Details
| Original language | English |
|---|---|
| Pages (from-to) | 511-518 |
| Number of pages | 8 |
| Journal | Molecular BioSystems |
| Volume | 5 |
| Issue number | 5 |
| Publication status | Published - 5 May 2009 |
| Externally published | Yes |
Abstract
Interactions between the acyl carrier protein (ACP) and ketoacylsynthase (KS) components of the actinorhodin polyketide synthase have been investigated using kinetic assays. These indicate that for three different quantifiable interactions (acceleration of self-malonylation, initiation and extension) mutations of E47 and E53 residues located on ACP helix II have different effects. Initiation clearly involves interaction between KSβ and ACP helix II, but self-malonylation acceleration and extension by KS α appear not to be affected strongly by the same mutations.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Molecular BioSystems, Vol. 5, No. 5, 05.05.2009, p. 511-518.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase
AU - Beltran-Alvarez, Pedro
AU - Arthur, Christopher J.
AU - Cox, Russell J.
AU - Crosby, John
AU - Crump, Matthew P.
AU - Simpson, Thomas J.
PY - 2009/5/5
Y1 - 2009/5/5
N2 - Interactions between the acyl carrier protein (ACP) and ketoacylsynthase (KS) components of the actinorhodin polyketide synthase have been investigated using kinetic assays. These indicate that for three different quantifiable interactions (acceleration of self-malonylation, initiation and extension) mutations of E47 and E53 residues located on ACP helix II have different effects. Initiation clearly involves interaction between KSβ and ACP helix II, but self-malonylation acceleration and extension by KS α appear not to be affected strongly by the same mutations.
AB - Interactions between the acyl carrier protein (ACP) and ketoacylsynthase (KS) components of the actinorhodin polyketide synthase have been investigated using kinetic assays. These indicate that for three different quantifiable interactions (acceleration of self-malonylation, initiation and extension) mutations of E47 and E53 residues located on ACP helix II have different effects. Initiation clearly involves interaction between KSβ and ACP helix II, but self-malonylation acceleration and extension by KS α appear not to be affected strongly by the same mutations.
UR - http://www.scopus.com/inward/record.url?scp=65349087275&partnerID=8YFLogxK
U2 - 10.1039/b821844g
DO - 10.1039/b821844g
M3 - Article
C2 - 19381365
AN - SCOPUS:65349087275
VL - 5
SP - 511
EP - 518
JO - Molecular BioSystems
JF - Molecular BioSystems
SN - 1742-206X
IS - 5
ER -