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. Author manuscript; available in PMC: 2014 Mar 19.
Published in final edited form as: Biochemistry. 2013 Mar 5;52(11):1839–1841. doi: 10.1021/bi400185v

Table 1.

Rates of transacylation and hydrolysis by DEBS AT3 and mutant AT domains. Rates were measured in the presence of 150 uM α-carboxyacyl-CoA substrate. Transacylation reactions were run in the presence of 100 uM DEBS holo-ACP3.

AT Domain Substrate v/[E]o
Transacylation
(min−1)		 v/[E]o
Hydrolysis
(min−1)
DEBSAT3 MMCoA 30 2
DEBSAT3-Q652L MMCoA 0.2 0.1
DEBSAT3-Y751H,S753F MMCoA <0.1 <0.1
DEBSAT3 MCoA 0.9 0.8
DEBSAT3-Q652L MCoA <0.1 <0.1
DEBSAT3-Y751H,S753F MCoA <0.1 <0.2