Acyl carrier protein

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'''Acyl carrier protein''' (ACP) is a component of the fatty acid biosynthesis cycle. ACP catalyzes the addition of a thioester to a phosphopantetheine moiety. The phosphopantetheine moiety is added post-translationally to ACP serine residue by ACP synthetase (ACPS). The phosphopantetheine contains a free SH group which binds acyl groups in the fatty acid biosynthesis as thioesters. The acyl groups from acetyl-CoA and malonyl-CoA are transferred to ACP. There are 2 types of ACP. '''ACP I''' is a multifunctional polypeptide found in yeast and mammals while '''ACP II''' is a monomeric protein found in bacteria and plants.<ref>PMID:18059524</ref>
'''Acyl carrier protein''' (ACP) is a component of the fatty acid biosynthesis cycle. ACP catalyzes the addition of a thioester to a phosphopantetheine moiety. The phosphopantetheine moiety is added post-translationally to ACP serine residue by ACP synthetase (ACPS). The phosphopantetheine contains a free SH group which binds acyl groups in the fatty acid biosynthesis as thioesters. The acyl groups from acetyl-CoA and malonyl-CoA are transferred to ACP. There are 2 types of ACP. '''ACP I''' is a multifunctional polypeptide found in yeast and mammals while '''ACP II''' is a monomeric protein found in bacteria and plants.<ref>PMID:18059524</ref>
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See also [[Molecular Playground/ACP apo]]
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See also:
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*[[Molecular Playground/ACP apo]]
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*[[Acyl carrier protein synthase]]
== Structural highlights ==
== Structural highlights ==

Revision as of 09:59, 19 December 2019

Structure of E. coli acyl carrier protein complex with thioester, Zn+2 (grey) and Na+ (purple) ions (PDB code 2fad).

Drag the structure with the mouse to rotate

References

  1. Byers DM, Gong H. Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family. Biochem Cell Biol. 2007 Dec;85(6):649-62. PMID:18059524 doi:http://dx.doi.org/10.1139/o07-109
  2. Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR. Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates. J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829 doi:10.1016/j.jmb.2006.09.049

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