):336-40, 2015 Apr.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:2-Acetyl-4-((1R,2S,3R)-1,2,3,4-tetrahydroxybutyl)imidazole (THI) is observed as a minor contaminant in caramel food colourings (E 150c). Feeding experiments with rodents have revealed a significant lymphopenic effect that has been linked to the presence of THI in these food colourings. Pyridoxal kinase inhibition by THI has been suggested, but not demonstrated, as a mode of action as it leads to lowered levels of pyridoxal-5'-phosphate, which are known to cause lymphopenia. Recently, THI was also shown to inhibit sphingosine-1-phosphate lyase causing comparable immunosuppressive effects and derivatives of THI are being developed for the treatment of rheumatoid arthritis in humans. Interestingly, sphingosine-1-phosphate lyase activity depends on pyridoxal-5'-phosphate, which in turn is provided by pyridoxal kinase. This report shows that THI does inhibit pyridoxal kinase with competitive and mixed-type non-competitive behaviour towards its two substrates, pyridoxal and ATP, respectively. The corresponding inhibition constants are in the low millimolar range.
[Mh] Termos MeSH primário: Corantes de Alimentos/farmacologia
Imidazóis/farmacologia
Piridoxal Quinase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Corantes de Alimentos/química
Seres Humanos
Imidazóis/química
Modelos Biológicos
Estrutura Molecular
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Food Coloring Agents); 0 (Imidazoles); 94944-70-4 (2-acetyl-4(5)-tetrahydroxybutylimidazole); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150403
[Lr] Data última revisão:
150403
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140606
[St] Status:MEDLINE
[do] DOI:10.3109/14756366.2014.915396


  9 / 202 MEDLINE  
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[PMID]:25372829
[Au] Autor:Kronenberger T; Lunev S; Wrenger C; Groves MR
[Ad] Endereço:Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Sciences, University of Saõ Paulo, Avenida Professor Lineu Prestes 1374, Saõ Paulo-SP 05508-000, Brazil.
[Ti] Título:Purification, crystallization and preliminary X-ray diffraction analysis of pyridoxal kinase from Plasmodium falciparum (PfPdxK).
[So] Source:Acta Crystallogr F Struct Biol Commun;70(Pt 11):1550-5, 2014 Nov.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyridoxal kinases (PdxK) catalyze the phosphorylation of vitamin B6 precursors. Thus, these enzymes are an essential part of many metabolic processes in all organisms. The protozoan parasite Plasmodium falciparum (the main causative agent of Malaria tropica) possesses a unique de novo B6-biosynthesis pathway in addition to a interconversion pathway based on the activity of plasmodial PdxK (PfPdxK). The role of PdxK in B6 salvage has prompted previous authors to suggest PdxK as a promising target for structure-based antimalarial drug design. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis of PfPdxK are reported. PfPdxK crystals have been grown in space group P21, with unit-cell parameters a=52.7, b=62.0, c=93.7 Å, ß=95°. A data set has been collected to 2 Šresolution and an initial molecular-replacement solution is described.
[Mh] Termos MeSH primário: Plasmodium falciparum/enzimologia
Proteínas de Protozoários/química
Proteínas de Protozoários/isolamento & purificação
Piridoxal Quinase/química
Piridoxal Quinase/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cristalização
Dados de Sequência Molecular
Estrutura Secundária de Proteína
Proteínas de Protozoários/genética
Piridoxal Quinase/genética
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protozoan Proteins); EC 2.7.1.35 (Pyridoxal Kinase)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141106
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X14019864


  10 / 202 MEDLINE  
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[PMID]:25157434
[Au] Autor:Kimura T; Shirakawa R; Yaoita N; Hayashi T; Nagano K; Horiuchi H
[Ad] Endereço:Department of Molecular and Cellular Biology, Institute of Development, Aging and Cancer, Tohoku University, 4-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan.
[Ti] Título:The antimalarial drugs chloroquine and primaquine inhibit pyridoxal kinase, an essential enzyme for vitamin B6 production.
[So] Source:FEBS Lett;588(20):3673-6, 2014 Oct 16.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Quinoline derivatives such as chloroquine and primaquine are widely used for the treatment of malaria. These drugs are also used for the treatment of trypanosomiasis, and more recently for cancer therapy. However, molecular target(s) of these drugs remain unclear. In this study, we have identified human pyridoxal kinase as a binding protein of primaquine. Primaquine inhibited pyridoxal kinases of malaria, trypanosome and human, while chloroquine inhibited only malaria pyridoxal kinase. Thus, we have identified pyridoxal kinase as a possible target molecule of the antimalarial drugs chloroquine and primaquine.
[Mh] Termos MeSH primário: Antimaláricos/farmacologia
Cloroquina/farmacologia
Inibidores Enzimáticos/farmacologia
Primaquina/farmacologia
Proteínas de Protozoários/antagonistas & inibidores
Piridoxal Quinase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
Plasmodium vivax/enzimologia
Ligação Proteica
Proteínas de Protozoários/metabolismo
Piridoxal Quinase/metabolismo
Especificidade por Substrato
Trypanosoma cruzi/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimalarials); 0 (Enzyme Inhibitors); 0 (Protozoan Proteins); 886U3H6UFF (Chloroquine); EC 2.7.1.35 (Pyridoxal Kinase); MVR3634GX1 (Primaquine)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:140926
[Lr] Data última revisão:
140926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140827
[St] Status:MEDLINE



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