ライフサイエンスコーパス: DGPP

1 DGPP inhibited the ability of PAP2 to dephosphorylate PA

2 DGPP phosphatase (DGPP phosphohydrolase) is a membrane-a

3 DGPP phosphatase activity was absent in pgpB mutant cell

4 DGPP phosphatase activity was associated with the 34-kDa

5 DGPP phosphatase activity was inhibited by zinc by a mec

6 DGPP phosphatase also catalyzed the dephosphorylation of

7 DGPP phosphatase catalyzed the dephosphorylation of the

8 DGPP phosphatase exhibited typical saturation kinetics w

9 DGPP phosphatase had a broad pH optimum between 6.0 and

10 DGPP phosphatase possesses a Mg2+-independent PA phospha

11 DGPP phosphatase was predicted to be an integral membran

12 DGPP phosphatase was purified 33,333-fold from Saccharom

13 DGPP phosphatases (DGPP phosphohydrolase) from Saccharom

14 DGPP stimulated the activity of pure phosphatidylserine

15 DGPP was neither a substrate nor an inhibitor of pure ph

16 DGPP was synthesized from phosphatidate via the phosphat

17 DGPP was the preferred substrate for the enzyme with a s

18 In addition, DGPP potently inhibited (Ki = 0.35 mol %) the dephosphor

19 oduct also exhibited lyso-PA phosphatase and DGPP phosphatase activities.

20 and S1P-induced increases in resistance, and DGPP (8:0) inhibited LPA-induced transcellular resistanc

21 ects: (1) degradation of flavonoids, such as DGPP and hesperidin; (2) destruction of the cell wall st

22 Intracellular signaling initiated by DGPP includes phosphorylation and activation of the Grou

23 the reaction catalyzed by the S. cerevisiae DGPP phosphatase.

24 We characterized DGPP phosphatase activity in membranes from cells overpr

25 isiae was shown to be similar to the E. coli DGPP phosphatase in its ability to utilize lyso-PA and p

26 These results establish DGPP as a novel macrophage-activating factor and suggest

27 hosphatase activity and accumulated (4-fold) DGPP.

28 PAP2 exhibited a high affinity for DGPP (Km = 0.04 mol %).

29 The specificity constant (Vmax/Km) for DGPP was 1.3-fold higher than that of PA.

30 The specificity constant (Vmax/Km) for DGPP was 9.3-fold greater than that for PA.

31 he specificity constants (V(max)/K(m)()) for DGPP of the R125A mutant and H233A mutant enzymes were 4

32 The Km value for DGPP was 3-fold greater than its cellular concentration

33 reduced V(max) and elevated K(m) values for DGPP when compared with the wild-type enzyme.

34 Amino acid sequence information derived from DGPP phosphatase was used to identify and isolate the DP

35 The enzyme removes the beta phosphate from DGPP to form phosphatidate.

36 of 3',5'-di-C-beta-glucopyranosylphloretin (DGPP) decreased drastically.

37 as 3',5'-di-C-beta-glucopyranosylphloretin (DGPP), acacetin 8-C-neohesperidoside (margaritene), acac

38 t): 3',5'-di-C-beta-glucopyranosylphloretin (DGPP, 285.9 +/- 2.9 mg/100g), acacetin 8-C-neohesperidos

39 r of substrate preference was PA > lyso-PA > DGPP.

40 a novel phosphatase sequence motif found in DGPP phosphatase and in the mouse Mg2+-independent PA ph

41 member of a phosphatase family that includes DGPP phosphatases from S. cerevisiae and E. coli.

42 ylserine and phosphatidylinositol, inhibited DGPP phosphatase activity by a mixed mechanism that caus

43 dpp1Delta lpp1Delta double mutant that lacks DGPP phosphatase activity.

44 phosphatase sequence motif had no measurable DGPP phosphatase activity.

45 The R125A and H233A mutant DGPP phosphatase enzymes had reduced V(max) and elevated

46 Mg2+-independent PA phosphatase activity of DGPP phosphatase purified from S. cerevisiae was inhibit

47 Analyses of DGPP phosphatase mRNA and protein levels, and expression

48 ichia coli catalyze the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyze the d

49 iae which catalyzes the dephosphorylation of DGPP to yield phosphatidate (PA) and then catalyzes the

50 and measurement of the dephosphorylation of DGPP.

51 rat liver catalyzed the dephosphorylation of DGPP.

52 A, and PA inhibited the dephosphorylation of DGPP.

53 ate did not inhibit the dephosphorylation of DGPP.

54 The mutant was devoid of DGPP phosphatase activity and accumulated (4-fold) DGPP.

55 e examined the hypothesis that expression of DGPP phosphatase was regulated by zinc availability.

56 nc by a mechanism that involved formation of DGPP-zinc complexes.

57 in a dose-dependent increase in the level of DGPP phosphatase activity in both exponential and statio

58 . cerevisiae regulate the cellular levels of DGPP, PA, and diacylglycerol.

59 ession correlated with the overexpression of DGPP phosphatase activity in S. cerevisiae and in insect

60 P1 gene directed a 10-fold overexpression of DGPP phosphatase activity in S. cerevisiae.

61 lls resulted in a 500-fold overexpression of DGPP phosphatase activity over that expressed in wild-ty

62 The regulation pattern of DGPP phosphatase in mutants defective in plasma membrane

63 e dephosphorylation of the beta phosphate of DGPP to form PA followed by the dephosphorylation of PA

64 e dephosphorylation of the beta phosphate of DGPP to yield phosphatidate and Pi.

65 e dephosphorylation of the beta phosphate of DGPP.

66 Regulation of DGPP phosphatase by inositol and growth phase occurred i

67 Regulation of DGPP phosphatase expression by inositol supplementation,

68 l- and growth phase-dependent regulations of DGPP phosphatase were additive.

69 DGPP phosphatase (DGPP phosphohydrolase) is a membrane-associated 34-kDa e

70 DGPP phosphatases (DGPP phosphohydrolase) from Saccharomyces cerevisiae and

71 Pure DGPP phosphatase from Saccharomyces cerevisiae was shown

72 metabolism of diacylglycerol pyrophosphate (DGPP) is involved in a novel lipid signaling pathway.

73 Diacylglycerol pyrophosphate (DGPP) is involved in a putative novel lipid signaling pa

74 coli exhibited diacylglycerol pyrophosphate (DGPP) phosphatase activity.

75 e DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol supplementation and growth

76 e DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase enzyme accounts for half of the Mg2+-i

77 gene, encoding diacylglycerol pyrophosphate (DGPP) phosphatase from Saccharomyces cerevisiae, has rec

78 Diacylglycerol pyrophosphate (DGPP) phosphatase is a novel membrane-associated enzyme

79 Diacylglycerol pyrophosphate (DGPP) phosphatase, encoded by the DPP1 gene, is a membra

80 l phospholipid diacylglycerol pyrophosphate (DGPP), identified in bacteria, yeast, and plants, but no

81 xin (PTX) or dioctyl-glycerol pyrophosphate (DGPP 8:0) was added along with LPA or S1P in separate ex

82 c antagonist dioctyl-glycerol pyrophosphate (DGPP) blocked the LPA response, but not the S1P response

83 n analysis of a dpp1Delta mutant showed that DGPP phosphatase played a role in the regulation of phos

84 The DGPP phosphatase activities of the R125A, the H169A, and

85 phatase activities of rat liver PAP2 and the DGPP phosphatase of S. cerevisiae regulate the cellular

86 The pH optimum for the DGPP phosphatase reaction was 6.5.

87 uence motif in the enzyme is involved in the DGPP phosphatase reaction.

88 yso-PA phosphatase activities and all of the DGPP phosphatase activity in S. cerevisiae.

89 ere 0.05, 9, and 0.03%, respectively, of the DGPP phosphatase activity of the wild-type enzyme.

90 +-independent PA phosphatase activity of the DGPP phosphatase enzyme.

91 Induction of the DGPP phosphatase protein and activity by zinc deprivatio

92 The deduced primary structure of the DGPP phosphatase protein contains a three-domain phospha

93 The substrate and product of the DGPP phosphatase reaction play roles in lipid signaling

94 unofluorescence microscopy revealed that the DGPP phosphatase enzyme was localized to the vacuolar me

95 Mouse PAP2 showed homology to DGPP phosphatases from S. cerevisiae and E. coli, especi

96 typical saturation kinetics with respect to DGPP (Km = 0.55 mol %).

97 The responses to DGPP are compatible with a receptor-recognition event be

98 Macrophage responses to DGPP are specific and are not mediated by its conversion

99 ds contributing to antioxidant activity were DGPP and apigenin 8-C-neohesperidoside, which could be e

100 extract are nobiletin and tangeretin, while DGPP and hesperidin are in the hot water extract.