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1 nto the binding of substrates to hNit2/omega-amidase.
2 mor suppressor, recently identified as omega-amidase.
3 FtsN-dependent localization with its cognate amidase.
4 a zinc-dependent N-acetylmuramoyl-l-alanine amidase.
5 efective in GPI anchoring through mutant GPI-amidase.
6 tein that we show here to be the Ntaq1 Nt(Q)-amidase.
7 tionally attributed to autolysis by the LytA amidase.
8 ole for AmiC as an N-acetylmuramyl-l-alanine amidase.
9 of the amiB gene, which encodes a cell wall amidase.
10 ation does not convert PGRP-S into an active amidase.
11 residue by a cwlD-encoded muramoyl-L-Alanine amidase.
12 the actions of lytic transglycosylases or an amidase.
13 sequence is dissimilar to sequences of other amidases.
14 and cells, or are peptidoglycan (PGN)-lytic amidases.
15 nstream control of periplasmic peptidoglycan amidases.
16 thin a sequence signature motif of Ser-based amidases.
17 active sites found in several peptidases and amidases.
18 product resembles N-acetylmuramoyl-L-alanine amidases.
19 numerous proteases, lipases, esterases, and amidases.
20 , which depends heavily upon the activity of amidases.
21 en daughter cells that cannot be resolved by amidases.
22 tidases, soluble lytic transglycosylases and amidases.
23 e several functionally redundant periplasmic amidases.
24 easure the activity of mycothiol-S-conjugate amidase, a metal-dependent amidase that is a potential d
25 domain-containing N-acetylmuramyl-L-alanine amidase, a peptidoglycan remodelling enzyme implicated i
26 dy contribute to acid resistance (urease and amidase), acetone metabolism (acetone carboxylase), resi
31 asmic interaction with EnvC are required for amidase activation, but the process itself is poorly und
33 NlpD, is a carboxypeptidase, rather than an amidase activator, which is the case for E. coli NlpD.
34 ver, in Vibrio cholerae, we demonstrate that amidase activity alone is insufficient for daughter cell
35 ebrafish PGRPs have both peptidoglycan-lytic amidase activity and broad-spectrum bactericidal activit
37 e anandamide transporter (FLAT), that lacked amidase activity but bound anandamide with low micromola
38 cherichia coli results in muramoyl L-Alanine amidase activity but no muramic delta-lactam formation.
39 he Ntan1(-/-) mouse strains lacked the Nt(N)-amidase activity but retained glutamine-specific Nt(Q)-a
46 ine mutant PGRP-SC1a, we find that PGRP-SC1a amidase activity is not necessary for Toll signaling, bu
48 Overall, our results suggest that cellular amidase activity is regulated spatially and temporally b
49 217A, S218A, S241A, and R243A, decreased the amidase activity of FAAH greater than 100-fold without d
51 amidases, is required and sufficient for the amidase activity of PGRP-L, although its activity (in th
52 onserved in T7 amidase) are required for the amidase activity of PGRP-L, whereas three other amino ac
55 provides a potential mechanism for coupling amidase activity with the contraction of the FtsZ cytosk
56 and non-cross-linked peptides indicative of amidase activity, and we provided the first evidence tha
57 lthough required, are not sufficient for the amidase activity, because changing them to the "active"
58 mised esterase activity but severely reduced amidase activity, indicating that the amidase and estera
60 nvelope in part by controlling peptidoglycan amidase activity, which confers bacterial resistance to
68 es in FAAH has been shown to severely reduce amidase activity; however, how these residues contribute
70 ology and putative N-acetylmuramoyl-L-alanyl amidase AmiA were both involved in the coccoid transitio
71 s performed by the N-acetylmuramyl-l-alanine amidase AmiA, which cleaves the bond between the carbohy
73 e control of cell division hydrolases called amidases (AmiA, AmiB and AmiC) required for Escherichia
74 t substrates, the N-acetylmuramoyl-l-alanine amidases, AmiA and AmiC, and the cell division protein,
75 ion of the genes encoding the two additional amidases, amiA and amiC, does not compensate for the out
82 y the pneumococcal N-acetylmuramyl-L-alanine amidase (amidase), the glycan strands of the peptidoglyc
90 each of the highly regulated activity of the amidase and clear PG debris that may block the completio
92 ow confirmed that AmiD is an anhMurNAc-l-Ala amidase and demonstrated that AmpD and AmiD are the only
93 e that one of the proteins (SpoIIP) has both amidase and endopeptidase activities, such that it remov
94 educed amidase activity, indicating that the amidase and esterase efficiencies of FAAH can be functio
95 nd phenylalanine amide in the presence of an amidase and phosphatase, four distinct self-assembling m
96 uman PGRP-L is an N-acetylmuramoyl-l-alanine amidase and this function is conserved in prokaryotes, i
97 elong to the N-terminal nucleophile group of amidases and function through a novel proteolytic mechan
98 w amino acid sequence identity with reported amidases and is encoded by an IncP1-beta plasmid (pBAM1,
99 Because FtsN has a known role in recruiting amidases and is predicted to stimulate the activity of F
101 in vivo by substrate availability, and that amidases and RlpA work in tandem to degrade peptidoglyca
102 gest that the order in which cell separation amidases and their activators localize to the septal rin
103 to their susceptibility to nonspecific serum amidases and, thus, would be predicted to have a short d
104 ding amino acids (conserved in PGRP-L and T7 amidase) and Cys-419 (not conserved in T7 amidase) are r
105 for potent inhibitors and enhancers of omega-amidase, and will assist in identifying biological inter
107 biological phenotype [C1Inh, C4, spontaneous amidase, angiotensin-I-converting enzyme (ACE), aminopep
108 uccinamate) were employed in purifying omega-amidase approximately 3600-fold from rat liver cytosol.
110 Three periplasmic N-acetylmuramoyl-l-alanine amidases are critical for hydrolysis of septal peptidogl
113 T7 amidase) and Cys-419 (not conserved in T7 amidase) are required for the amidase activity of PGRP-L
114 r amino acids, needed for the activity of T7 amidase, are not required for the activity of PGRP-L.
115 n the yeast Saccharomyces cerevisiae, the Nt-amidase, arginyltransferase, and the double-E3 ubiquitin
116 identify two lytic transglycosylases and an amidase as new divisome components that are recruited to
117 on is stimulated by the reversible relief of amidase autoinhibition governed by conserved subcomplexe
119 athway, which is currently restricted to the amidase BbdA converting BAM into 2,6-dichlorobenzoic aci
122 e of anandamide in those cells containing an amidase called fatty-acid amide hydrolase (FAAH) is hydr
123 wth and division defects due to loss of this amidase can be mitigated by attenuating the polymerase a
124 ed the first evidence that a cell separation amidase can utilize a small synthetic PG fragment as sub
125 ll plate assay procedure that measures omega-amidase-catalyzed hydroxaminolysis of commercially avail
128 Our findings lead to a model wherein the amidase complex regulates the density of peptidoglycan a
129 present; it is also the first peptidoglycan amidase complex structure of an important human pathogen
131 CwlM, a protein homologous to peptidoglycan amidases, coordinates peptidoglycan synthesis with nutri
132 ons that indicate changes in the activity of amidases, deacetylases, and lytic transglycosylases.
135 amily of genes with sequence homology to the amidase domain of the high-MW SLP was identified in the
136 LytA revealed a potential substrate for the amidase domain within the cell wall where the formation
139 a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase (EC 3.5.1.28), an enzyme that hydrolyzes the ami
140 eptide-N(4)-(N-acetyl-beta-glucosaminyl) Asn amidase (EC 3.5.1.52)-released complex, and beta-elimina
141 casions, and that the resulting domesticated amidase effector (dae) genes have been preserved for hun
143 y acquired from bacteria-called domesticated amidase effector 2 (dae2)-has evolved to kill mammalian
145 nd found that two N-acetylmuramoyl-l-alanine amidases, encoded by amiA and amiC, elevated bacterial r
147 mous mutations for hydrolysis activity of an amidase expressed in E. coli with three different substr
149 This prodrug strategy targets a specific amidase, fatty acid amide hydrolase (FAAH), an enzyme wi
151 lglycerol lipase, N-acetylmuramoyl-L-alanine amidase, flagellin, outer membrane protein A, stringent
152 Asn, would be captured by a complex-bound Nt-amidase, followed by sequential Nt modifications of the
153 with three largely redundant cell separation amidases found in Escherichia coli (AmiA, AmiB, and AmiC
154 weak homology to N-acetyl muramoyl-L-alanine amidase from Bacillus subtilis, and both the native SLP
155 the Glu, Lys, Cys "catalytic triad." In the amidase from Geobacillus pallidus, mutating this glutama
157 heterologously expressed repeats of the AtlE amidase from Staphylococcus epidermidis suggest that the
158 ng residues, structurally conserved in other amidases from Gram-positive Firmicutes, are pivotal for
159 eased virulence in vivo, indicating that the amidase function is not absolutely required for viabilit
160 (transforming benzonitrile to benzamide) or amidase (further conversion of benzamide to benzoic acid
161 tein, with homology to the amiS genes of the amidase gene cluster and to UreI of Helicobacter hepatic
164 The physiological function of cell wall amidases has been investigated in several proteobacteria
167 Cleavage of septal PG is mediated by PG amidases, hydrolytic enzymes that release peptide side c
168 nase, glucose-6-phosphate dehydrogenase, and amidase in both species but not urocanase, although the
170 encoding the asparagine-specific N-terminal amidase in mice results in impaired spatial memory [26].
172 here is not only the first of any bacterial amidase in which both the PGN component and the water mo
173 tivity but retained glutamine-specific Nt(Q)-amidase, indicating that the two enzymes are encoded by
174 e encodes a single N-acetylmuramyl-l-alanine amidase involved in cell separation (AmiC), as compared
175 idation of N-terminal Gln by the Ntaq1 Nt(Q)-amidase is a part of the Arg/N-end rule pathway, a ubiqu
176 with 100 microM MSmB, demonstrating that the amidase is highly specific for S-conjugates of mycothiol
177 indicated that an N-acetylmuramyl-l-alanine amidase is responsible for cell wall breakdown during au
178 L, homologous to bacteriophage and bacterial amidases, is required and sufficient for the amidase act
181 idoglycan hydrolases, consisting of multiple amidases, lytic transglycosylases, and endopeptidases.
183 detoxification enzyme mycothiol-S-conjugate amidase (MCA) and the mycothiol biosynthetic enzyme D-Gl
185 detoxification enzyme mycothiol- S-conjugate amidase (MCA) from Mycobacterium tuberculosis are report
186 ependent detoxification pathway utilizes the amidase (Mca) to cleave mycothiol S-conjugates to produc
189 eletion of penicillin-binding protein 5 from amidase mutants exacerbated the formation of twisted cha
191 is preferentially hydrolyzed by the cysteine amidase N-acylethanolamine-hydrolyzing acid amidase (NAA
194 l)amides, a class of N-acylethanolamine acid amidase (NAAA) inhibitors endowed with anti-inflammatory
197 ve inhibitors of the N-acylethanolamine acid amidase (NAAA) potentially useful for the treatment of p
200 AAH) and N-acylethanolamine-hydrolyzing acid amidase (NAAA), which have been shown to break down the
201 amidase N-acylethanolamine-hydrolyzing acid amidase (NAAA), which is highly expressed in macrophages
205 onoglyceride lipase, N-acylethanolamine acid amidase, NAPE-selective phospholipase D, and protein tyr
206 l help to characterize the function of omega-amidase/Nit2 in tumor suppression, will provide the basi
207 s lacking the asparagine-specific N-terminal amidase (Nt(N)-amidase), encoded by the Ntan1 gene.
208 discovered that the human Nt-Asn-specific Nt-amidase NTAN1, Nt-Gln-specific Nt-amidase NTAQ1, arginyl
209 pecific Nt-amidase NTAN1, Nt-Gln-specific Nt-amidase NTAQ1, arginyltransferase ATE1, and the ubiquiti
210 is thaliana Gln-specific amino-terminal (Nt)-amidase (NTAQ1) controls the expression of specific defe
211 1ab-R2ab) of the N-acetyl-muramoyl-L-alanine amidase of Atl are essential for binding of hTSP-1.
216 Glu-tRNA by amidotransferases that couple an amidase or an asparaginase to liberate ammonia with a tR
217 idoglycan synthases, the major peptidoglycan amidases, or any of the low-molecular-weight penicillin
220 irst found for an N-acetylmuramoyl-l-alanine amidase PGRP that cleaves peptidoglycan at the lactylami
221 ate that mycothiol and mycothiol S-conjugate amidase play an important role in the detoxification of
223 c cofactor typically used by cell separation amidases, potentially protecting its ability to function
229 n silico prediction combined with an in vivo amidase reporter assay indicates that at least 23 protei
232 rect regulators of the cell wall hydrolases (amidases) responsible for cell separation (AmiA, AmiB an
234 ession of AmiA, AmiC, or AmiB, a periplasmic amidase secreted via the general secretory pathway, rest
235 large group of hydrolytic enzymes termed the amidase signature (AS) family that is defined by a conse
236 am), a hydrolytic enzyme that belongs to the amidase signature (AS) family, selectively catalyzes the
240 ids with 37% identity to rat FAAH within the amidase signature domain (18% over the entire length).
241 y acid amide hydrolase (FAAH) is a mammalian amidase signature enzyme that inactivates neuromodulator
243 of FAAH and two distantly related bacterial amidase signature enzymes indicates that these enzymes e
244 ctively, these studies provide evidence that amidase signature enzymes represent a large class of ser
245 a regulatory protein (mdlX), a member of the amidase signature family (mdlY), and an NAD(P)(+)-depend
246 lase, is a recently discovered member of the amidase signature family that catalyzes the terminal rea
247 FAAH that are conserved among members of the amidase signature family, and have assessed their indivi
249 nalysis suggests that MAH is a member of the amidase signature family, which is widespread in nature
250 arge class of hydrolytic enzymes termed the "amidase signature family," whose members are defined by
255 is DNA sequences containing a characteristic amidase signature sequence (PS00571) were identified in
256 limited number of conserved residues in the amidase signature sequence of the enzyme, identifying Se
258 of approximately 130 amino acids termed the "amidase signature sequence." Recently, site-directed mut
260 d in vitro (with human serum and recombinant amidase) study was performed in order to generate inform
261 nal fold is related to that of the cell wall amidase, T7 lysozyme, and contains a conserved zinc coor
263 o the ring was mediated by an N-terminal non-amidase targeting domain and required the septal ring co
266 ceramidase (AC) is an intracellular cysteine amidase that catalyzes the hydrolysis of the lipid messe
267 ristoyl]-GlcNAc deacetylase (LpxC) is a zinc amidase that catalyzes the second step of lipid A biosyn
268 e that PlyL is an N-acetylmuramoyl-L-alanine amidase that cleaves the cell wall of several Bacillus s
269 Acid ceramidase (AC) is a lysosomal cysteine amidase that controls sphingolipid signaling by lowering
271 ression of acid ceramidase (AC) - a cysteine amidase that hydrolyses the proapoptotic lipid ceramide
272 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and is c
273 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and is d
274 thiol-S-conjugate amidase, a metal-dependent amidase that is a potential drug target involved in the
277 s during elongation and that the periplasmic amidases that aid in cell separation are minor players,
278 ring as a product of catalysis by cell-wall amidases that participate in the separation of daughter
279 umococcal N-acetylmuramyl-L-alanine amidase (amidase), the glycan strands of the peptidoglycan of Sta
281 with previously characterized peptidoglycan amidases, the enzyme contains an extra disulfide-bonded
282 ervations that in the absence of two or more amidases, thickened and dark bands, which we term septal
287 tile enzyme that catalyzes a large number of amidase, transamidase, and ester hydrolysis reactions.
288 The bifunctional trypanothione synthetase-amidase (TRYS) comprises two structurally distinct catal
291 es the activity of periplasmic peptidoglycan amidases via its interaction with the murein hydrolase a
294 t detoxification enzyme, mycothiol conjugate amidase, was recently identified in Mycobacterium smegma
295 ate the catalytic specificity of hNit2/omega-amidase, we performed molecular dynamics simulations on
296 that Lc-Lys is an N-acetylmuramoyl-L-alanine amidase, whereas Lc-Lys-2 is a gamma-D-glutamyl-L-lysyl
297 acid ceramidase (AC) is a lysosomal cysteine amidase, which has received a great deal of interest in