ライフサイエンスコーパス: methylesterase

1 enzymes, CheR (methyltransferase) and CheB (methylesterase).

2 tic action for the methyltransferase and the methylesterase.

3 logy to human carboxyl methyltransferase and methylesterase.

4 ansferase and removed by a specific carboxyl methylesterase.

5 ymes: CheR, a methyltransferase, and CheB, a methylesterase.

6 at binds the CheR methyltransferase and CheB methylesterase.

7 ucine carboxymethyltransferase 1/phosphatase methylesterase 1 (LCMT-1/PME-1).

8 ansferase 1 (LCMT-1) and protein phosphatase methylesterase 1 (PME-1) and regulates PP2A holoenzyme f

9 The serine hydrolase protein phosphatase methylesterase-1 (PME-1) regulates the methylesterificat

10 ficient in PP2A-specific protein phosphatase methylesterase-1 (PME-1), indicating a role for the PP2A

11 the PP2A methylesterase, protein phosphatase methylesterase-1 (PME-1), or the PP2A methyltransferase,

12 the PP2A repressor, the protein phosphatase methylesterase-1 (PME-1), thus preserving the methylatio

13 r proteins, herein named protein phosphatase methylesterase-1 (PME-1), was purified and microsequence

14 such target, the enzyme protein phosphatase methylesterase-1 (PME-1), which regulates the methyleste

15 mmalian serine hydrolase protein-phosphatase methylesterase-1 (PME-1).

16 Streptonigrin methylesterase A (StnA) is one of the tailoring enzymes

17 icate that the basis for the nearly 100-fold methylesterase activation upon phosphorylation is due to

18 at the deletion strain is unable to modulate methylesterase activity after serine addition or photost

19 t only relieves inhibition of the C-terminal methylesterase activity but also provides an enhancement

20 e of the C-terminal domain and thus inhibits methylesterase activity by directly restricting access t

21 During chemotaxis, the changes of methylesterase activity in C gelida cells were similar t

22 utations in CheB that show an enhancement of methylesterase activity in the absence of phosphorylatio

23 within the regulatory domain, the C-terminal methylesterase activity is stimulated, resulting in the

24 domain of histidine kinase CheA inhibits the methylesterase activity of CheB and that this inhibition

25 egulator, the regulatory domain inhibits the methylesterase activity of the effector domain.

26 ylated state, the regulatory domain inhibits methylesterase activity of the effector domain.

27 regulatory domain leads to an enhancement of methylesterase activity through a relief of inhibition a

28 a statistically significant effect on pectin methylesterase activity, typically at or lower than 60 H

29 tor substrate and simultaneously stimulating methylesterase activity.

30 emselves participate in signal transduction: methylesterases, adenylate or diguanylate cyclases, c-di

31 undermethylated fusion protein purified from methylesterase and methyltransferase-deficient E. coli,

32 ll wall pectins through the action of pectin-methylesterase and pectate-lyase that possibly originate

33 moderate electric field treatments on pectin methylesterase and polygalcturonase activities in tomato

34 This is the first structure of a pectin methylesterase and reveals the enzyme to comprise a righ

35 Interestingly, both MeSA methylesterase and SA methyltransferase, which catalyze

36 that lack the receptor methyltransferase and methylesterase and why motors show signal-dependent FliM

37 sociated with cell wall modification (pectin methylesterase) and biosynthesis (cellulose synthase).

38 uding the NWETF sequence that binds the CheR methylesterase, are missing in Tap.

39 tors was thought to be catalyzed by the CheB methylesterase, as is the case for E. coli receptors.

40 In in vitro methylesterase assays in the presence of Mg(2+), the ana

41 Finally, studies of methylesterase catalysis by the free catalytic domain in

42 Methylesterase CheB and methyltransferase CheR modulate

43 Escherichia coli, methyltransferase CheR and methylesterase CheB bind both substrate sites and a carb

44 Methylesterase CheB functions together with methyltransf

45 Methylesterase CheB is a two-domain response regulator c

46 l structure of the unphosphorylated state of methylesterase CheB shows that the regulatory domain blo

47 on, or the methyltransferase CheR and/or the methylesterase CheB to examine the roles of accelerated

48 We report the x-ray crystal structure of the methylesterase CheB, a phosphorylation-activated respons

49 ylated CheY, and also that phosphatase CheZ, methylesterase CheB, and methyltransferase CheR would be

50 ined, those of transcription factor NarL and methylesterase CheB, both revealed extensive interdomain

51 ing either the methyltransferase CheR or the methylesterase CheB.

52 cated methyltransferase CheR and a dedicated methylesterase CheB.

53 ions catalyzed by methyltransferase CheR and methylesterase CheB.

54 ions catalyzed by methyltransferase CheR and methylesterase CheB.

55 in both the presence and the absence of the methylesterase CheB.

56 ates catalyzed by methyltransferase CheR and methylesterase CheB.

57 r methyltransferase (cheR) and chemoreceptor methylesterase (cheB) genes present in the mcpA operon.

58 otein methyltransferase (CheR) and a protein methylesterase (CheB) that catalyze the methylation and

59 We purified a Carica papaya pectin methylesterase (CpL-PME; EC 3.1.1.11) from a commercial

60 entapeptide serves as a docking site for the methylesterase/deamidase and that the truncated receptor

61 ty from the product by treatment with pectin methylesterase, demonstrated that the bulk of the methyl

62 led that interaction of the sequence and the methylesterase enhanced the rate constant of demethylati

63 rified polymer, demethylesterified by pectin methylesterase enzymes and cross-linked by calcium ions

64 esterified by specific methyltransferase and methylesterase enzymes at a completely conserved C-termi

65 in mucilage, potentially by recycling pectin methylesterase enzymes in the endomembrane system of see

66 l terminus by specific methyltransferase and methylesterase enzymes which have been purified, but not

67 Here, we identified this activity as methylesterase family member 16 (MES16; At4g16690).

68 We identify a pectin methylesterase gene, PME6, which is highly expressed in

69 genomes for the presence of putative pectin methylesterase genes and conducted a sequence analysis o

70 f PP2A in cell lysates with recombinant PP2A methylesterase greatly decreased the amount of C subunit

71 Pectin methylesterase has no significant sequence similarity wi

72 Sequence conservation among the pectin methylesterases has been mapped onto the structure and r

73 genic plants overproducing isoprenylcysteine methylesterase (ICME) exhibit ABA hypersensitivity in st

74 o decreased after ectopic expression of PP2A methylesterase in Neuro-2a (N2a) cells.

75 okadaic acid, a known inhibitor of the PP2A methylesterase, inhibited this reaction.

76 A pectin methylesterase inhibitor (SolyPMEI) from tomato has been

77 pectin methylesterase inhibitor and a pectin methylesterase inhibitor -pectin methylesterase, respect

78 0g02150 and Glyma10g02160, encoding a pectin methylesterase inhibitor and a pectin methylesterase inh

79 he impaired locus was identified as a pectin methylesterase inhibitor gene, PECTIN METHYLESTERASE INH

80 elated to the confirmed presence of a pectin methylesterase inhibitor.

81 pectin methylesterase inhibitor gene, PECTIN METHYLESTERASE INHIBITOR6 (PMEI6), specifically expresse

82 walls and are regulated by endogenous pectin methylesterase inhibitors (PMEIs).

83 parably large number of proteinaceous pectin methylesterase inhibitors (PMEIs; 76 members in Arabidop

84 Two of these genes encode pectin methylesterase inhibitors, which, when ectopically expre

85 The methylesterase is a two-domain response regulator in whi

86 The structure of pectin methylesterase is an example of a new family of esterase

87 unable to construct ripples, whereas a frzG methylesterase mutant forms numerous, tightly packed rip

88 However, prenylcysteine alpha-carboxyl methylesterase (PCME) activity has not been described in

89 non-rafts wherein small amounts of the PP2A methylesterase PME-1 are exclusively present.

90 The PP2A methylesterase PME-1 limits the activity of PP2A by deme

91 ation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to h

92 A continuous, fluorometric assay for pectin methylesterase (PME) activity is described.

93 Pectin methylesterase (PME) and polygalacturonase (PG) activiti

94 ivity of the pectin-modifying enzymes pectin-methylesterase (PME) and polygalacturonase (PG) in tomat

95 Pectin methylesterase (PME) controls the methylesterification s

96 )QTL2.2 and a region containing three pectin methylesterase (PME) genes underlying Fir(s.p.)QTL2.5 we

97 bsequently deesterified by the enzyme pectin methylesterase (PME) in a process that exposes acidic re

98 es empirical evidence for the role of Pectin Methylesterase (PME) in influencing solid wood character

99 Pectin methylesterase (PME) is responsible for the demethylatio

100 th sequences common to genes encoding pectin methylesterase (PME) was found to be tightly correlated,

101 Pectin methylesterase (PME), a ubiquitous enzyme in plants, de-

102 notation predicts that QRT1 encodes a pectin methylesterase (PME), and enzymatic assays of QRT1 expre

103 pectin to be de-methyl-esterified by pectin methylesterase (PME), and that the PG beta-subunit prote

104 d cell wall-modifying enzymes, namely pectin methylesterase (PME), beta-galactosidase (beta-Gal), end

105 Here, we examined whether or not pectin methylesterase (PME), one of the few cellular proteins k

106 In contrast, poppy gene homologues to pectin methylesterase (PME), pectin acetylesterase (PAE) and pe

107 ovide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the esse

108 cco leaf cell walls and identified as pectin methylesterase (PME).

109 e basis for a gel diffusion assay for pectin methylesterase (PME, EC 3.1.1.11) activity.

110 hanol in tomato fruit is regulated by pectin methylesterase (PME, EC 3.1.1.11), an enzyme that cataly

111 urther accentuated by overexpression of PP2A methylesterase (PME-1) but cannot be rescued by PME-1 kn

112 pically affects the activity of plant pectin methylesterases (PMEs) and is inactive against a microbi

113 Many pectin methylesterases (PMEs) are expressed in plants to modify

114 Pectin methylesterases (PMEs) catalyze the demethylesterificati

115 Pectin methylesterases (PMEs) catalyze the demethylesterificati

116 Pectin methylesterases (PMEs) demethylate homogalacturonan (HG)

117 hypothesis is that high expression of pectin methylesterases (PMEs) increases Ca(2)(+) bound to the c

118 oes not contain cellulose or callose, pectin methylesterases (PMEs) likely play a central role in the

119 lgi and are partially deesterified by pectin methylesterases (PMEs) upon export to the cell wall.

120 onans, mediated through the action of pectin methylesterases (PMEs), influences the biophysical prope

121 ion of pectin is controlled mainly by pectin methylesterases (PMEs), whose activity is posttranscript

122 ion is spatiotemporally controlled by pectin methylesterases (PMEs; 66 members in Arabidopsis [Arabid

123 en is partially demethylesterified by pectin methylesterases (PMEs; EC 3.1.1.11).

124 -hybrid screen identified Arabidopsis pectin methylesterase protein 3 (PME3) as strongly and specific

125 ed transgenic mice that overexpress the PP2A methylesterase, protein phosphatase methylesterase-1 (PM

126 hange in the catalytic rate constant for the methylesterase reaction.

127 to activate or inactivate endogenous pectin methylesterase, respectively.

128 nd a pectin methylesterase inhibitor -pectin methylesterase, respectively.

129 Pectin methylesterase showed a negligible activity which is rel

130 e, we report the crystal structure of pectin methylesterase that has neither the common alpha/beta hy

131 ously overlooked intermediate, and Dph7 is a methylesterase that hydrolyzes methylated diphthine to p

132 -specific movement factors, including pectin methylesterase, that are involved in regulating plasmode

133 including the SABATH methyltransferases, the methylesterases, the GH3 acyl acid-amido synthetases, an

134 PME-1 represents the first mammalian protein methylesterase to be cloned.

135 nofuranosidase, polygalacturonase and pectin methylesterase, were measured.

136 h as RNA binding and interaction with pectin methylesterases, were not affected.

137 of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those obser