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Divergent sequence motifs correlated with the substrate specificity of (methyl)malonyl‐CoA:acyl carrier protein transacylase domains in modular polyketide synthases
Author(s) -
Haydock Stephen F.,
Aparicio Jesús F.,
Molnár István,
Schwecke Torsten,
Khaw Lake Ee,
König Ariane,
Marsden Andrew F.A.,
Galloway Ian S.,
Staunton James,
Leadlay Peter F.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01119-y
Subject(s) - acyl carrier protein , acyltransferase , acyltransferases , polyketide synthase , polyketide , biochemistry , malonyl coa , stereochemistry , biology , peptide sequence , active site , chemistry , enzyme , biosynthesis , gene , beta oxidation
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.