Details
| Original language | English |
|---|---|
| Pages (from-to) | 1644-1649 |
| Number of pages | 6 |
| Journal | Journal of the Chemical Society. Perkin Transactions 1 |
| Volume | 14 |
| Publication status | Published - 1 Jan 2002 |
| Externally published | Yes |
Abstract
Streptomyces coelicolor is host to a number of biosynthetic proteins requiring post-translational modification by the addition of phosphopantetheine groups. The S. coelicolor genome, was probed, in silico, with the sequence of Escherichia coli holo-Acyl Carrier Protein Synthase (ACPS). A single open reading frame (ORF) strongly matching the E. coli ACPS was discovered. The putative S. coelicolor ACPS ORF was cloned and expressed and the resulting protein purified and characterised. S. coelicolor ACPS appears to be extremely promiscuous in its substrate specificity, accepting varied acyl CoA substrates and protein substrates from Type I and Type II fatty acid synthases (FAS) as well as from Type I and Type II polyketide synthase (PKS) biosynthetic protein complexes. This phosphopantetheinyl transferase thus has high potential for the synthesis of diverse holo- and acylated acyl carrier proteins.
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
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In: Journal of the Chemical Society. Perkin Transactions 1, Vol. 14, 01.01.2002, p. 1644-1649.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Streptomyces coelicolor phosphopantetheinyl transferase
T2 - A promiscuous activator of polyketide and fatty acid synthase acyl carrier proteins
AU - Cox, Russell J.
AU - Crosby, John
AU - Daltrop, Oliver
AU - Glod, Frank
AU - Jarzabek, Malgorzata E.
AU - Nicholson, Thomas P.
AU - Reed, Michelle
AU - Simpson, Thomas J.
AU - Smith, Leah H.
AU - Soulas, Florilène
AU - Szafranska, Anna E.
AU - Westcott, James
PY - 2002/1/1
Y1 - 2002/1/1
N2 - Streptomyces coelicolor is host to a number of biosynthetic proteins requiring post-translational modification by the addition of phosphopantetheine groups. The S. coelicolor genome, was probed, in silico, with the sequence of Escherichia coli holo-Acyl Carrier Protein Synthase (ACPS). A single open reading frame (ORF) strongly matching the E. coli ACPS was discovered. The putative S. coelicolor ACPS ORF was cloned and expressed and the resulting protein purified and characterised. S. coelicolor ACPS appears to be extremely promiscuous in its substrate specificity, accepting varied acyl CoA substrates and protein substrates from Type I and Type II fatty acid synthases (FAS) as well as from Type I and Type II polyketide synthase (PKS) biosynthetic protein complexes. This phosphopantetheinyl transferase thus has high potential for the synthesis of diverse holo- and acylated acyl carrier proteins.
AB - Streptomyces coelicolor is host to a number of biosynthetic proteins requiring post-translational modification by the addition of phosphopantetheine groups. The S. coelicolor genome, was probed, in silico, with the sequence of Escherichia coli holo-Acyl Carrier Protein Synthase (ACPS). A single open reading frame (ORF) strongly matching the E. coli ACPS was discovered. The putative S. coelicolor ACPS ORF was cloned and expressed and the resulting protein purified and characterised. S. coelicolor ACPS appears to be extremely promiscuous in its substrate specificity, accepting varied acyl CoA substrates and protein substrates from Type I and Type II fatty acid synthases (FAS) as well as from Type I and Type II polyketide synthase (PKS) biosynthetic protein complexes. This phosphopantetheinyl transferase thus has high potential for the synthesis of diverse holo- and acylated acyl carrier proteins.
UR - http://www.scopus.com/inward/record.url?scp=0035996942&partnerID=8YFLogxK
U2 - 10.1039/b204633b
DO - 10.1039/b204633b
M3 - Article
AN - SCOPUS:0035996942
VL - 14
SP - 1644
EP - 1649
JO - Journal of the Chemical Society. Perkin Transactions 1
JF - Journal of the Chemical Society. Perkin Transactions 1
SN - 1472-7781
ER -