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1 talyze the rearrangement of n-butyryl-CoA to isobutyryl-CoA.
2 upon incubation with either n-butyryl-CoA or isobutyryl-CoA.
3 aleryl-coenzyme A (CoA), isovaleryl-CoA, and isobutyryl-CoA.
4 microM for butyryl-CoA, and 0.41 microM for isobutyryl-CoA.
5 aline, which is not efficiently converted to isobutyryl-CoA.
6 family that catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA also catalyzes the inte
7 catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA and exists as a heterot
9 utyryl-CoA mutase (ICM), which interconverts isobutyryl-CoA and n-butyryl-CoA; ethylmalonyl-CoA mutas
10 mal enzymes for a modified beta-oxidation of isobutyryl-CoA and propionyl-CoA could function for meta
11 e function of these enzymes in metabolism of isobutyryl-CoA and propionyl-CoA, intermediates in the m
12 ndicate the likely upper and lower limits of isobutyryl-CoA and related acyl-CoA concentrations withi
13 d via condensation of isobutyryl-coenzyme A (isobutyryl-CoA) and methylmalonyl-CoA catalysed by a 3-k
14 oA donor can be replaced with propionyl-CoA, isobutyryl-CoA, and benzoyl-CoA and the acyl chains acce
17 g conditions with limited treatment options, isobutyryl-CoA dehydrogenase (IBD), and 2-methylbutyryl-
18 malonyl-CoA mutase, an R-specific crotonase, isobutyryl-CoA dehydrogenase, and a GTPase are involved
19 ermediates, repeated attempts to demonstrate isobutyryl-CoA-dependent glucose acylation were unsucces
21 llinus, which suggested that butyryl-CoA and isobutyryl-CoA function as starter units for palmitate a
22 es by the presence of high concentrations of isobutyryl-CoA (>100 microM), a branched-chain fatty aci
24 4.4 microM) with similar efficiency, whereas isobutyryl-CoA is a poor substrate and displayed 13-fold
25 These observations clearly demonstrate that isobutyryl-CoA is a starter unit for isopalmitate biosyn
27 thway: ethylmalonyl-CoA, methylsuccinyl-CoA, isobutyryl-CoA, methacrylyl-CoA, and beta-hydroxyisobuty
28 to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA mutase (ICM) large subunit (36%) and smal
29 e recently discovered family members include isobutyryl-CoA mutase (ICM), which interconverts isobuty
31 itant approximately 240-fold decrease in the isobutyryl-CoA mutase activity compared with wild-type I
32 Neither PCM nor PCM-F displayed detectable isobutyryl-CoA mutase activity, demonstrating that PCM r
33 rotetrameric organization similar to that of isobutyryl-CoA mutase and a recently characterized archa
34 a natural fusion protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein ch
35 ses the two subunits of the AdoCbl-dependent isobutyryl-CoA mutase flanking a G-protein chaperone and
36 ugh most chaperones are standalone proteins, isobutyryl-CoA mutase fused (IcmF) has a G-protein domai
42 of IcmF, a natural fusion protein variant of isobutyryl-CoA mutase, in complex with the adenosylcobal
43 However, both methylmalonyl-CoA mutase and isobutyryl-CoA mutase, which catalyze the two CoB12-depe
44 no protection from inactivation when either isobutyryl-CoA or n-butyryl-CoA was used as substrate.
45 lonyl CoA, succinyl CoA, methylcrotonyl CoA, isobutyryl CoA, oxidized CoA, acetyl CoA, crotonoyl CoA,
47 ts show that isobutyric acid is converted to isobutyryl-CoA that flows into the even-chain acyl-acyl
48 y crystal structures of HAT1 in complex with isobutyryl-CoA that gleaned an atomic level insight into
52 s, the apparent Km values for acetyl-CoA and isobutyryl-CoA were 25 and 29 microM, respectively, for
54 metabolism, isovaleryl-Coenzyme A (CoA) and isobutyryl-CoA, with three molecules of malonyl-CoA to f