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Two functional domains of coenzyme A activate catalysis by coenzyme A transferase. Pantetheine and adenosine 3'-phosphate 5'-diphosphate.
Fierke CA, Jencks WP. Fierke CA, et al. J Biol Chem. 1986 Jun 15;261(17):7603-6. J Biol Chem. 1986. PMID: 3458707 Free article.
We report here that interaction between the enzyme and the pantetheine moiety of CoA provides the majority of the rate acceleration and destabilization of the enzyme-thiol ester intermediate that is observed with CoA substrates. The role of the adenosine 3'-phosp …
We report here that interaction between the enzyme and the pantetheine moiety of CoA provides the majority of the rate acceleration and dest …
Suspect screening and targeted analysis of acyl coenzyme A thioesters in bacterial cultures using a high-resolution tribrid mass spectrometer.
Cakić N, Kopke B, Rabus R, Wilkes H. Cakić N, et al. Anal Bioanal Chem. 2021 Jun;413(14):3599-3610. doi: 10.1007/s00216-021-03318-3. Epub 2021 Apr 21. Anal Bioanal Chem. 2021. PMID: 33881564 Free PMC article.
They make use of the formation of the adenosine 3',5'-diphosphate key fragment (m/z 428.0365) and the neutral loss of the adenosine 3'-phosphate-5'-diphosphate moiety (506.9952) as preselection criteria for the detection of acyl-CoAs. ...
They make use of the formation of the adenosine 3',5'-diphosphate key fragment (m/z 428.0365) and the neutral loss of the adenosine …