Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

Pedro Beltran-Alvarez; Christopher J. Arthur; Russell J. Cox; John Crosby; Matthew P. Crump; Thomas J. Simpson

doi:10.1039/b821844g

Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

Pedro Beltran-Alvarez, Christopher J. Arthur, Russell J. Cox, John Crosby, Matthew P. Crump, Thomas J. Simpson

School of Chemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

6 Citations (Scopus)

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 KS beta and ACP helix II, but self-malonylation acceleration and extension by KS alpha appear not to be affected strongly by the same mutations.

Original language	English
Pages (from-to)	511-518
Number of pages	8
Journal	Molecular bioSystems
Volume	5
Issue number	5
DOIs	https://doi.org/10.1039/b821844g
Publication status	Published - 2009

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title = "Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase",

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 KS beta and ACP helix II, but self-malonylation acceleration and extension by KS alpha appear not to be affected strongly by the same mutations.",

author = "Pedro Beltran-Alvarez and Arthur, {Christopher J.} and Cox, {Russell J.} and John Crosby and Crump, {Matthew P.} and Simpson, {Thomas J.}",

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doi = "10.1039/b821844g",

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journal = "Molecular bioSystems",

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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

Y1 - 2009

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 KS beta and ACP helix II, but self-malonylation acceleration and extension by KS alpha 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 KS beta and ACP helix II, but self-malonylation acceleration and extension by KS alpha appear not to be affected strongly by the same mutations.

U2 - 10.1039/b821844g

DO - 10.1039/b821844g

M3 - Article (Academic Journal)

C2 - 19381365

SN - 1742-206X

VL - 5

SP - 511

EP - 518

JO - Molecular bioSystems

JF - Molecular bioSystems

IS - 5

ER -

Preliminary kinetic analysis of acyl carrier protein-ketoacylsynthase interactions in the actinorhodin minimal polyketide synthase

Abstract

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