Mechanism and substrate recognition of human holo ACP synthase.
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ABSTRACT:
SUBMITTER: Bunkoczi G
PROVIDER: S-EPMC2148441 | biostudies-literature | 2007 Nov
REPOSITORIES: biostudies-literature
Publications
Mechanism and substrate recognition of human holo ACP synthase.
Bunkoczi Gabor G Pasta Saloni S Joshi Anil A Wu Xiaoqiu X Kavanagh Kathryn L KL Smith Stuart S Oppermann Udo U
Chemistry & biology 20071101 11
Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed with CoA and Mg(2+), and in ternary complex with CoA ...[more]
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