Abstract:
:ADP-forming acetyl-CoA synthetase (ACD) catalyzes the interconversion of acetyl-CoA and acetate. The related succinyl-CoA synthetase follows a three-step mechanism involving a single phosphoenzyme, but a novel four-step mechanism with two phosphoenzyme intermediates was proposed for Pyrococcus ACD. Characterization of enzyme variants of Entamoeba ACD in which the two proposed phosphorylated His residues were individually altered revealed that only His252 is essential for enzymatic activity. Analysis of variants altered at two residues proposed to interact with the phosphohistidine loop that swings between distinct parts of the active site are consistent with a mechanism involving a single phosphoenzyme intermediate. Our results suggest ACDs with different subunit structures may employ slightly different mechanisms to bridge the span between active sites I and II.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Jones CP,Khan K,Ingram-Smith Cdoi
10.1002/1873-3468.12573subject
Has Abstractpub_date
2017-02-01 00:00:00pages
603-612issue
4eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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