1 s nucleophiles, and is strongly protected by octanoyl-CoA.

2       FabH utilized neither hexanoyl-CoA nor octanoyl-CoA.

3 gible activity toward substrates longer than octanoyl-CoA.

4 g (2R,3S)- inverted question mark2, 3-(2)H(2)octanoyl-CoA.

5                             The Km values of octanoyl-CoA and lauroyl-CoA were determined to be 1.1 +

6 both normal and 3'-dephosphorylated forms of octanoyl-CoA and octenoyl-CoA (cumulatively referred to

7 s using our standard substrates butyryl-CoA, octanoyl-CoA, and palmitoyl-CoA.

8 /- 0.4 microM) values for the oxidation of n-octanoyl-CoA (C(8)-CoA) by WT pMCAD recombinantly expres

9 E376Q mutation not only impaired the rate of octanoyl-CoA-dependent reduction of the enzyme-bound FAD

10 nd thermodynamic correspondences between the octanoyl-CoA-dependent reductive half-reaction and the e

11 ation of Glu-376-->Gln(E376Q) slows down the octanoyl-CoA-dependent reductive half-reaction of the en

12              The E376D mutation impaired the octanoyl-CoA-dependent reductive half-reaction such that

13 ur bioassays from acetyl-CoA, malonyl-CoA, n-octanoyl-CoA, n-decanoyl-CoA, DL-beta-hydroxybutanoyl-Co

14  interaction and enzyme catalysis, utilizing octanoyl-CoA/octenoyl-CoA as a physiological substrate/p

15                   Although palmitoyl-CoA and octanoyl-CoA provided reducing equivalents to OXPHOS-con

16 functionally diverse C(8)-CoA-ligands, viz., octanoyl-CoA (substrate), octenoyl-CoA (product), and oc

17 nsferred the [(3)H]octanoyl group from [(3)H]octanoyl CoA to recombinant proghrelin in vitro.

18 microM-1 min-1 with butyryl-, hexanoyl-, and octanoyl-CoA used as substrates, respectively.

19  kcat/K(m) values for butyryl-hexanoyl-, and octanoyl-CoA were 220, 22, and 3.2 microM-1 min-1, respe