ライフサイエンスコーパス: isobutyryl-CoA

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 family that catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA also catalyzes the inte

6 catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA and exists as a heterot

7 IcmF catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA, whereas GTPase activit

8 utyryl-CoA mutase (ICM), which interconverts isobutyryl-CoA and n-butyryl-CoA; ethylmalonyl-CoA mutas

9 mal enzymes for a modified beta-oxidation of isobutyryl-CoA and propionyl-CoA could function for meta

10 e function of these enzymes in metabolism of isobutyryl-CoA and propionyl-CoA, intermediates in the m

11 ndicate the likely upper and lower limits of isobutyryl-CoA and related acyl-CoA concentrations withi

12 oA donor can be replaced with propionyl-CoA, isobutyryl-CoA, and benzoyl-CoA and the acyl chains acce

13 One, termed ACS I, uses acetyl-CoA and isobutyryl-CoA but not indoleacetyl-CoA or phenylacetyl-

14 Isobutyryl-CoA dehydrogenase (IBD) is involved in the ca

15 malonyl-CoA mutase, an R-specific crotonase, isobutyryl-CoA dehydrogenase, and a GTPase are involved

16 ermediates, repeated attempts to demonstrate isobutyryl-CoA-dependent glucose acylation were unsucces

17 llinus, which suggested that butyryl-CoA and isobutyryl-CoA function as starter units for palmitate a

18 es by the presence of high concentrations of isobutyryl-CoA (>100 microM), a branched-chain fatty aci

19 Butyryl-CoA and isobutyryl-CoA interacted with the acetyltransferase P30

20 4.4 microM) with similar efficiency, whereas isobutyryl-CoA is a poor substrate and displayed 13-fold

21 These observations clearly demonstrate that isobutyryl-CoA is a starter unit for isopalmitate biosyn

22 thway: ethylmalonyl-CoA, methylsuccinyl-CoA, isobutyryl-CoA, methacrylyl-CoA, and beta-hydroxyisobuty

23 to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA mutase (ICM) large subunit (36%) and smal

24 e recently discovered family members include isobutyryl-CoA mutase (ICM), which interconverts isobuty

25 rearrangements, methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM).

26 itant approximately 240-fold decrease in the isobutyryl-CoA mutase activity compared with wild-type I

27 Neither PCM nor PCM-F displayed detectable isobutyryl-CoA mutase activity, demonstrating that PCM r

28 rotetrameric organization similar to that of isobutyryl-CoA mutase and a recently characterized archa

29 a natural fusion protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein ch

30 ses the two subunits of the AdoCbl-dependent isobutyryl-CoA mutase flanking a G-protein chaperone and

31 flanking a G-protein chaperone and named it isobutyryl-CoA mutase fused (IcmF).

32 We designate this fusion protein as IcmF (isobutyryl-CoA mutase fused).

33 In the closely related isomerase, isobutyryl-CoA mutase the homologous residues are F80 an

34 We have recently demonstrated that an isobutyryl-CoA mutase variant, IcmF, a member of this en

35 Like isobutyryl-CoA mutase, HCM consists of a large substrate

36 of IcmF, a natural fusion protein variant of isobutyryl-CoA mutase, in complex with the adenosylcobal

37 However, both methylmalonyl-CoA mutase and isobutyryl-CoA mutase, which catalyze the two CoB12-depe

38 no protection from inactivation when either isobutyryl-CoA or n-butyryl-CoA was used as substrate.

39 lonyl CoA, succinyl CoA, methylcrotonyl CoA, isobutyryl CoA, oxidized CoA, acetyl CoA, crotonoyl CoA,

40 enase, permitting the optimal binding of the isobutyryl-CoA substrate.

41 talyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA.

42 sm of valine and catalyzes the conversion of isobutyryl-CoA to methacrylyl-CoA.

43 In these extracts perdeuterated isobutyryl-CoA was converted to isopalmitate (a branched

44 s, the apparent Km values for acetyl-CoA and isobutyryl-CoA were 25 and 29 microM, respectively, for

45 Propionyl-CoA and isobutyryl-CoA were the two most preferred substrates of

46 metabolism, isovaleryl-Coenzyme A (CoA) and isobutyryl-CoA, with three molecules of malonyl-CoA to f