Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis
about
Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinasesBacterial lipids: metabolism and membrane homeostasisStructure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthaseCosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putidaCrystal structure of a carbonyl reductase fromCandida parapsilosiswith anti-Prelog stereospecificitySolution Structure of 4′-Phosphopantetheine - GmACP3 from Geobacter metallireducens : A Specialized Acyl Carrier Protein with Atypical Structural Features and a Putative Role in Lipopolysaccharide BiosynthesisStructure of 3-ketoacyl-(acyl-carrier-protein) reductase from Rickettsia prowazekii at 2.25 Å resolutionCrystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal FabG1 in positive cooperativity for NADPHThe T4 Phage SF1B Helicase Dda Is Structurally Optimized to Perform DNA Strand SeparationDiscovery of an Allosteric Inhibitor Binding Site in 3-Oxo-acyl-ACP Reductase from Pseudomonas aeruginosaStructure of a short-chain dehydrogenase/reductase from Bacillus anthracisCrystal structure of hexanoyl-CoA bound to β-ketoacyl reductase FabG4 of Mycobacterium tuberculosisInsights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenaseUsing modern tools to probe the structure-function relationship of fatty acid synthasesA new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae3-oxoacyl-ACP reductase from Schistosoma japonicum: integrated in silico-in vitro strategy for discovering antischistosomal lead compoundsStructural Characterisation of FabG from Yersinia pestis, a Key Component of Bacterial Fatty Acid SynthesisIsolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar TyphimuriumIn vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coliDissecting the Structural Elements for the Activation of β-Ketoacyl-(Acyl Carrier Protein) Reductase from Vibrio cholerae.Structural elucidation of chalcone reductase and implications for deoxychalcone biosynthesis.Structural enzymology of polyketide synthases.BdcA, a protein important for Escherichia coli biofilm dispersal, is a short-chain dehydrogenase/reductase that binds specifically to NADPH.Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA)A type II pathway for fatty acid biosynthesis presents drug targets in Plasmodium falciparum.Haemophilus influenzae Rd lacks a stringently conserved fatty acid biosynthetic enzyme and thermal control of membrane lipid composition.Fatty acid biosynthesis as a target for novel antibacterialsRalstonia solanacearum fatty acid composition is determined by interaction of two 3-ketoacyl-acyl carrier protein reductases encoded on separate replicons.The type I fatty acid and polyketide synthases: a tale of two megasynthasesCrystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5Identification, cloning, and characterization of a novel ketoreductase from the cyanobacterium Synechococcus sp. strain PCC 7942Structural analysis of protein-protein interactions in type I polyketide synthasesIdentification of the polyhydroxyalkanoate (PHA)-specific acetoacetyl coenzyme A reductase among multiple FabG paralogs in Haloarcula hispanica and reconstruction of the PHA biosynthetic pathway in Haloferax volcanii.Structure and function of eukaryotic fatty acid synthases.Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents.Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.FabG can function as PhaB for poly-3-hydroxybutyrate biosynthesis in photosynthetic cyanobacteria Synechocystis sp. PCC 6803.Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis.Crystallization and preliminary X-ray diffraction analysis of the high molecular weight ketoacyl reductase FabG4 complexed with NADH.Identification of the Leishmania major proteins LmjF07.0430, LmjF07.0440, and LmjF27.2440 as components of fatty acid synthase II.
P2860
Q24609350-3E8F476D-3DB4-4FA0-BA5D-E95FF21353D8Q26829512-1DD5FD20-EB75-4186-9FAF-4F3C5839DE2CQ27641290-3CB34F7B-B7B8-4E32-BED2-3D976D8F090AQ27648884-EA6F5BEF-FA42-452C-9B97-F87D90AA8D8DQ27650898-FAA10D6C-D7F3-462F-97CD-C0C9ED4285B3Q27666583-174769ED-0673-4786-A0AE-F8CB6274A596Q27673602-0EEE14EF-8897-49AA-A4C1-8E3B7EC29BEEQ27676871-C3487FBD-1C8A-4617-9220-F02B69744E2BQ27679439-9A9EFB23-7B43-4348-B47C-1E74CA58A5DAQ27679901-156F6C7B-5A0E-4EEB-A52D-D06E155B5186Q27681078-1A586C54-4219-4878-9D79-1C9B156C7F7BQ27683485-0FF30B23-15E1-45A9-8956-0D2FA45548B9Q27695594-0A53A213-B528-4BD7-9423-70653E53E672Q28080940-CB578CD6-7795-49D7-B545-2A62C411F72DQ28485210-D17792AA-F4D1-451A-B43B-A787DEEDD7DFQ28533754-4532F2C2-A8B9-4B3C-B43E-6D43481D20B0Q28550728-E4591A4F-CB90-4724-A57B-9B077463319DQ28563574-D84F8AA5-2481-4C56-B21D-6A1114FC3254Q28742590-BF18561C-99F9-4F15-81EE-CD96C27DFB29Q30278363-9F6C9872-A991-49B2-9755-7201E958DDF8Q30350920-511B53B5-4E21-4F87-88CE-85B8982C2308Q33862817-C27ACBD9-0D2C-496F-8712-9137599F4A4CQ34224463-4EAEABEC-D3B3-4C4E-8B46-1545265FAD61Q34420138-E19DD559-75DE-42E9-B79F-C78634085214Q34722217-C4DD0888-85F2-4E90-AD7A-547577583802Q35172330-CE44E851-B90B-404A-961E-D5CB0D59863AQ35713880-C1A04CAD-2999-4E48-B558-0573DDE884EFQ35816769-A7CA0A2B-C3AB-40BA-8C9F-5F66CEE53C75Q36489362-526219FD-3B8A-47C4-9DD7-D05ADB5FD979Q36580432-5408420C-546C-4C6E-A628-F8B419B13BA5Q36958115-6386AEEA-48DB-4D93-8A6E-383FB113F200Q37352218-245176C2-C05A-45CD-A550-3B6E18A29D6EQ37365266-C68061B6-F29A-4B72-84D8-78CEB4581E4AQ37781847-EF87A52C-4411-4205-83B8-F15F70D9B9BCQ38124842-D0C99A4B-3415-477F-B599-BC4E3954F36DQ38264138-91F75136-DF72-4D8C-B341-8F9B3150085BQ38791927-BEAA9FAF-0E94-4B80-9DD1-7C2189409805Q41390034-8C715EAB-9ED4-4BF9-B8B5-99471FE1E7BAQ41913837-7021AFEB-010E-44FF-892F-6058CCB56150Q42084175-613D6676-4843-47F1-8C42-A72D34F1450A
P2860
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@ast
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@en
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@nl
type
label
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@ast
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@en
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@nl
prefLabel
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@ast
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@en
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@nl
P2093
P356
P1433
P1476
Structure of beta-ketoacyl-[ac ...... ivity and its structural basis
@en
P2093
P304
P356
10.1021/BI010737G
P407
P577
2001-10-30T00:00:00Z