Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.
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Mechanism and substrate recognition of human holo ACP synthaseBiochemical and structural characterization of germicidin synthase: analysis of a type III polyketide synthase that employs acyl-ACP as a starter unit donorStructure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesisStructural Insight into the Tetramerization of an Iterative Ketoreductase SiaM through Aromatic Residues in the InterfacesMalonyl-CoA: acyl carrier protein transacylase fromHelicobacter pylori: Crystal structure and its interaction with acyl carrier proteinSolution structure and proposed domain-domain recognition interface of an acyl carrier protein domain from a modular polyketide synthaseA mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chainsStructural basis for catalytic and inhibitory mechanisms of beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ)Inhibition Kinetics and Emodin Cocrystal Structure of a Type II Polyketide Ketoreductase † , ‡Structural characterization of CalO2: A putative orsellinic acid P450 oxidase in the calicheamicin biosynthetic pathwayStructural modification of acyl carrier protein by butyryl groupCharacterization of Molecular Interactions between ACP and Halogenase Domains in the Curacin A Polyketide SynthaseStructure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone InhibitorsBiochemical and Structural Studies of NADH-Dependent FabG Used To Increase the Bacterial Production of Fatty Acids under Anaerobic ConditionsStructure 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 dehydrogenaseStructure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanismUsing modern tools to probe the structure-function relationship of fatty acid synthasesAcyl carrier protein: structure-function relationships in a conserved multifunctional protein family.Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis.Structural enzymology of polyketide synthases.Gene-specific random mutagenesis of Escherichia coli in vivo: isolation of temperature-sensitive mutations in the acyl carrier protein of fatty acid synthesis.Disrupting the Acyl Carrier Protein/SpoT interaction in vivo: identification of ACP residues involved in the interaction and consequence on growthMolecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase.Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.Ralstonia 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 megasynthasesSecreted Acb1 Contributes to the Yeast-to-Hypha Transition in Cryptococcus neoformansStructure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coliStructural analysis of protein-protein interactions in type I polyketide synthasesStructural insights into the acyl intermediates of the Plasmodium falciparum fatty acid synthesis pathway: the mechanism of expansion of the acyl carrier protein core.Revisiting the modularity of modular polyketide synthases.Current understanding of fatty acid biosynthesis and the acyl carrier protein.Structure and function of eukaryotic fatty acid synthases.The structural role of the carrier protein--active controller or passive carrier.A high yield optimized method for the production of acylated ACPs enabling the analysis of enzymes involved in P. falciparum fatty acid biosynthesis.Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction.Substrate recognition by β-ketoacyl-ACP synthases.Probing the Substrate Specificity and Protein-Protein Interactions of the E. coli Fatty Acid Dehydratase, FabA.
P2860
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P2860
Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Key residues responsible for a ...... reductase (FabG) interaction.
@en
Key residues responsible for a ...... acyl carrier protein reductase
@nl
type
label
Key residues responsible for a ...... reductase (FabG) interaction.
@en
Key residues responsible for a ...... acyl carrier protein reductase
@nl
prefLabel
Key residues responsible for a ...... reductase (FabG) interaction.
@en
Key residues responsible for a ...... acyl carrier protein reductase
@nl
P2093
P2860
P356
P1476
Key residues responsible for a ...... reductase (FabG) interaction.
@en
P2093
Charles O Rock
Yong-Mei Zhang
P2860
P304
52935-52943
P356
10.1074/JBC.M309874200
P407
P50
P577
2003-10-03T00:00:00Z