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

FEBS Letters

Schwecke, Torsten¹  Marsden, Andrew F.A.¹  Molnár, István¹  Staunton, James²  Haydock, Stephen F.¹  König, Ariane¹  Khaw, Lake Ee¹  Galloway, Ian S.¹  Leadlay, Peter F.¹  Aparicio, Jesús F.¹ 

[1] Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1 QW, UK;Cambridge Centre for Molecular Recognition, University of Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK

关键词: Acyltransferase;    Structural motif;    Sequence homology;    Polyketide synthase;    Fatty acid synthase;    ACP;    acyl carrier protein;    AT;    acyl-CoA:ACP acyltransferase;    PKS;    polyketide synthase;   

DOI  :  10.1016/0014-5793(95)01119-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown