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1  enzymes, CheR (methyltransferase) and CheB (methylesterase).
2 ymes: CheR, a methyltransferase, and CheB, a methylesterase.
3 tic action for the methyltransferase and the methylesterase.
4 logy to human carboxyl methyltransferase and methylesterase.
5 ansferase and removed by a specific carboxyl methylesterase.
6 contacts at structured cores to activate the methylesterase.
7 at binds the CheR methyltransferase and CheB methylesterase.
8 ucine carboxymethyltransferase 1/phosphatase methylesterase 1 (LCMT-1/PME-1).
9 ansferase 1 (LCMT-1) and protein phosphatase methylesterase 1 (PME-1) and regulates PP2A holoenzyme f
10                                         PP2A methylesterase 1 (PME-1) is a cancer-promoting enzyme an
11  phosphatase 2A (CIP2A), protein phosphatase methylesterase 1 (PME-1), and SET nuclear proto-oncogene
12     The serine hydrolase protein phosphatase methylesterase-1 (PME-1) regulates the methylesterificat
13 ficient in PP2A-specific protein phosphatase methylesterase-1 (PME-1), indicating a role for the PP2A
14 the PP2A methylesterase, protein phosphatase methylesterase-1 (PME-1), or the PP2A methyltransferase,
15  the PP2A repressor, the protein phosphatase methylesterase-1 (PME-1), thus preserving the methylatio
16 r proteins, herein named protein phosphatase methylesterase-1 (PME-1), was purified and microsequence
17  such target, the enzyme protein phosphatase methylesterase-1 (PME-1), which regulates the methyleste
18 mmalian serine hydrolase protein-phosphatase methylesterase-1 (PME-1).
19                                Streptonigrin methylesterase A (StnA) is one of the tailoring enzymes
20 ) is a cancer-promoting enzyme and undergoes methylesterase activation upon binding to the PP2A core
21 icate that the basis for the nearly 100-fold methylesterase activation upon phosphorylation is due to
22 at the deletion strain is unable to modulate methylesterase activity after serine addition or photost
23 t only relieves inhibition of the C-terminal methylesterase activity but also provides an enhancement
24 e of the C-terminal domain and thus inhibits methylesterase activity by directly restricting access t
25            During chemotaxis, the changes of methylesterase activity in C gelida cells were similar t
26 utations in CheB that show an enhancement of methylesterase activity in the absence of phosphorylatio
27 within the regulatory domain, the C-terminal methylesterase activity is stimulated, resulting in the
28 domain of histidine kinase CheA inhibits the methylesterase activity of CheB and that this inhibition
29 egulator, the regulatory domain inhibits the methylesterase activity of the effector domain.
30 ylated state, the regulatory domain inhibits methylesterase activity of the effector domain.
31 regulatory domain leads to an enhancement of methylesterase activity through a relief of inhibition a
32 a statistically significant effect on pectin methylesterase activity, typically at or lower than 60 H
33 tor substrate and simultaneously stimulating methylesterase activity.
34 emselves participate in signal transduction: methylesterases, adenylate or diguanylate cyclases, c-di
35 undermethylated fusion protein purified from methylesterase and methyltransferase-deficient E. coli,
36 ll wall pectins through the action of pectin-methylesterase and pectate-lyase that possibly originate
37 moderate electric field treatments on pectin methylesterase and polygalcturonase activities in tomato
38      This is the first structure of a pectin methylesterase and reveals the enzyme to comprise a righ
39                     Interestingly, both MeSA methylesterase and SA methyltransferase, which catalyze
40 that lack the receptor methyltransferase and methylesterase and why motors show signal-dependent FliM
41 sociated with cell wall modification (pectin methylesterase) and biosynthesis (cellulose synthase).
42 uding the NWETF sequence that binds the CheR methylesterase, are missing in Tap.
43 tors was thought to be catalyzed by the CheB methylesterase, as is the case for E. coli receptors.
44                                  In in vitro methylesterase assays in the presence of Mg(2+), the ana
45                          Finally, studies of methylesterase catalysis by the free catalytic domain in
46                                              Methylesterase CheB and methyltransferase CheR modulate
47 Escherichia coli, methyltransferase CheR and methylesterase CheB bind both substrate sites and a carb
48                                              Methylesterase CheB functions together with methyltransf
49                                              Methylesterase CheB is a two-domain response regulator c
50 l structure of the unphosphorylated state of methylesterase CheB shows that the regulatory domain blo
51 on, or the methyltransferase CheR and/or the methylesterase CheB to examine the roles of accelerated
52 We report the x-ray crystal structure of the methylesterase CheB, a phosphorylation-activated respons
53 ylated CheY, and also that phosphatase CheZ, methylesterase CheB, and methyltransferase CheR would be
54 ined, those of transcription factor NarL and methylesterase CheB, both revealed extensive interdomain
55 ates catalyzed by methyltransferase CheR and methylesterase CheB.
56 ing either the methyltransferase CheR or the methylesterase CheB.
57 cated methyltransferase CheR and a dedicated methylesterase CheB.
58 ions catalyzed by methyltransferase CheR and methylesterase CheB.
59  in both the presence and the absence of the methylesterase CheB.
60 r methyltransferase (cheR) and chemoreceptor methylesterase (cheB) genes present in the mcpA operon.
61 otein methyltransferase (CheR) and a protein methylesterase (CheB) that catalyze the methylation and
62           We purified a Carica papaya pectin methylesterase (CpL-PME; EC 3.1.1.11) from a commercial
63 entapeptide serves as a docking site for the methylesterase/deamidase and that the truncated receptor
64 ty from the product by treatment with pectin methylesterase, demonstrated that the bulk of the methyl
65 led that interaction of the sequence and the methylesterase enhanced the rate constant of demethylati
66 rified polymer, demethylesterified by pectin methylesterase enzymes and cross-linked by calcium ions
67 esterified by specific methyltransferase and methylesterase enzymes at a completely conserved C-termi
68 in mucilage, potentially by recycling pectin methylesterase enzymes in the endomembrane system of see
69 l terminus by specific methyltransferase and methylesterase enzymes which have been purified, but not
70 ences of a proteinaceous inhibitor of pectin methylesterase enzymes.
71         Here, we identified this activity as methylesterase family member 16 (MES16; At4g16690).
72                         We identify a pectin methylesterase gene, PME6, which is highly expressed in
73  genomes for the presence of putative pectin methylesterase genes and conducted a sequence analysis o
74 f PP2A in cell lysates with recombinant PP2A methylesterase greatly decreased the amount of C subunit
75                                       Pectin methylesterase has no significant sequence similarity wi
76       Sequence conservation among the pectin methylesterases has been mapped onto the structure and r
77 potential speciation gene, encoding a pectin methylesterase homolog.
78 genic plants overproducing isoprenylcysteine methylesterase (ICME) exhibit ABA hypersensitivity in st
79 o decreased after ectopic expression of PP2A methylesterase in Neuro-2a (N2a) cells.
80  okadaic acid, a known inhibitor of the PP2A methylesterase, inhibited this reaction.
81 d plants expressing an ovule-specific pectin methylesterase inhibitor (PMEI), exhibit reduced HG accu
82                                     A pectin methylesterase inhibitor (SolyPMEI) from tomato has been
83 pectin methylesterase inhibitor and a pectin methylesterase inhibitor -pectin methylesterase, respect
84 0g02150 and Glyma10g02160, encoding a pectin methylesterase inhibitor and a pectin methylesterase inh
85 he impaired locus was identified as a pectin methylesterase inhibitor gene, PECTIN METHYLESTERASE INH
86 elated to the confirmed presence of a pectin methylesterase inhibitor.
87  pectin or cellulose matrix using the PECTIN METHYLESTERASE INHIBITOR5 overexpression line or korriga
88 pectin methylesterase inhibitor gene, PECTIN METHYLESTERASE INHIBITOR6 (PMEI6), specifically expresse
89 walls and are regulated by endogenous pectin methylesterase inhibitors (PMEIs).
90 parably large number of proteinaceous pectin methylesterase inhibitors (PMEIs; 76 members in Arabidop
91             Two of these genes encode pectin methylesterase inhibitors, which, when ectopically expre
92                                          The methylesterase is a two-domain response regulator in whi
93                      The structure of pectin methylesterase is an example of a new family of esterase
94  unable to construct ripples, whereas a frzG methylesterase mutant forms numerous, tightly packed rip
95       However, prenylcysteine alpha-carboxyl methylesterase (PCME) activity has not been described in
96  non-rafts wherein small amounts of the PP2A methylesterase PME-1 are exclusively present.
97                                     The PP2A methylesterase PME-1 limits the activity of PP2A by deme
98 ation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to h
99 ness levels were associated to higher pectin methylesterase (PME) activity and calcium contents.
100  A continuous, fluorometric assay for pectin methylesterase (PME) activity is described.
101        Additionally, the influence of pectin methylesterase (PME) activity on aphid settling and feed
102 ower Opening Time 1 (DFOT1) modulates pectin methylesterase (PME) activity to regulate pectin methyle
103                                       Pectin methylesterase (PME) and polygalacturonase (PG) activiti
104 ivity of the pectin-modifying enzymes pectin-methylesterase (PME) and polygalacturonase (PG) in tomat
105                                       Pectin methylesterase (PME) controls the methylesterification s
106 )QTL2.2 and a region containing three pectin methylesterase (PME) genes underlying Fir(s.p.)QTL2.5 we
107 filing of the nucellus identified two pectin methylesterase (PME) genes, OVULE PECTIN MODIFIER 1 (OPM
108 bsequently deesterified by the enzyme pectin methylesterase (PME) in a process that exposes acidic re
109 es empirical evidence for the role of Pectin Methylesterase (PME) in influencing solid wood character
110  oxidase (PPO), peroxidase (POD), and pectin methylesterase (PME) inactivation, phenolic and volatile
111                                       Pectin methylesterase (PME) is responsible for the demethylatio
112 th sequences common to genes encoding pectin methylesterase (PME) was found to be tightly correlated,
113                                       Pectin methylesterase (PME), a ubiquitous enzyme in plants, de-
114 notation predicts that QRT1 encodes a pectin methylesterase (PME), and enzymatic assays of QRT1 expre
115  pectin to be de-methyl-esterified by pectin methylesterase (PME), and that the PG beta-subunit prote
116 d cell wall-modifying enzymes, namely pectin methylesterase (PME), beta-galactosidase (beta-Gal), end
117 been reported that ZmGa1P, encoding a pectin methylesterase (PME), is a male determinant of the Ga1 l
118      Here, we examined whether or not pectin methylesterase (PME), one of the few cellular proteins k
119 In contrast, poppy gene homologues to pectin methylesterase (PME), pectin acetylesterase (PAE) and pe
120 ovide a mechanism for the activity of pectin methylesterase (PME), the enzyme that catalyses the esse
121 cco leaf cell walls and identified as pectin methylesterase (PME).
122 e basis for a gel diffusion assay for pectin methylesterase (PME, EC 3.1.1.11) activity.
123 hanol in tomato fruit is regulated by pectin methylesterase (PME, EC 3.1.1.11), an enzyme that cataly
124 urther accentuated by overexpression of PP2A methylesterase (PME-1) but cannot be rescued by PME-1 kn
125 y that transgenic overexpression of the PP2A methylesterase, PME-1, or the PP2A methyltransferase, LC
126 cally reducing endogenous levels of the PP2A methylesterase, PME-1, prevents the cognitive and electr
127 pically affects the activity of plant pectin methylesterases (PMEs) and is inactive against a microbi
128                                  Many pectin methylesterases (PMEs) are expressed in plants to modify
129                                       Pectin methylesterases (PMEs) catalyze the demethylesterificati
130                                       Pectin methylesterases (PMEs) catalyze the demethylesterificati
131                                       Pectin methylesterases (PMEs) demethylate homogalacturonan (HG)
132 hypothesis is that high expression of pectin methylesterases (PMEs) increases Ca(2)(+) bound to the c
133 oes not contain cellulose or callose, pectin methylesterases (PMEs) likely play a central role in the
134 lgi and are partially deesterified by pectin methylesterases (PMEs) upon export to the cell wall.
135 onans, mediated through the action of pectin methylesterases (PMEs), influences the biophysical prope
136 ion of pectin is controlled mainly by pectin methylesterases (PMEs), whose activity is posttranscript
137 ion is spatiotemporally controlled by pectin methylesterases (PMEs; 66 members in Arabidopsis [Arabid
138 en is partially demethylesterified by pectin methylesterases (PMEs; EC 3.1.1.11).
139 ities of fruit softening enzymes like pectin methylesterase, polygalacturonase and cellulase.
140 -hybrid screen identified Arabidopsis pectin methylesterase protein 3 (PME3) as strongly and specific
141 ed transgenic mice that overexpress the PP2A methylesterase, protein phosphatase methylesterase-1 (PM
142 hange in the catalytic rate constant for the methylesterase reaction.
143  to activate or inactivate endogenous pectin methylesterase, respectively.
144 nd a pectin methylesterase inhibitor -pectin methylesterase, respectively.
145                                       Pectin methylesterase showed a negligible activity which is rel
146 e, we report the crystal structure of pectin methylesterase that has neither the common alpha/beta hy
147 ously overlooked intermediate, and Dph7 is a methylesterase that hydrolyzes methylated diphthine to p
148 -specific movement factors, including pectin methylesterase, that are involved in regulating plasmode
149 including the SABATH methyltransferases, the methylesterases, the GH3 acyl acid-amido synthetases, an
150 PME-1 represents the first mammalian protein methylesterase to be cloned.
151 ough modulating auxin to downregulate pectin methylesterase VANGUARD1, resulting in decreased cell wa
152 nofuranosidase, polygalacturonase and pectin methylesterase, were measured.
153 h as RNA binding and interaction with pectin methylesterases, were not affected.
154 of PPE1, the yeast gene homologous to bovine methylesterase, yields phenotypes similar to those obser

 
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