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Mitochondrial Acyl Carrier Protein of Displays Features Distinct from the Canonical Type II ACP.
Biochemistry
December 2023
National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110 067, India.
Article Synopsis
- * Comparison of mitochondrial ACP with bacterial and plastid types reveals unique structural differences, particularly in helices and loops, influencing the properties of ACP, like hydrophobic to hydrophilic residue substitutions.
- * NMR studies indicate that while ACP's cavity size changes minimally upon acylation, mutations in critical structural residues can dramatically affect its stability and function, emphasizing the importance of understanding these variations across organisms.
Atomistic insight on structure and dynamics of spinach acyl carrier protein with substrate length.
Biophys J
September 2021
Pacific Northwest National Laboratory, Physical and Computational Sciences Directorate, Richland, Washington.
Article Synopsis
- The plant acyl-acyl carrier protein (ACP) desaturases are essential enzymes that convert saturated fatty acids into monounsaturated ones, influencing fatty acid biosynthesis in plants.
- Researchers studied the dynamics and structure of spinach ACP with various acyl chains, finding that different fatty acids can form two distinct binding structures that affect ACP's activity.
- Molecular simulations indicate that the interactions between ACP and different desaturases could affect which binding motif is preferred, potentially altering enzymatic efficiency.
Modeling holo-ACP:DH and holo-ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study.
BMC Struct Biol
May 2012
Bioinformatics Center, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Background: Modular polyketide synthases are multifunctional megasynthases which biosynthesize a variety of secondary metabolites using various combinations of dehydratase (DH), ketoreductase (KR) and enoyl-reductase (ER) domains. During the catalysis of various reductive steps these domains act on a substrate moiety which is covalently attached to the phosphopantetheine (P-pant) group of the holo-Acyl Carrier Protein (holo-ACP) domain, thus necessitating the formation of holo-ACP:DH and holo-ACP:KR complexes. Even though three dimensional structures are available for DH, KR and ACP domains, no structures are available for DH or KR domains in complex with ACP or substrate moieties.
View Article and Find Full Text PDFSubstrate selectivity of glycerol-3-phosphate acyl transferase in rice.
J Integr Plant Biol
November 2009
School of Life Sciences, Nantong University, Nantong 226007, China.
Substrate selectivity of glycerol-3-phosphate acyltransferase (EC 2. 3. 1.
View Article and Find Full Text PDFCharacterization of a new stearoyl-acyl carrier protein desaturase gene from Jatropha curcas.
Biotechnol Lett
May 2006
College of Life Sciences, Sichuan University, Chengdu, China.
A new full-length cDNA of stearoyl-acyl carrier protein desaturase was obtained by RT-PCR and RACE techniques from developing seeds of Jatropha curcas. Sequence alignment showed that its deduced amino acid sequence had high similarity with other stearoyl-acyl carrier protein desaturases. The gene was functionally expressed in E.
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