ライフサイエンスコーパス: hydroxyacyl-CoA dehydrogenase

1 tty acid binding protein), and Hadh (encodes hydroxyacyl-CoA dehydrogenase).

2 to aspects of the catalytic mechanism of l-3-hydroxyacyl-CoA dehydrogenase.

3 may have a Glu474Gln mutation in long-chain hydroxyacyl-CoA dehydrogenase.

4 ied as an essential catalytic residue of L-3-hydroxyacyl-CoA dehydrogenase.

5 fer substantially from the classic, type I 3-hydroxyacyl-CoA dehydrogenases.

6 hase, a marker of oxidative metabolism; beta-hydroxyacyl-CoA dehydrogenase, a marker of lipolytic met

7 rome-c-oxidase, lactate dehydrogenase, and 3-hydroxyacyl-CoA dehydrogenase activities were found to b

8 mumol.min-1.mg protein-1; P < .05) and beta-hydroxyacyl-CoA dehydrogenase activity (normal, 0.27 +/-

9 etabolize fat, as indicated by measures beta-hydroxyacyl-CoA dehydrogenase activity or its ratio to c

10 Consistent with the hypothesis, l-3-hydroxyacyl-CoA dehydrogenase activity was inhibited by

11 rate-limiting enzyme in beta-oxidation (beta-hydroxyacyl-CoA dehydrogenase activity) were reduced by

12 lactate dehydrogenase, pyruvate kinase and 3-hydroxyacyl-CoA dehydrogenase activity.

13 atty acid transporters CD36 and CPT1 or beta-hydroxyacyl-CoA dehydrogenase activity.

14 protein level, and a tendency for reduced 3-hydroxyacyl-CoA dehydrogenase activity.

15 Human type II hydroxyacyl-CoA dehydrogenase/amyloid-beta binding alcoh

16 a 6.1-fold decrease in the kcat/k(m) of L-3-hydroxyacyl-CoA dehydrogenase and a 10-fold increase in

17 ildren had a deficiency only of long-chain 3-hydroxyacyl-CoA dehydrogenase and presented with hypoket

18 across high-altitude taxa included increased hydroxyacyl-coA dehydrogenase and succinate dehydrogenas

19 y an enzyme in the beta-oxidation pathway (3-hydroxyacyl-CoA dehydrogenase), and increased synthesis

20 long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain 3-ketoacyl

21 he only histidine conserved in all known L-3-hydroxyacyl-CoA dehydrogenases, and since its counterpar

22 f which (2-trans enoyl-CoA hydratase and L-3-hydroxyacyl-CoA dehydrogenase) are core activities requi

23 endent pathway is the higher activity of L-3-hydroxyacyl-CoA dehydrogenase as compared with Delta3,De

24 n from a peroxisomal enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme gene p

25 tic functions of human brain short chain L-3-hydroxyacyl-CoA dehydrogenase could weaken the protectiv

26 hway and D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase (D-PBE) of the noninducibl

27 metabolic disease states correlated with L-3-hydroxyacyl-CoA dehydrogenase deficiencies.

28 In 24 children with 3-hydroxyacyl-CoA dehydrogenase deficiency, we used DNA am

29 Toxoplasma consisting of one N-terminal d-3-hydroxyacyl-CoA dehydrogenase domain fused to two tandem

30 renal function include enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (EHHADH) and apolipoprotei

31 ma cultures rely on fatty acid oxidation and hydroxyacyl-CoA dehydrogenase for their survival upon MA

32 A novel L-3-hydroxyacyl-CoA dehydrogenase from human brain has been

33 The human short chain L-3-hydroxyacyl-CoA dehydrogenase gene is organized into six

34 RAP150, to the mouse enoyl-CoA hydratase/l-3-hydroxyacyl-CoA dehydrogenase gene promoter.

35 tion is encoded by the human short chain L-3-hydroxyacyl-CoA dehydrogenase gene.

36 l-3-Hydroxyacyl-CoA dehydrogenase (HAD), the penultimate enz

37 and glucose; (3) an increase in muscle beta-hydroxyacyl-CoA dehydrogenase (HADH) and adipose lipopro

38 vity levels of the mitochondrial enzyme beta-hydroxyacyl-CoA-dehydrogenase (HADH) can indicate previo

39 also had significantly decreased activity of hydroxyacyl-CoA dehydrogenase (HADHA) and accumulated mo

40 arnitine palmitoyltransferase 1a (CPT1a) and hydroxyacyl-CoA dehydrogenase (HADHA) enzymes.

41 teroid dehydrogenase type 10/short chain L-3-hydroxyacyl-CoA dehydrogenase have been investigated.

42 yl-CoA oxidase (ACOX), enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD), and thiolase, has be

43 se (THIO), peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD), peroxisomal membrane

44 Measurement of the activity of L-3-hydroxyacyl-CoA dehydrogenase in cultured skin fibroblas

45 The activity of beta-hydroxyacyl-CoA dehydrogenase increased with GW610742 (P

46 ain (C18:0) substrates, whereas the MFP2 L-3-hydroxyacyl-CoA dehydrogenase is active on C6:0, C12:0 a

47 f the second enzyme, enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L-PBE) of the inducible p

48 udy, the function of enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase (L-PBE), the second enzyme

49 purification of human brain short chain L-3-hydroxyacyl-CoA dehydrogenase made it possible to charac

50 of valine-enriched transcripts, among which hydroxyacyl-CoA dehydrogenase mRNA encodes for a key enz

51 that His450 is the catalytic residue of L-3-hydroxyacyl-CoA dehydrogenase of the E. coli multifuncti

52 roperties of 3-ketoacyl-CoA thiolase and l-3-hydroxyacyl-CoA dehydrogenase of the mutant complexes we

53 2-terminal hydratase and the COOH-terminal 3-hydroxyacyl-CoA dehydrogenase, result in a unique neurom

54 l-3-Hydroxyacyl-CoA dehydrogenase reversibly catalyzes the c

55 Human heart short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) catalyzes the oxid

56 Sequencing of the short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) genomic DNA from t

57 with inactivating mutations of short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD) was examined in mi

58 Human brain short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was found to catal

59 mutations in the gene encoding short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD), a ubiquitously ex

60 ubiquitously expressed enzyme short-chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD).

61 Exercise training increased mtDNA and beta-hydroxyacyl-CoA dehydrogenase similarly in WT and CD36-K

62 nsferase, carnitine palmitoyltransferase 1A, hydroxyacyl-CoA-dehydrogenase, Sirtuin 6 (SIRT6), and AM

63 a-peptide (Abeta)-binding protein (ERAB)/L-3-hydroxyacyl-CoA dehydrogenase type II (HADH II) is expre

64 Here, we report that L-3-hydroxyacyl-CoA dehydrogenase type II/amyloid binding al

65 xyacyl-coenzyme A dehydrogenase (HADH) and 3-hydroxyacyl-CoA dehydrogenase type-2 (HSD17B10), were fu

66 -/-) hearts, we measured the activity of l-3-hydroxyacyl-CoA dehydrogenase, which was acetylated in t

67 37 +/- 8% versus O(TR) 97 +/- 33%) and beta-hydroxyacyl-CoA-dehydrogenase (Y(TR) 31 +/- 7%, versus O