戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
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
27                                 The cysteine amidase, acid ceramidase (AC), hydrolyzes these substanc
28 this degenerate active site are critical for amidase activation in vivo and in vitro.
29                         Residues involved in amidase activation map to a previously identified groove
30                Our results thus suggest that amidase activation via EnvC in the periplasm is regulate
31 asmic interaction with EnvC are required for amidase activation, but the process itself is poorly und
32 experimentally test a proposed mechanism for amidase activation.
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
36                                          The amidase activity associated with PGRP-LB may scavenge th
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
40 nces, tertiary structures, and activation of amidase activity by intramolecular autoproteolysis.
41 ed in Escherichia coli were found to display amidase activity by zymography.
42      Furthermore, we find that the PGRP-SC1a amidase activity can be substituted by exogenous additio
43                                  The optimal amidase activity for PpFAAH1 was at 37 degrees C and pH
44 s of accessory proteins proposed to regulate amidase activity in cells.
45       Our results thus reveal a key role for amidase activity in cytokinetic ring contraction.
46 ine mutant PGRP-SC1a, we find that PGRP-SC1a amidase activity is not necessary for Toll signaling, bu
47 olysis has a Km value of 5.6 mm, the in vivo amidase activity is probably negligible.
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
50                                          The amidase activity of lysozyme is needed for abrupt lysis
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
53                                        omega-Amidase activity toward alpha-ketoglutaramate and alpha-
54                          The kinetics of the amidase activity were monitored using Pro-Phe-Arg-pNA, i
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
59          In contrast to PGRPs with PGN-lytic amidase activity, no zinc ion is present in the PGN-bind
60 nvelope in part by controlling peptidoglycan amidase activity, which confers bacterial resistance to
61 and pPGRP-L2 have N-acetylmuramoyl-L-alanine amidase activity.
62 of the purified zymogen and generation of an amidase activity.
63 pha, PGRP-Ibeta, and PGRP-S, do not have the amidase activity.
64 tial role in autoproteolysis to activate the amidase activity.
65 tral role in both autoproteolysis and in its amidase activity.
66 s, we did not detect any YbAnbu peptidase or amidase activity.
67 articipate in cell separation by stimulating amidase activity.
68 es in FAAH has been shown to severely reduce amidase activity; however, how these residues contribute
69  BLAST search shows that the closest-related amidases almost exclusively target Clostridia.
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
72 the important Escherichia coli cell division amidase AmiA.
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
76       Septal PG splitting is mediated by the amidases: AmiA, AmiB, and AmiC.
77  defective for the N-acetylmuramyl-l-alanine amidases: AmiA, AmiB, and AmiC.
78 to the division site well before its cognate amidase AmiB.
79 gen Vibrio cholerae, encode only a single PG amidase, AmiB.
80                                  Periplasmic amidases AmiC and AmiA, secreted by the twin arginine tr
81                Unlike the periplasmic murein amidases, AmiD did not participate in cell separation.
82 y the pneumococcal N-acetylmuramyl-L-alanine amidase (amidase), the glycan strands of the peptidoglyc
83                                          The amidase AmpD degrades peptidoglycan monomers by removing
84       Deamidation of N-terminal Gln by Nt(Q)-amidase, an N-terminal amidohydrolase, is a part of the
85 ubstrate and has dual activity, acting as an amidase and a carboxypeptidase.
86        In Arabidopsis, colocalization of NPA amidase and aminopeptidase (AP) activities, inhibition o
87                        In addition, NTAQ1 Nt-amidase and ATE1 arginyltransferase also bind to UBR1/UB
88              Glycosylasparaginase (GA) is an amidase and belongs to a novel family of N-terminal nucl
89              All known nitrilase superfamily amidase and carbamoylase structures have an additional g
90 each of the highly regulated activity of the amidase and clear PG debris that may block the completio
91 ctions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase.
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
100        Here, we investigated the function of amidases and LytM proteins in the opportunistic pathogen
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
106 oiling conditions and were synthesized in an amidase- and sltY-independent manner.
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.
109 active site and catalytic mechanism of Nt(Q)-amidase are similar to those of transglutaminases.
110 Three periplasmic N-acetylmuramoyl-l-alanine amidases are critical for hydrolysis of septal peptidogl
111                 The results suggest that the amidases are necessary for continued peptidoglycan synth
112                                   Penicillin amidases are thought to function as scavengers for pheny
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
118 nutes in a process dependent on the suicidal amidase autolysin LytA.
119 athway, which is currently restricted to the amidase BbdA converting BAM into 2,6-dichlorobenzoic aci
120                                           An amidase-BbdA-converting BAM to 2,6-dichlorobenzoic acid
121 R2-UBE2A/B) form a complex in which NTAN1 Nt-amidase binds to NTAQ1, ATE1, and UBR1/UBR2.
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
126 of both the polyketide synthase ClbO and the amidase ClbL.
127                                          The amidases cleave the amide bond between the lactyl group
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
130                                However, this amidase controls cell growth.
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.
133  both enzymatic functions were essential, an amidase-dead mutant cDKO line was generated.
134                Importantly, the phenotype of amidase-defective P. aeruginosa cells also differed in i
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
137           Based on the presence of conserved amidase domains, tsetse PGRP-LB may scavenge the peptido
138  4 collaborates with the major peptidoglycan amidases during cell separation.
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
142                        The type VI secretion amidase effector (Tae) proteins are potent bacteriocidal
143 y acquired from bacteria-called domesticated amidase effector 2 (dae2)-has evolved to kill mammalian
144 sparagine-specific N-terminal amidase (Nt(N)-amidase), encoded by the Ntan1 gene.
145 nd found that two N-acetylmuramoyl-l-alanine amidases, encoded by amiA and amiC, elevated bacterial r
146 into four families composed of peptidoglycan amidase enzymes of differing specificities.
147 mous mutations for hydrolysis activity of an amidase expressed in E. coli with three different substr
148 D are recruited to septal rings, whereas the amidases fail to localize.
149     This prodrug strategy targets a specific amidase, fatty acid amide hydrolase (FAAH), an enzyme wi
150                     The intracellular serine amidase, fatty acid amide hydrolase (FAAH), degrades a h
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
156 to have substrate specificity similar to the amidase from M. smegmatis.
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
162 g8253 gene that we show here to encode Nt(Q)-amidase has defective long-term memory.
163                                        omega-Amidase has recently been shown to be identical to Nit2,
164      The physiological function of cell wall amidases has been investigated in several proteobacteria
165 well understood, with only regulators for PG amidases having been described.
166  Ami- cells form chains, indicating that the amidases help to split the septal murein.
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
169 o-N-acetylmuramic acid (anhMurNAc)-l-alanine amidase in Escherichia coli.
170  encoding the asparagine-specific N-terminal amidase in mice results in impaired spatial memory [26].
171  gene for a putative peptidoglycan-degrading amidase in N. gonorrhoeae.
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
179                            Thus, hNit2/omega-amidase links sulfur metabolism to the tricarboxylic aci
180       In this study, we demonstrate that the amidase LytA, the main pneumococcal autolysin, inhibits
181 idoglycan hydrolases, consisting of multiple amidases, lytic transglycosylases, and endopeptidases.
182 tion, we find that the E. coli peptidoglycan amidases may have different substrate preferences.
183  detoxification enzyme mycothiol-S-conjugate amidase (MCA) and the mycothiol biosynthetic enzyme D-Gl
184                        Mycothiol S-conjugate amidase (Mca) cleaves the amide bond of mycothiol S-conj
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
187             To efficiently hydrolyze PG, the amidases must be activated by LytM domain factors.
188 arates daughter cells in an Escherichia coli amidase mutant.
189 eletion of penicillin-binding protein 5 from amidase mutants exacerbated the formation of twisted cha
190                                Unexpectedly, amidase mutants lacking PBP 5 grew in long twisted chain
191 is preferentially hydrolyzed by the cysteine amidase N-acylethanolamine-hydrolyzing acid amidase (NAA
192 are terminated by the intracellular cysteine amidase, N-acylethanolamine acid amidase (NAAA).
193                          The PEA-hydrolyzing amidase NAAA may provide a previously undescribed target
194 l)amides, a class of N-acylethanolamine acid amidase (NAAA) inhibitors endowed with anti-inflammatory
195                      N-Acylethanolamine acid amidase (NAAA) is a lysosomal cysteine hydrolase involve
196                      N-Acylethanolamine acid amidase (NAAA) is an N-terminal cysteine hydrolase prima
197 ve inhibitors of the N-acylethanolamine acid amidase (NAAA) potentially useful for the treatment of p
198                      N-acylethanolamine acid amidase (NAAA), a cysteine hydrolase highly expressed in
199 cerol lipase (MAGL), N-acylethanolamine acid amidase (NAAA), or cyclooxygenase 2 (COX-2).
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
202 olase or N-acylethanolamine-hydrolyzing acid amidase (NAAA).
203 ar cysteine amidase, N-acylethanolamine acid amidase (NAAA).
204 -studied N-acylethanolamine-hydrolyzing acid amidase (NAAA).
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.
212               The N-acetylmuramoyl-l-alanine amidases of Escherichia coli (AmiA, B and C) are peripla
213                                        omega-Amidase (omega-amidodicarboxylate amidohydrolase, EC 3.5
214                        The results show that amidase operon expression is controlled by a novel type
215                            Expression of the amidase operon of Pseudomonas aeruginosa is controlled b
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
218 d due to exopeptidase- (amino- or carboxy-), amidase-, or endopeptidase activity.
219                                      Peptide amidase (Pam), a hydrolytic enzyme that belongs to the a
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
222                                  hNit2/omega-amidase plays a crucial metabolic role by catalyzing the
223 c cofactor typically used by cell separation amidases, potentially protecting its ability to function
224        AtzE and AtzF are members of a common amidase protein family.
225 n of a second one upstream of a penicillin V amidase (PVA) gene on the small chromosome.
226 ein, the putative N-acetylmuramoyl-l-alanine amidase RC0497.
227 rolysis at the division site, accompanied by amidase recruitment.
228                                Cell division amidases remain largely uncharacterized because substrat
229 n silico prediction combined with an in vivo amidase reporter assay indicates that at least 23 protei
230                  We recently showed that the amidases require activation at the cytokinetic ring by p
231 hesis and degradation activities of FtsI and amidases respectively.
232 rect regulators of the cell wall hydrolases (amidases) responsible for cell separation (AmiA, AmiB an
233  the mycobacterial N-acetylmuramyl-L-alanine amidase, Rv3717.
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
237  to a single integral membrane enzyme of the amidase signature (AS) family.
238  diverse class of enzymes referred to as the amidase signature (AS) family.
239 scomitrella patens (PpFAAH1 to PpFAAH9) with amidase signature and catalytic triad.
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
242 uggests a functional convergence between the amidase signature enzymes and serine proteases.
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
248                            AH belongs to the amidase signature family, which is characterized by a co
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
251 ation interface that is not conserved in the amidase signature family.
252 reviously identified in other members of the amidase signature family.
253  there are two distinct subgroups within the amidase signature family.
254 d specificity among divergent members of the amidase signature family.
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
257 A-subunit, which displays the characteristic amidase signature sequence.
258 of approximately 130 amino acids termed the "amidase signature sequence." Recently, site-directed mut
259        Fatty acid amide hydrolase (FAAH), an amidase-signature family member, is an integral membrane
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
262 c interaction of Hcp1 with the antibacterial amidase Tae4.
263 o the ring was mediated by an N-terminal non-amidase targeting domain and required the septal ring co
264            We detected the activity of Nt(Q)-amidase, termed Ntaq1, in mouse tissues, purified Ntaq1
265                               LpxC is a zinc amidase that catalyses the second step of lipid A biosyn
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
270                            T7 lysozyme is an amidase that cuts a bond in the peptidoglycan layer of t
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
275                 Treatment of sacculi with an amidase that removes stem peptides enhanced SPOR domain
276                  This complex consists of an amidase that removes stem peptides from uncrosslinked pe
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
280 ysis by activating N-acetylmuramyl-L-alanine amidase, the pneumococcal autolysin.
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
283 ere subjected to a limited digestion with an amidase to remove some of the stem peptides.
284 imulate PG cleavage by target enzymes called amidases to promote cell separation.
285  must be split by hydrolytic enzymes called "amidases" to drive daughter-cell separation.
286 ds in the binding specificity of hNit2/omega-amidase toward various substrates.
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
289                                              Amidases typically hydrolyse crosslinked peptidoglycan b
290 izing enzymes: nitrile hydratase (NHase) and amidase versus nitrilase activity.
291 es the activity of periplasmic peptidoglycan amidases via its interaction with the murein hydrolase a
292                  The activity of hNit2/omega-amidase was determined with alpha-ketoglutaramate and su
293                                         MpaA amidase was identified in Escherichia coli by its amino
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
298 of k(cat) = 8 s(-)(1) was determined for the amidase with MSmB as substrate.
299 nzymes, as a template for the engineering of amidases with novel and/or tailored specificities.
300               The presence of genes encoding amidases with twin-arginine signal sequences in the geno

 
Page Top