The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme a, a coenzyme a antimetabolite.
about
Potential Molecular Targets for Narrow-Spectrum Agents to Combat Mycoplasma pneumoniae Infection and DiseaseLocation and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme actionCrystal structures of Klebsiella pneumoniae pantothenate kinase in complex with N-substituted pantothenamidesComplex stability and dynamic subunit interchange modulates the disparate activities of the yeast moonlighting proteins Hal3 and Vhs3Inhibitors of pantothenate kinase: novel antibiotics for staphylococcal infectionsCharacterization of a new pantothenate kinase isoform from Helicobacter pyloriCrystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteriaThe structure of the pantothenate kinase.ADP.pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolitesStructural modification of pantothenamides counteracts degradation by pantetheinase and improves antiplasmodial activityAntibacterial activity of N-pentylpantothenamide is due to inhibition of coenzyme a synthesisMechanistic insight with HBCH2CoA as a probe to polyhydroxybutyrate (PHB) synthasesA class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasitesThiolase engineering for enhanced butanol production in Clostridium acetobutylicum.Pantothenamides are potent, on-target inhibitors of Plasmodium falciparum growth when serum pantetheinase is inactivatedGeminal dialkyl derivatives of N-substituted pantothenamides: synthesis and antibacterial activity.Synthesis of 4'-aminopantetheine and derivatives to probe aminoglycoside N-6'-acetyltransferaseFunctional copper at the acetyl-CoA synthase active siteExploring structural motifs necessary for substrate binding in the active site of Escherichia coli pantothenate kinase.The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.Inhibiting bacterial fatty acid synthesis.Chemoenzymatic Synthesis of Acyl Coenzyme A Substrates Enables in Situ Labeling of Small Molecules and Proteins.Functional Dissection of the Bipartite Active Site of the Class I Coenzyme A (CoA)-Transferase Succinyl-CoA:Acetate CoA-Transferase.A cross-metathesis approach to novel pantothenamide derivatives.Biosynthesis of Pantothenic Acid and Coenzyme A.The human malaria parasite Plasmodium falciparum is not dependent on host coenzyme A biosynthesis.Inhibitors of aminoglycoside resistance activated in cells.Understanding and overcoming aminoglycoside resistance caused by N-6'-acetyltransferase.Stereochemical modification of geminal dialkyl substituents on pantothenamides alters antimicrobial activityRecent advances in targeting coenzyme A biosynthesis and utilization for antimicrobial drug development.Exploiting the coenzyme A biosynthesis pathway for the identification of new antimalarial agents: the case for pantothenamides.Inhibitors of polyhydroxyalkanoate (PHA) synthases: synthesis, molecular docking, and implications.In vivo modification of native carrier protein domains.Novel pantothenate derivatives for anti-malarial chemotherapy.Antibiotic evaluation and in vivo analysis of alkynyl Coenzyme A antimetabolites in Escherichia coli.Metabolic perturbation of an essential pathway: evaluation of a glycine precursor of coenzyme A.In vivo cloning of up to 16 kb plasmids in E. coli is as simple as PCR.Combination of pantothenamides with vanin inhibitors as a novel antibiotic strategy against gram-positive bacteria.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 selectivity for cysteine over serine in coenzyme A biosynthesis.
P2860
Q26768548-A7FB5606-B6E4-445F-AF11-0CAA4128EEF3Q27673462-02E2CB68-5177-4153-8F1A-E741DF5023AAQ27684357-7EDA20BE-BE04-4004-BE7D-550413989020Q27933972-D9165E78-2CDD-4A78-8D73-B2992AFB95F9Q28205718-58EC1A62-952D-4E11-81B9-D0BF7A238DA3Q28242022-12814018-30B0-4B8B-B0B3-AD3F641DC988Q28252916-5F2705A9-BBD4-423E-9790-CD2B2CC44F8DQ28261114-E407F30C-900A-44BC-9868-99A1A4D9C715Q33636093-5D446A80-8333-4F80-8021-03512829CE1BQ33676334-BEC713AD-D899-4A29-991B-28AF9D08CF67Q34061280-3E228D02-0828-4B96-9DD7-035931159D63Q34123671-8D527121-E76C-4BD0-9FA3-28E2BF22719BQ34457519-CE77047B-85B1-4AC4-AE4A-B9354C93B689Q34584014-09D8A08A-B4DB-4A6E-817F-51F540BCB6ACQ34881968-7F766D08-087A-4035-AC7B-3F2A4E7C4087Q34882031-1FED6665-E6CB-44BB-BC87-B72CC429F3CAQ34915407-5131D8BC-FF6D-48E5-B9AD-4A8C0BB13D3FQ35166199-96DB2C93-8CF7-41B4-844E-4CD59A214A7FQ35992631-1EAA895E-C779-4B15-9DF5-532A8482398CQ36464020-9AC454AA-3433-433B-894F-0D6726619DFEQ36482701-6AC00FFA-6946-454B-806B-B93EAED8BDFDQ36924526-F759F493-EB54-43EA-B897-6B3E2F3B71A8Q36992106-14B59F73-95E8-41F6-AE3A-B025EE19D7A3Q37108988-29364316-75DA-4158-BEBA-C217B0EFC675Q37375676-9FD36331-B991-48E1-9A6A-7A1C46804655Q37525084-484AA86E-5365-4E8A-9FDA-BC4D8A9A06CEQ37528001-0792F977-CE7E-4533-B17F-1B03FB948CE2Q37580696-25E7B7A3-9912-4FC8-A9A1-F1D8E3C1D378Q38238659-758354D5-FBEB-4970-ADA8-C9D04BD45169Q38238661-F5D1EA09-2F9F-4043-98F4-75F037BDF322Q39460137-64A7CE85-E0E6-4EFB-9D86-68F1B11B93EEQ39869076-7E1D9E80-65FD-41FA-B2E6-F5B47580AE34Q40484106-F8E1077A-0E23-40C7-B6F2-DC757C095736Q40778891-39365E8B-1563-4308-8862-5A7BEF7D376BQ40814956-FFE58B28-2EF0-442B-B71C-B397DF3DBDF7Q41512624-F2A23BF3-8BD5-4DE4-9BB8-91A16B6BBB11Q41976407-C2D62744-17B8-49CB-AC97-7C5205594FA7Q42793378-1A3B4716-5C83-4942-BDB4-116CA12ED7AAQ43628197-2BF34C8F-A300-46B2-B371-D43A253293FBQ45184137-767A5D33-1EDB-451D-BC37-65461A2FD130
P2860
The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme a, a coenzyme a antimetabolite.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@en
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@nl
type
label
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@en
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@nl
prefLabel
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@en
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@nl
P2860
P356
P1476
The antibiotic activity of N-p ...... , a coenzyme a antimetabolite.
@en
P2093
Tadhg P Begley
P2860
P304
48205-48209
P356
10.1074/JBC.M204560200
P407
P577
2002-10-07T00:00:00Z