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1 g (2R,3S)- inverted question mark2, 3-(2)H(2)octanoyl-CoA.
2 s nucleophiles, and is strongly protected by octanoyl-CoA.
3       FabH utilized neither hexanoyl-CoA nor octanoyl-CoA.
4 gible activity toward substrates longer than 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  advanced statistical analysis, to show that octanoyl-CoA binding increases the activation free energ
9 /- 0.4 microM) values for the oxidation of n-octanoyl-CoA (C(8)-CoA) by WT pMCAD recombinantly expres
10 E376Q mutation not only impaired the rate of octanoyl-CoA-dependent reduction of the enzyme-bound FAD
11 nd thermodynamic correspondences between the octanoyl-CoA-dependent reductive half-reaction and the e
12 ation of Glu-376-->Gln(E376Q) slows down the octanoyl-CoA-dependent reductive half-reaction of the en
13              The E376D mutation impaired the octanoyl-CoA-dependent reductive half-reaction such that
14 he results in terms of key interactions that octanoyl-CoA establishes with the four alpha-helices of
15 traight-chain acyl-CoA esters (decanoyl-CoA, octanoyl-CoA, hexanoyl-CoA, butanoyl-CoA, acetyl-CoA) in
16 ur bioassays from acetyl-CoA, malonyl-CoA, n-octanoyl-CoA, n-decanoyl-CoA, DL-beta-hydroxybutanoyl-Co
17  interaction and enzyme catalysis, utilizing octanoyl-CoA/octenoyl-CoA as a physiological substrate/p
18                   Although palmitoyl-CoA and octanoyl-CoA provided reducing equivalents to OXPHOS-con
19 functionally diverse C(8)-CoA-ligands, viz., octanoyl-CoA (substrate), octenoyl-CoA (product), and oc
20 nsferred the [(3)H]octanoyl group from [(3)H]octanoyl CoA to recombinant proghrelin in vitro.
21 microM-1 min-1 with butyryl-, hexanoyl-, and octanoyl-CoA used as substrates, respectively.
22  kcat/K(m) values for butyryl-hexanoyl-, and octanoyl-CoA were 220, 22, and 3.2 microM-1 min-1, respe