Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases.

Haydock, S. F.; Aparicio, J. F.; König, Ariane; Molnár, I.; Schwecke, T.; Marsden, A. F. A.; Galloway, I. S. M.; Staunton, J.; Leadlay, P. F.

doi:10.1016/0014-5793(95)01119-Y

Reference : Divergent sequence motifs correlated with the substrate specificity of (methyl)malony...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Multidisciplinary, general & others
	To cite this reference:	http://hdl.handle.net/10993/12418

Title :	Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases.
Language :	English
Author, co-author :	Haydock, S. F. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Aparicio, J. F. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	König, Ariane [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Molnár, I. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Schwecke, T. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Marsden, A. F. A. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Galloway, I. S. M. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
	Staunton, J. [University of Cambridge > Cambridge Centre for Molecular Recognition > University Chemical Laboratory]
	Leadlay, P. F. [University of Cambridge > Cambridge Centre for Molecular Recognition > Department of Biochemistry]
Publication date :	30-Oct-1995
Journal title :	FEBS Letters
Volume :	374
Issue/season :	2
Pages :	246-248
Peer reviewed :	No
Audience :	International
ISSN :	0014-5793
Keywords :	[en] Acyltransferase ; Structuralmotif ; Sequence homology ; Polyketide synthase ; Fatty acid synthase
Abstract :	[en] The amino acid sequences of a large number of polyketide synthase domains that catalyse the transacylation of either methylmalonyl-CoA or malonyl-CoA onto acyl carrier protein (ACP) have been compared. Regions were identified in which the acyltransferase sequences diverged according to whether they were specific for malonyl-CoA or methylmalonyl-CoA. These differences are sufficiently clear to allow unambiguous assignment of newly-sequenced acyltransferase domains in modular polyketide synthases. Comparison with the recently-determined structure of the malonyltransferase from Escherichia coli fatty acid synthase showed that the divergent region thus identified lies near the acyltransferase active site, though not close enough to make direct contact with bound substrate.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/10993/12418
DOI :	10.1016/0014-5793(95)01119-Y

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