Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria
about
Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomicsIdentification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)Flavoenzymes: versatile catalysts in biosynthetic pathwaysComplex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3Role of feedback regulation of pantothenate kinase (CoaA) in control of coenzyme A levels in Escherichia coliInhibitors of pantothenate kinase: novel antibiotics for staphylococcal infectionsThe structure of the pantothenate kinase.ADP.pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolitesGermline deletion of pantothenate kinases 1 and 2 reveals the key roles for CoA in postnatal metabolismDrosophila phosphopantothenoylcysteine synthetase is required for tissue morphogenesis during oogenesis.Identification, purification, and characterization of an eukaryotic-like phosphopantetheine adenylyltransferase (coenzyme A biosynthetic pathway) in the hyperthermophilic archaeon Pyrococcus abyssi.Gene essentiality, conservation index and co-evolution of genes in cyanobacteriaCharacterization and kinetics of phosphopantothenoylcysteine synthetase from Enterococcus faecalis.Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial dfp flavoproteins.Elevated levels of ketopantoate hydroxymethyltransferase (PanB) lead to a physiologically significant coenzyme A elevation in Salmonella enterica serovar Typhimurium.Identification of the gene cluster for the dithiolopyrrolone antibiotic holomycin in Streptomyces clavuligerus.The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.Biosynthesis of Pantothenic Acid and Coenzyme A.The human malaria parasite Plasmodium falciparum is not dependent on host coenzyme A biosynthesis.Selective inhibitors of bacterial phosphopantothenoylcysteine synthetase.Molecular characterization of the Arabidopsis thaliana flavoprotein AtHAL3a reveals the general reaction mechanism of 4'-phosphopantothenoylcysteine decarboxylases.Molecular characterization of the 4'-phosphopantothenoylcysteine decarboxylase domain of bacterial Dfp flavoproteins.The flavoprotein MrsD catalyzes the oxidative decarboxylation reaction involved in formation of the peptidoglycan biosynthesis inhibitor mersacidinAntibiotic evaluation and in vivo analysis of alkynyl Coenzyme A antimetabolites in Escherichia coli.Acetyl-4'-phosphopantetheine is stable in serum and prevents phenotypes induced by pantothenate kinase deficiency.Pantethine rescues phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase deficiency in Escherichia coli but not in Pseudomonas aeruginosa.Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites.The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme a, a coenzyme a antimetabolite.4'-phosphopantetheine and coenzyme A biosynthesis in plants.De novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous system.4'-phosphopantetheine biosynthesis in Archaea.An Arabidopsis mutant impaired in coenzyme A biosynthesis is sugar dependent for seedling establishment.Fosmetpantotenate (RE-024), a phosphopantothenate replacement therapy for pantothenate kinase-associated neurodegeneration: Mechanism of action and efficacy in nonclinical models.Mutations at the hydrophobic core affect Hal3 trimer stability, reducing its Ppz1 inhibitory capacity but not its PPCDC moonlighting function
P2860
Q24292910-42A132E1-3E2A-4815-AF26-CC2B6BCCDE25Q24296719-221E46E3-CBC7-4487-A244-B8960A2C44B7Q27022878-C60F59DA-9B1F-46FE-B161-D1FB4CB686B4Q27933972-FDE74CD2-971C-4D34-9B0F-9863D4EA111DQ28204877-84A8FB52-CD78-4548-AFB6-9CFFD268C22CQ28205718-65ACF9CE-B13F-4537-A1CC-CF47A3D4DD23Q28261114-9C066482-6903-413A-8CFE-6D11BE7F108FQ28509589-83C4AFE6-6A39-4BD5-A208-369372CA5686Q30847483-E2C4073C-B2AE-4533-998B-2848802A54E1Q30934265-5A7EF08D-2443-4EA8-8BFF-9AE943217547Q33778541-B04E8A2B-CC33-4374-8347-3E6C82F59331Q33941188-D8CF6A89-A2C1-486B-A730-7F47C95CFE61Q34141178-C039A374-A58D-436D-AA9A-404A179A1DFFQ34311303-BE5918A1-40B1-4B7C-9D4F-383EFB2C45AAQ34359207-2913126E-42C2-4462-B851-99019C273971Q35992631-A47F4DC7-1F39-400B-9E2D-80FBC4034332Q37108988-FBFBDA7C-7FB7-4834-8943-279C75E738DEQ37375676-F594F4C1-3404-4DFF-8EF4-65C5C55FE54FQ37453777-6B7D8943-C271-4539-B1EE-A486010B91ADQ38290697-F9EE6B9F-4A72-409B-973C-808FA8D9A621Q38300646-C273C79D-DCB5-419B-B4D5-991098E7C4D1Q39678311-DE39D566-B425-4F61-B761-EB5C4FB4C5A6Q40778891-5AB459DE-BE6D-492E-9B01-8B7F7869C661Q41199152-ACFE210B-678F-4DE0-B5A6-C0E1744477ABQ42793378-A9FB4367-3B28-4344-BA07-606D44157279Q43628197-6A587503-F85D-490B-A5D1-FDD9AF7F097AQ44174357-2A2DB295-8067-40A5-8734-E80B0B6ACD46Q44513250-1D89DE75-930F-4895-A2DC-D075355E2BC4Q46648320-DF08DF70-AD0E-4C08-8E07-B100CFA02FCFQ46863328-68DDFE41-B9DD-4923-92FF-AF553DF1519AQ46895662-04F53510-70C7-40B6-A0F6-AA69981D55DFQ52664420-216C2486-1C2F-43ED-9A0E-3FDB8EB194F4Q57050462-D254F3D9-5CD0-40FA-BE19-48A5D0EA61DB
P2860
Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria
description
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2001
@ast
im April 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2001/04/27)
@sk
vědecký článek publikovaný v roce 2001
@cs
wetenschappelijk artikel (gepubliceerd op 2001/04/27)
@nl
наукова стаття, опублікована у квітні 2001
@uk
name
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@ast
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@en
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@nl
type
label
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@ast
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@en
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@nl
prefLabel
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@ast
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@en
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@nl
P2093
P2860
P356
P1476
Phosphopantothenoylcysteine sy ...... iosynthetic enzyme in bacteria
@en
P2093
C. Kinsland
E. Strauss
F. W. McLafferty
T. P. Begley
P2860
P304
13513–13516
P356
10.1074/JBC.C100033200
P407
P577
2001-04-27T00:00:00Z