(Q44009258)

English

Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity an

scientific article published on 28 May 2002

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Europe PubMed Central

PubMed publication ID

28 November 2017

Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity an (English)

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Europe PubMed Central

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28 November 2017

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transmembrane protein

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Escherichia coli

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Paul N Black

4

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James D Weimar

1

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Europe PubMed Central

PubMed publication ID

28 November 2017

Concetta C DiRusso

2

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Europe PubMed Central

PubMed publication ID

28 November 2017

Raymond Delio

3

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Europe PubMed Central

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28 November 2017

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publication date

28 May 2002

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28 November 2017

Journal of Biological Chemistry

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28 November 2017

277

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Europe PubMed Central

PubMed publication ID

28 November 2017

33

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Europe PubMed Central

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28 November 2017

29369-29376

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Europe PubMed Central

PubMed publication ID

28 November 2017

Possible role for fatty acyl-coenzyme A in intracellular protein transport

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Fatty acylation promotes fusion of transport vesicles with Golgi cisternae

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Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

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Regulation of transcription of genes required for fatty acid transport and unsaturated fatty acid biosynthesis in Escherichia coli by FadR.

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21 January 2018

The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR

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21 January 2018

Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold

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Molecular inroads into the regulation and metabolism of fatty acids, lessons from bacteria

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The kinetics of enzyme-catalyzed reactions with two or more substrates or products

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21 January 2018

The kinetics of enzyme-catalyzed reactions with two or more substrates or products

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21 January 2018

Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity.

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Multiple sequence alignment with hierarchical clustering

1 reference

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Evidence that His110 of the protein FadL in the outer membrane of Escherichia coli is involved in the binding and uptake of long-chain fatty acids: possible role of this residue in carboxylate binding.

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Substitution of alanine for serine 250 in the murine fatty acid transport protein inhibits long chain fatty acid transport

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Molecular aspects of fatty acid transport: mutations in the IYTSGTTGXPK motif impair fatty acid transport protein function

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Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S

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Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes

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21 January 2018

Affinity labeling fatty acyl-CoA synthetase with 9-p-azidophenoxy nonanoic acid and the identification of the fatty acid-binding site.

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Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases.

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Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases

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Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis

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21 January 2018

Energetics underlying the process of long-chain fatty acid transport

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The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization.

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Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4α

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21 January 2018

Identifiers

10.1074/JBC.M107022200

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

28 November 2017

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