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

Stephen F. Haydock, Jesús F. Aparicio, István Molnár, Torsten Schwecke, Lake Ee Khaw, Ariane König, Andrew F.A. Marsden, Ian S. Galloway, James Staunton, Peter F. Leadlay (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

206 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)246-248
Number of pages3
JournalFEBS Letters
Volume374
Issue number2
DOIs
Publication statusPublished - 30 Oct 1995
MoE publication typeA1 Journal article-refereed

Keywords

  • Acyltransferase
  • Fatty acid synthase
  • Polyketide synthase
  • Sequence homology
  • Structural motif

Fingerprint

Dive into the research topics of 'Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl-CoA:acyl carrier protein transacylase domains in modular polyketide synthases'. Together they form a unique fingerprint.

Cite this