Details
| Original language | English |
|---|---|
| Pages (from-to) | 463-471 |
| Number of pages | 9 |
| Journal | Organic and Biomolecular Chemistry |
| Volume | 1 |
| Issue number | 3 |
| Publication status | Published - 7 Feb 2003 |
| Externally published | Yes |
Abstract
While X-ray and NMR structures are now available for most components of the Type II fatty acid synthase (FAS), there are no structures for Type I FAS domains. A region from the mammalian (rat) FAS, including the putative acyl carrier protein (ACP), has been cloned and over-expressed. Here we report multinuclear, multidimensional NMR studies which show that this isolated ACP domain contains four α-helices (residues 8-16 [1]; 41-51 [2]; 58-63 [3] and 66-74 [4]) and an overall global fold characteristic of ACPs from both Type II FAS and polyketide synthases (PKSs). ‡ The overall length of the structured ACP domain (67 residues) is smaller than the structured regions of the Eschericia coli FAS ACP (75 residues), the actinorhodin PKS ACP (78 residues) and the Bacillus subtilis FAS ACP (76 residues). We further show that the rat FAS ACP is recognised as an efficient substrate by enzymes known to modify Type II ACPs including phosphopantetheinyl and malonyl transferases, but not by the heterologous S, coelicolor minimal polyketide synthase.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Chemistry(all)
- Physical and Theoretical Chemistry
- Chemistry(all)
- Organic Chemistry
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In: Organic and Biomolecular Chemistry, Vol. 1, No. 3, 07.02.2003, p. 463-471.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The type I rat fatty acid synthase ACP shows structural homology and analogous biochemical properties to type II ACPs
AU - Reed, Michelle A.C.
AU - Schweizer, Michael
AU - Szafranska, Anna E.
AU - Arthur, Chris
AU - Nicholson, Thomas P.
AU - Cox, Russell J.
AU - Crosby, John
AU - Crump, Matthew P.
AU - Simpson, Thomas J.
PY - 2003/2/7
Y1 - 2003/2/7
N2 - While X-ray and NMR structures are now available for most components of the Type II fatty acid synthase (FAS), there are no structures for Type I FAS domains. A region from the mammalian (rat) FAS, including the putative acyl carrier protein (ACP), has been cloned and over-expressed. Here we report multinuclear, multidimensional NMR studies which show that this isolated ACP domain contains four α-helices (residues 8-16 [1]; 41-51 [2]; 58-63 [3] and 66-74 [4]) and an overall global fold characteristic of ACPs from both Type II FAS and polyketide synthases (PKSs). ‡ The overall length of the structured ACP domain (67 residues) is smaller than the structured regions of the Eschericia coli FAS ACP (75 residues), the actinorhodin PKS ACP (78 residues) and the Bacillus subtilis FAS ACP (76 residues). We further show that the rat FAS ACP is recognised as an efficient substrate by enzymes known to modify Type II ACPs including phosphopantetheinyl and malonyl transferases, but not by the heterologous S, coelicolor minimal polyketide synthase.
AB - While X-ray and NMR structures are now available for most components of the Type II fatty acid synthase (FAS), there are no structures for Type I FAS domains. A region from the mammalian (rat) FAS, including the putative acyl carrier protein (ACP), has been cloned and over-expressed. Here we report multinuclear, multidimensional NMR studies which show that this isolated ACP domain contains four α-helices (residues 8-16 [1]; 41-51 [2]; 58-63 [3] and 66-74 [4]) and an overall global fold characteristic of ACPs from both Type II FAS and polyketide synthases (PKSs). ‡ The overall length of the structured ACP domain (67 residues) is smaller than the structured regions of the Eschericia coli FAS ACP (75 residues), the actinorhodin PKS ACP (78 residues) and the Bacillus subtilis FAS ACP (76 residues). We further show that the rat FAS ACP is recognised as an efficient substrate by enzymes known to modify Type II ACPs including phosphopantetheinyl and malonyl transferases, but not by the heterologous S, coelicolor minimal polyketide synthase.
UR - http://www.scopus.com/inward/record.url?scp=0041317602&partnerID=8YFLogxK
U2 - 10.1039/b208941f
DO - 10.1039/b208941f
M3 - Article
C2 - 12926246
AN - SCOPUS:0041317602
VL - 1
SP - 463
EP - 471
JO - Organic and Biomolecular Chemistry
JF - Organic and Biomolecular Chemistry
SN - 1477-0520
IS - 3
ER -