ライフサイエンスコーパス: acyl-CoA dehydrogenase

1 een mapped onto the structure of short chain acyl-CoA dehydrogenase.

2 of mitochondrial medium- or very long-chain acyl-CoA dehydrogenase.

3 probe of the active site in the medium chain acyl-CoA dehydrogenase.

4 not require involvement of the medium-chain acyl-CoA dehydrogenase.

5 g thioester polarization in the medium chain acyl-CoA dehydrogenase.

6 such an intermediate in the biogenesis of an acyl-CoA dehydrogenase.

7 ogenase family except for IVD and long-chain acyl-CoA dehydrogenase.

8 The enzyme is a homologue of acyl-CoA dehydrogenase.

9 amate which acts as the base in medium chain acyl-CoA dehydrogenase.

10 11 constitute a distinct class of eucaryotic acyl CoA dehydrogenases.

11 FkbI has a similar fold to acyl-CoA dehydrogenases.

12 not as favorable as that observed with other acyl-CoA dehydrogenases.

13 oxylation reaction which is unique among the acyl-CoA dehydrogenases.

14 and has high levels of homology with various acyl-CoA dehydrogenases.

15 s which induce competitive inhibition of the acyl-CoA dehydrogenases.

16 The same mechanism may regulate other acyl-CoA dehydrogenases.

17 e dehydrogenase (PDH), citrate synthase, and acyl-CoA dehydrogenases.

18 ng induces a large enzyme potential shift in acyl-CoA dehydrogenases.

19 ehyde dehydrogenase 2 (ALDH2), ATP synthase, acyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, and man

20 Acyl-CoA dehydrogenase 9 (ACAD9) is a recently identifie

21 Acyl-CoA dehydrogenase 9 (ACAD9) is an assembly factor f

22 Medium-chain acyl-CoA dehydrogenase and acyl-CoA dehydrogenase 9, two related enzymes with lysin

23 ased acetylation of mitochondrial long-chain acyl-CoA dehydrogenase, a known SIRT3 deacetylation targ

24 The flavoenzyme is a new member of the acyl-CoA dehydrogenase (ACAD) family, but it does not re

25 oned cDNA showed that NOA is a member of the acyl-CoA dehydrogenase (ACAD) superfamily.

26 rally distinct subfamily of acyl coenzyme A (acyl-CoA) dehydrogenase (ACAD) enzymes that are alpha2be

27 nalysis indicated that, like very-long-chain acyl-CoA dehydrogenase, ACAD-9 is a dimer, in contrast t

28 The expression of acyl-CoA dehydrogenase ACADM, the first enzyme involved

29 The acyl-CoA dehydrogenases (ACADs) are enzymes that catalyz

30 However, their oxidation in vivo by acyl-CoA dehydrogenases (ACADs) that catalyze the first

31 lock in B-oxidation at the step catalyzed by acyl-CoA dehydrogenases (ACADs), which in other organism

32 l side chain metabolism requires one or more acyl-CoA dehydrogenases (ACADs).

33 ogenase (VLCAD) is a member of the family of acyl-CoA dehydrogenases (ACADs).

34 (MCD) belongs to the family of FAD-dependent acyl-CoA dehydrogenase (ACD) and is a key enzyme of the

35 nserved Caenorhabditis elegans gene acdh-11 (acyl-CoA dehydrogenase [ACDH]) facilitates heat adaptati

36 Acyl-CoA dehydrogenases (ACDs) are a family of flavoenzy

37 of the enzymes discussed in this review [the acyl-CoA dehydrogenases (ACDs), CDP-6-deoxy-l-threo-d-gl

38 The measurement of acyl-CoA dehydrogenase activities is an essential part o

39 Acyl-CoA dehydrogenase activities were measured in rat s

40 nthesis of the substrates used for measuring acyl-CoA dehydrogenase activities; however, the yields a

41 cid oxidation enzyme integrity, medium-chain acyl-CoA dehydrogenase activity and fat oxidation are el

42 differentiation by attenuating medium-chain acyl-CoA dehydrogenase activity and that inhibition of t

43 confirmed that conversion is performed by an acyl-CoA dehydrogenase and a subsequent hydratase yieldi

44 Medium-chain acyl-CoA dehydrogenase and acyl-CoA dehydrogenase 9, two

45 he powerful epoxyketone residue involving an acyl-CoA dehydrogenase and an unconventional free-standi

46 and PPARalpha-regulated genes (medium chain acyl-CoA dehydrogenase and pyruvate dehydrogenase kinase

47 or medium-chain acyl CoAs, and medium-chain acyl-CoA dehydrogenase and short-chain acyl-CoA dehydrog

48 y to receive electrons from the medium chain acyl-CoA dehydrogenase and the glutaryl-CoA dehydrogenas

49 atty acids by the mitochondrial medium-chain acyl-CoA dehydrogenase and the peroxisomal acyl-CoA oxid

50 Acyl-CoA dehydrogenases and acyl-CoA oxidases are two cl

51 a tetrameric enzyme that shares a fold with acyl-CoA dehydrogenases and class D flavin-containing mo

52 is similar to those of previously determined acyl-CoA dehydrogenases and consists of an NH2-terminal

53 7 and Phe-320, which are conserved among all acyl-CoA dehydrogenases and coordinate the enzyme-bound

54 base in medium-chain (MCAD) and short-chain acyl-CoA dehydrogenases and is conserved in all members

55 f these ORFs, two had sequence similarity to acyl-CoA dehydrogenases and polyketide synthases, respec

56 lism (eg, pyruvate dehydrogenase complex and Acyl-CoA dehydrogenase) and enzymes involved in electron

57 s, such as acetyl-CoA synthetase, long-chain acyl-CoA dehydrogenase, and 3-hydroxy-3-methylglutaryl-C

58 xidation, such as cytochrome c, medium-chain acyl-CoA dehydrogenase, and adipocyte protein 2.

59 ptide, beta myosin heavy chain, medium chain acyl-CoA dehydrogenase, and adrenomedullin correlate equ

60 nge the basal acyl-CoA oxidase, medium chain acyl-CoA dehydrogenase, and malic enzyme mRNA levels.

61 topropionic acid, an inhibitor of long chain acyl-CoA dehydrogenase, and partially inhibited by 2-tet

62 at liver is compared to that of medium chain acyl-CoA dehydrogenase, and the structural basis for the

63 nitine palmitoyl transferase-1, medium-chain acyl-CoA dehydrogenase, and uncoupling protein 3), calci

64 chain acyl-CoA dehydrogenase and short-chain acyl-CoA dehydrogenase are unable to catalyze oxidation

65 y, it appears that ACAD9 and very-long-chain acyl-CoA dehydrogenase are unable to compensate for each

66 lf-reaction of ETF with porcine medium chain acyl-CoA dehydrogenase are unaltered when alphaT244M ETF

67 The acyl-CoA dehydrogenases are a family of flavin adenine d

68 The acyl-CoA dehydrogenases are a family of flavoenzymes wit

69 The acyl-CoA dehydrogenases are a family of mitochondrial fl

70 The acyl-CoA dehydrogenases are a family of multimeric flavo

71 t is generally held that the active sites of acyl-CoA dehydrogenases are desolvated when substrate bi

72 the suppression of oxygen reactivity in the acyl-CoA dehydrogenases are discussed.

73 eview examines the structure of medium chain acyl-CoA dehydrogenase, as a representative of the dehyd

74 ious work demonstrated that the medium-chain acyl-CoA dehydrogenase both bioactivates and is inhibite

75 inactivation of short chain and medium chain acyl-CoA dehydrogenases by this inhibitor and related 2-

76 miting step in the inactivation of the other acyl-CoA dehydrogenases can involve the abstraction of a

77 nes encoding key mitochondrial (medium-chain acyl-CoA dehydrogenase, carnitine palmitoyltransferase I

78 The medium chain acyl-CoA dehydrogenase catalyzes the flavin-dependent ox

79 The crystal structure of rat short chain acyl-CoA dehydrogenase complexed with the inhibitor acet

80 Children with medium-chain acyl-coenzyme A (acyl-CoA) dehydrogenase defects can metabolize fatty aci

81 Multiple acyl-CoA dehydrogenase deficiencies (MADDs) are a hetero

82 tine are effective in some cases of multiple acyl-CoA dehydrogenase deficiency and primary carnitine

83 ciencies in ETF or ETF-QO result in multiple acyl-CoA dehydrogenase deficiency, a human metabolic dis

84 te methyltransferase deficiency, short-chain acyl-CoA dehydrogenase deficiency, adrenoleukodystrophy,

85 In three patients with very-long-chain acyl-CoA dehydrogenase deficiency, this treatment led ra

86 Two fatty acyl-CoA dehydrogenases (designated FadE1 and FadE2) are

87 on transferring flavoprotein and short chain acyl-CoA dehydrogenase-electron transferring flavoprotei

88 sly expressed and purified FadE28-FadE29, an acyl-CoA dehydrogenase encoded by the igr operon, cataly

89 Rat and human short/branched chain acyl-CoA dehydrogenases exhibit key differences in subst

90 Changes in medium-chain acyl-CoA dehydrogenase expression and acylcarnintine flu

91 beta-oxidation gene (medium and short chain acyl-CoA dehydrogenase) expression levels remain unchang

92 nases and is conserved in all members of the acyl-CoA dehydrogenase family except for IVD and long-ch

93 atalytically essential glutamate base in the acyl-CoA dehydrogenase family is found either on the loo

94 When an acyl-CoA dehydrogenase family member, human short chain

95 elements: the nuclear pore complex (NPC) and acyl-CoA dehydrogenase family member-10 (ACAD10).

96 y been identified as being homologous to the acyl-CoA dehydrogenase family of enzymes.

97 -CoA dehydrogenase is the only member of the acyl-CoA dehydrogenase family with a cationic residue, A

98 ch is a tyrosine in all other members of the acyl-CoA dehydrogenase family, is important for conferri

99 n example of convergent evolution within the acyl-CoA dehydrogenase family, leading to the independen

100 activity, a property of other members of the acyl-CoA dehydrogenase family.

101 tional discrimination between members of the acyl-CoA dehydrogenase family.

102 ely high oxidase activity of the short chain acyl-CoA dehydrogenase from the obligate anaerobe Megasp

103 the targeted inactivation of the long chain acyl CoA dehydrogenase gene (Acadl) are also sensitive t

104 ement (NRRE-1) derived from the medium chain acyl-CoA dehydrogenase gene promoter and nuclear protein

105 susceptibility variations in the short-chain acyl-CoA dehydrogenase gene, and guidelines for the bioc

106 Short chain acyl-CoA dehydrogenase has maximal activity toward butyr

107 Comparison to other acyl-CoA dehydrogenases has provided additional insight

108 otein complex decreased, indicating that the acyl-CoA dehydrogenases have the ability to compete with

109 Short-chain acyl-CoA dehydrogenase (hSCAD) catalyzes the first matri

110 Human short-chain acyl-CoA dehydrogenase (hSCAD) catalyzes the first matri

111 on-transfer properties of human medium-chain acyl-CoA dehydrogenase (hwtMCADH) has been studied using

112 gene regulation of ACAD9 and very-long-chain acyl-CoA dehydrogenase identify the presence of two inde

113 defects have been identified in most of the acyl-CoA dehydrogenases in humans.

114 ydrogenase is also differentiated from other acyl-CoA dehydrogenases in that the catalytic base must

115 atty acids and stimulated gene expression of acyl-CoA dehydrogenases in the liver.

116 g chain acyl-CoA synthetase, very long chain acyl-CoA dehydrogenase) in livers of the ethanol-fed ani

117 of thioester substrates in the medium-chain acyl-CoA dehydrogenase involves alpha-proton abstraction

118 Short chain acyl-CoA dehydrogenase is a homotetramer with a subunit

119 The medium chain acyl-CoA dehydrogenase is rapidly inhibited by racemic 3

120 The overall structure of short chain acyl-CoA dehydrogenase is very similar to those of mediu

121 ed desolvation within the active site of the acyl-CoA dehydrogenases is discussed.

122 efines a side of the binding cavity in other acyl-CoA dehydrogenases is replaced by a leucine (Leu-37

123 ase is very similar to those of medium chain acyl-CoA dehydrogenase, isovaleryl-CoA dehydrogenase, an

124 Crystal structures of human long-chain acyl-CoA dehydrogenase (LCAD) and the catalytically inac

125 A kinetic study of long-chain acyl-CoA dehydrogenase (LCAD) and very long-chain acyl-C

126 Long-chain acyl-CoA dehydrogenase (LCAD) catalyzes the initial step

127 y, none have been documented with long-chain acyl-CoA dehydrogenase (LCAD) deficiency.

128 Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitochondrial fat

129 Long-chain acyl-CoA dehydrogenase (LCAD) is a mitochondrial fatty a

130 studied mice with a deficiency of long-chain acyl-CoA dehydrogenase (LCAD), a key enzyme in mitochond

131 chondrial C(12) oxidation enzyme, long-chain acyl-CoA dehydrogenase (LCAD), also developed periportal

132 genase (IVD), and Glu261 in human long chain acyl-CoA dehydrogenase (LCAD), has been suggested to aff

133 g the fatty acid oxidation enzyme long-chain acyl-CoA dehydrogenase (LCAD).

134 ement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, hav

135 catabolism that is salvaged by the dedicated acyl-CoA dehydrogenase-like flavoenzyme TdaE.

136 nheme FeII-dependent halogenase KtzD and the acyl-CoA dehydrogenase-like flavoprotein KtzA, proposed

137 T2 cells via deleting either Cpt1a or Acadl (acyl-CoA dehydrogenase long chain) restricts alveolar in

138 been performed on the wild-type medium-chain acyl-CoA dehydrogenase (MCAD) and two of its mutant form

139 g of octenoyl-CoA to pig kidney medium chain acyl-CoA dehydrogenase (MCAD) by isothermal titration mi

140 Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-depen

141 Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency is the most com

142 ox and ionization properties of medium-chain acyl-CoA dehydrogenase (MCAD) from pig kidney.

143 ctive site residue, Glu-376, of medium-chain acyl-CoA dehydrogenase (MCAD) has been known to abstract

144 fatty acid synthase (FASN) and medium chain acyl-CoA dehydrogenase (MCAD) protein within the same ce

145 376 --> Asp (E376D) mutation in medium chain acyl-CoA dehydrogenase (MCAD), creates a complementary c

146 identified as Glu376 in porcine medium chain acyl-CoA dehydrogenase (MCAD), Glu254 in human isovalery

147 octynoyl-CoA (inactivator) with medium chain acyl-CoA dehydrogenase (MCAD), were essentially identica

148 in regulating the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyzes the initi

149 The human liver medium chain acyl-CoA dehydrogenase (MCAD)-catalyzed reaction proceed

150 in the recombinant human liver medium-chain acyl-CoA dehydrogenase (MCAD)-catalyzed reaction, we bec

151 here it directly interacts with medium-chain acyl-CoA dehydrogenase (MCAD).

152 model between human ETF and pig medium-chain acyl-CoA dehydrogenase (MCAD).

153 oleacryloyl-CoA) to human liver medium-chain acyl-CoA dehydrogenase (MCAD).

154 oup) upon binding to pig kidney medium-chain acyl-CoA dehydrogenase (MCAD).

155 phenylpropionic acid involving medium-chain acyl-CoA dehydrogenase (MCAD).

156 of the soluble ACADs including medium-chain acyl-CoA dehydrogenase (MCAD).

157 gion of the gene encoding human medium-chain acyl-CoA dehydrogenase (MCAD, which catalyzes a rate-lim

158 ructures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in wh

159 ATP content and medium Acyl-CoA dehydrogenase mRNA were lower in RXRalpha mutan

160 ter introduction of a 2-trans-double bond by acyl-CoA dehydrogenase or acyl-CoA oxidase, the resultan

161 es were reduced (long chain and medium chain acyl-CoA dehydrogenases) or failed to be induced (acyl-C

162 polipoprotein AI, AII, or CIII; medium chain acyl-CoA dehydrogenase; or stearoyl-CoA desaturase mRNAs

163 trate-binding cavity relative to short-chain acyl-CoA dehydrogenase, permitting the optimal binding o

164 Moreover, the FAO enzyme very-long-chain acyl-CoA dehydrogenase physically interacted with TFP, t

165 synthases (pltB, pltC), an acyl coenzyme A (acyl-CoA) dehydrogenase (pltE), an acyl-CoA synthetase (

166 n the reaction catalyzed by pig medium-chain acyl-CoA dehydrogenase (pMCAD) has been investigated usi

167 With the exception of long-chain acyl-CoA dehydrogenase protein level, which was increase

168 Comparing the structures of four other acyl-CoA dehydrogenases provides further insights into t

169 tative mitochondria-targeted, bacterial-type acyl-CoA dehydrogenase (PtMACAD1) that is present in Str

170 se), 3-hydroxybutyryl-CoA dehydrogenase, and acyl-CoA dehydrogenase, respectively.

171 CoA dehydrogenase (LCAD) and very long-chain acyl-CoA dehydrogenase revealed that 5-trans-tetradeceno

172 ns is dehydrogenated by short/branched-chain acyl-CoA dehydrogenase (SBCAD).

173 Rat short/branched chain acyl-CoA dehydrogenases (SBCAD) are more active toward s

174 Short chain acyl-CoA dehydrogenase (SCAD) is a homotetrameric flavoe

175 f liver-specific expression of a short-chain acyl-CoA dehydrogenase (SCAD) transgene in the SCAD-defi

176 late on substrate specificity in short chain acyl-CoA dehydrogenase (SCAD).

177 and E376Q mutants of the human medium chain acyl-CoA dehydrogenase showed that these two active site

178 te of FkbI reveal key differences from other acyl-CoA dehydrogenases, suggesting that FkbI may recogn

179 , which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins.

180 Structurally, the enzyme is a member of the acyl-CoA dehydrogenase superfamily.

181 places it into the well-characterized fatty acyl-CoA dehydrogenase superfamily.

182 nzyme nitroalkane oxidase is a member of the acyl-CoA dehydrogenase superfamily.

183 arget the FAD of the medium- and short-chain acyl-CoA dehydrogenases support this conclusion.

184 regulatory circuit involving a heat-induced acyl-CoA dehydrogenase that controls the lipid saturatio

185 drogenase 9 (ACAD9) is a recently identified acyl-CoA dehydrogenase that demonstrates maximum activit

186 longs to an important flavoprotein family of acyl-CoA dehydrogenases that catalyze the alpha,beta-deh

187 detectable semiquinone; however, like other acyl-CoA dehydrogenases, the human enzyme stabilizes an

188 mV), the greatest magnitude measured in any acyl-CoA dehydrogenase to date.

189 er flavoprotein that shuttles electrons from acyl-CoA dehydrogenases to coenzyme Q.

190 ydrogenase kinase, medium-chain length fatty acyl-CoA dehydrogenase, ubiquinone-cytochrome c reductas

191 the two human genes encoding very long chain acyl-CoA dehydrogenase (VLCAD) and postsynaptic density

192 Very-long-chain acyl-CoA dehydrogenase (VLCAD) catalyzes the first step

193 Very long acyl-CoA dehydrogenase (VLCAD) deficiency is a genetic p

194 Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is an inherite

195 Very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency is the most co

196 ents have been found to have very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency, none have bee

197 hibit down-regulation of the very-long-chain acyl-CoA dehydrogenase (VLCAD) enzyme, which exacerbates

198 Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a major enzyme catalys

199 Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a member of the family

200 Very long-chain acyl-CoA dehydrogenase (VLCAD) is an inner mitochondrial

201 Very long chain acyl-CoA dehydrogenase (VLCAD; ACADVL) was found to be o

202 s highly homologous to human very-long-chain acyl-CoA dehydrogenase was identified by large-scale ran

203 hydrogenase family member, human short chain acyl-CoA dehydrogenase, was incubated with dimethylglyci

204 With the known structure of medium chain acyl-CoA dehydrogenase, we hypothesize a possible struct

205 the fatty acid oxidation enzyme medium-chain acyl-CoA dehydrogenase, we tested whether acetylation-de

206 nitine palmitoyltransferase and medium-chain acyl-CoA dehydrogenase were unaltered with fasting.

207 -CoAs are poor substrates of very long-chain acyl-CoA dehydrogenase when compared with myristoyl-CoA.

208 ETF catalyzed by sarcosine and medium chain acyl-CoA dehydrogenases which reduce the flavin to the s

209 near Acads, a gene encoding the short chain acyl CoA dehydrogenase, which is mutated in BALB/cByJ mi

210 vity and steady-state levels of medium-chain acyl-CoA dehydrogenase, which catalyzes a rate-limiting

211 loning revealed that IBR3 encodes a putative acyl-CoA dehydrogenase with a consensus peroxisomal targ

212 CoA dehydrogenase, and bacterial short chain acyl-CoA dehydrogenase with a three-domain structure com

213 The turnover of medium chain acyl-CoA dehydrogenase with native ETF and ETF containin