Acyl Carrier Protein (ACP) (65-74) is an active acyl carrier protein (ACP) fragment.
CAT No: R1160
CAS No:66851-75-0
Synonyms/Alias:Acyl carrier protein (65-74);66851-75-0;Acp (65-74);DTXSID90216976;Acyl Carrier Protein (ACP) (65-74);Glycine, N-(N2-(N-(N-(N-(N-(N-(N-(N2-L-valyl-L-glutaminyl)-L-alanyl)-L-alanyl)-L-isoleucyl)-L-alpha-aspartyl)-L-tyrosyl)-L-isoleucyl)-L-asparaginyl)-;Acyl Carrier Protein (ACP) 65-74;DTXCID20139467;G12523;
Acyl Carrier Protein (ACP) 65-74 is a synthetic peptide fragment corresponding to amino acid residues 65 through 74 of the acyl carrier protein, a central component in fatty acid biosynthesis across prokaryotic and eukaryotic organisms. As a well-defined segment of ACP, this peptide represents a region critical for protein-protein interactions and post-translational modifications, particularly those involving the phosphopantetheinyl arm essential for acyl group transfer. Its sequence and structural features make it a valuable tool for dissecting the molecular mechanisms underlying fatty acid metabolism, enzyme recognition, and the regulation of biosynthetic pathways. The availability of this defined peptide fragment enables researchers to study specific domains of ACP in isolation, facilitating targeted investigations into its biochemical roles.
Protein-Protein Interaction Studies: The ACP 65-74 peptide is widely utilized to probe the interaction interfaces between acyl carrier protein and its partner enzymes within the fatty acid synthase complex. By isolating this segment, researchers can map binding sites, characterize affinity determinants, and elucidate the contribution of the C-terminal region to the assembly and function of multi-enzyme complexes. Such studies provide mechanistic insights into how ACP orchestrates substrate channeling and enzyme dynamics during fatty acid elongation.
Enzyme Recognition and Substrate Specificity: Investigations into the specificity of acyltransferases, thioesterases, and other ACP-interacting enzymes often rely on synthetic peptide fragments like ACP 65-74. This peptide serves as a minimal recognition element, allowing detailed analysis of the structural and chemical features required for selective binding and catalysis. It enables the design of biochemical assays to quantify enzyme activity, measure kinetic parameters, and screen for modulators that affect ACP-dependent processes.
Phosphopantetheinylation Research: The 65-74 region of ACP encompasses the conserved serine residue that undergoes phosphopantetheinylation, a post-translational modification essential for ACP function. Utilizing this peptide, researchers can reconstitute enzymatic modification reactions in vitro, study the substrate preferences of phosphopantetheinyl transferases, and monitor the efficiency of cofactor attachment. Such experimental systems are instrumental in clarifying the molecular basis of ACP activation and the regulation of fatty acid biosynthesis.
Structural Biology and Peptide Conformation: ACP 65-74 provides a model system for investigating the conformational properties of ACP domains using spectroscopic and crystallographic techniques. By studying the isolated peptide, scientists can explore secondary structure tendencies, flexibility, and the impact of specific amino acid substitutions on folding and stability. These structural insights inform broader understanding of ACP dynamics and its adaptability within biosynthetic assemblies.
Analytical and Detection Tool: As a chemically defined peptide, ACP 65-74 is frequently employed as a standard or probe in analytical methods such as mass spectrometry, immunoassays, and affinity chromatography. Its use facilitates the calibration of detection platforms, validation of antibody specificity, and identification of ACP-related fragments in complex biological samples. This application supports the development of sensitive assays for monitoring ACP expression, modification state, or interaction partners in diverse research settings.
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