ライフサイエンスコーパス: acetoacetyl-CoA

1 ensation of two acetyl CoA molecules to form acetoacetyl CoA.

2 acetyl-S-enzyme during its condensation with acetoacetyl-CoA.

3 y E95Q was not stimulated in the presence of acetoacetyl-CoA.

4 ernary complex of the enzyme with NAD(+) and acetoacetyl-CoA.

5 ensitive to feedback substrate inhibition by acetoacetyl-CoA.

6 of S-3-oxobutyl-CoA, the thioether analog of acetoacetyl-CoA.

7 roximately 100-fold increase in the k(m) for acetoacetyl-CoA.

8 nsible for the formation of butyryl-CoA from acetoacetyl-CoA.

9 arent k(m) values for S-(3-oxobutyl)-CoA and acetoacetyl-CoA.

10 obtained using the physiological substrate, acetoacetyl-CoA.

11 by monitoring the use of a second substrate, acetoacetyl-CoA (300 nm).

12 n solution, where HMG-CoA is cleaved to form acetoacetyl-CoA (AcAc-CoA) and acetate.

13 netic and chemical mechanisms of KACPR using acetoacetyl-CoA (AcAc-CoA) as a substrate.

14 Escherichia coli cells that overexpress the acetoacetyl-CoA:acetyl-CoA transferase, AtoAD (EC 2.8.3.

15 ossessed virtually unchanged K(m) values for acetoacetyl-CoA and CoA but had a greater than 99% decre

16 t in opposite directions) for the binding of acetoacetyl-CoA and indoleacryloyl-CoA to the enzyme.

17 h apparent Km values of 89 and 20 microM for acetoacetyl-CoA and NADH, respectively.

18 eneral base both in the condensation between acetoacetyl-CoA and the acetylated enzyme, and the hydro

19 nt types of CoA-ligands (viz., octenoyl-CoA, acetoacetyl-CoA, and indoleacryloyl-CoA) to human liver

20 rporate carbon from glucose into acetyl-CoA, acetoacetyl-CoA, and succinyl-CoA and carbon from leucin

21 le substrate analogs, 3-thiaglutaryl-CoA and acetoacetyl-CoA, are not altered by the mutations.

22 The acetoacetyl-CoA binary structure demonstrates reduced co

23 of acetyl phosphate, acetoacetyl coenzyme A (acetoacetyl-CoA), butyryl CoA, acetoacetate, and beta-hy

24 contrast, abstraction of the alpha-proton of acetoacetyl-CoA by Arg-94 --> Gln mutant dehydrogenase i

25 ed HMGS from Staphylococcus aureus and bound acetoacetyl-CoA by cryo-cooling enzyme crystals at three

26 ay a role in anchoring the second substrate, acetoacetyl-CoA, by interacting with the carbonyl oxygen

27 off-rate" of acetoacetyl-CoA from the enzyme-acetoacetyl-CoA complex.

28 st that, in the absence of second substrate (acetoacetyl-CoA), enzymatic addition of H(2)(18)O to the

29 in formation of a stable binary complex with acetoacetyl-CoA, F204L exhibits binding stoichiometries

30 argely attributed to a decreased affinity of acetoacetyl-CoA for these enzymes and, more specifically

31 n increase in the dissociation "off-rate" of acetoacetyl-CoA from the enzyme-acetoacetyl-CoA complex.

32 of the purine and nicotinamide nucleotides, acetoacetyl-CoA, H2O2, reduced glutathione, and 2-monoac

33 A dehydrogenase complexed with the inhibitor acetoacetyl-CoA has been determined at 2.25 A resolution

34 Succinyl-CoA and acetoacetyl-CoA increased the rate of glycine proton rem

35 catalyzes the condensation of acetyl-CoA and acetoacetyl-CoA into 3-hydroxy-3-methylglutaryl CoA.

36 athway is the condensation of acetyl-CoA and acetoacetyl-CoA into HMG-CoA, catalyzed by the enzyme HM

37 ndensation of two molecules of acetyl-CoA to acetoacetyl-CoA, is thermodynamically unfavorable.

38 imilar K(m) values for binding of substrates acetoacetyl-CoA (K(m) 9.8 +/- 0.8 microM) and CoA (K(m)

39 DH II inhibited, in parallel, reduction of S-acetoacetyl-CoA (Ki approximately 1.6 microM), as well a

40 , acetyl CoA, crotonoyl CoA, n-propzoyl CoA, acetoacetyl CoA, malonyl CoA) were completely separated

41 ondria and enzymes that can form acetyl-CoA, acetoacetyl-CoA, malonyl-CoA, and HMG-CoA in their cytos

42 initially reacts with acetoacetate to yield acetoacetyl-CoA plus succinate in the succinyl-CoA-aceto

43 role of AACT2 in generating the bulk of the acetoacetyl CoA precursor required for the cytosol-local

44 tructure of E170Q in complex with NAD(+) and acetoacetyl-CoA (R = 21.9%, R(free) = 27.6%, 2.2 A) reve

45 This would be followed by acetoacetyl-CoA reacting with acetyl-CoA to generate HMG

46 catalyzed by a beta-ketothiolase (PhaA), an acetoacetyl-CoA reductase (PhaB), and a polyhydroxyalkan

47 etic fragment encoding beta-ketothiolase and acetoacetyl-CoA reductase behind a modified synthase gen

48 haB2 and phaB3 as well as 15 other potential acetoacetyl-CoA reductases.

49 se-catalyzed condensation of acetyl-CoA with acetoacetyl-CoA requires enolization/carbanion formation

50 r H264 interacts with the carbonyl oxygen of acetoacetyl-CoA's thioester, turnover of S-(3-oxobutyl)-

51 ydrogenase in cultured skin fibroblasts with acetoacetyl-CoA substrate showed reduced activity.

52 ass spectrometry measurements of acetyl-CoA, acetoacetyl-CoA, succinyl-CoA, hydroxymethylglutaryl-CoA

53 s acutely stimulated 1.5-5-fold increases in acetoacetyl-CoA, succinyl-CoA, malonyl-CoA, hydroxymethy

54 zation, and a new acetylation target, namely acetoacetyl-CoA synthetase (SlAacS).

55 However, lowering acetoacetyl-CoA synthetase 80% partially inhibited gluco

56 sent a conserved mechanism for regulation of acetoacetyl-CoA synthetase activity in all domains of li

57 succinyl-CoA:3-ketoacid-CoA transferase and acetoacetyl-CoA synthetase to synthesize and use acetoac

58 forms acetoacetate in the mitochondria, and acetoacetyl-CoA synthetase, which uses acetoacetate to f

59 ivo evidence show that SlAacS is a bona fide acetoacetyl-CoA synthetase.

60 In the case of acetoacetyl-CoA, the spectrum of the enzyme-ligand compl

61 Acetoacetyl CoA thiolase (AACT, EC 2.3.1.9) catalyzes th

62 d more forcefully to regulatory stimuli than acetoacetyl-CoA thiolase activity but usually less than

63 6.5-kDa mvaE gene product catalyzed both the acetoacetyl-CoA thiolase and HMG-CoA reductase reactions

64 Under conditions at which acetoacetyl-CoA thiolase and long-chain thiolase were co

65 g as a selective SNO-CoA reductase, protects acetoacetyl-CoA thiolase from inhibitory S-nitrosylation

66 Kinetic studies of acetoacetyl-CoA thiolase implicated a ping-pong mechanis

67 s demonstrated by using HMG-CoA synthase and acetoacetyl-CoA thiolase/HMG-CoA reductase from E. faeca

68 d mitochondrial thiolases, as well as to the acetoacetyl-CoA thiolases of prokaryotes.

69 the kinetics of the reaction that have shown acetoacetyl-CoA to be a potent inhibitor of the overall

70 r) is crotonyl-CoA reductase, which converts acetoacetyl-CoA to butyryl-CoA for use as a 4C extender

71 acetyl-CoA, which precedes condensation with acetoacetyl-CoA to form the HMG-CoA product.

72 the DeltaH degrees value for the binding of acetoacetyl-CoA to the enzyme was 5.6 kcal/mol more favo

73 enzyme complexed with its second substrate, acetoacetyl-CoA, to 1.9 A.

74 a crystal structure of HMG-CoA synthase with acetoacetyl-CoA was determined at 2.5-A resolution.

75 of S-(3-oxobutyl)-CoA, a thioether analog of acetoacetyl-CoA, was investigated.

76 differences in (13)C NMR chemical shifts for acetoacetyl-CoA when bound as an enolate to MCAD and eno

77 catalyzed the NADH-dependent reduction of S-acetoacetyl-CoA with a Km of approximately 68 microM and