ライフサイエンスコーパス: amidase

1 al autolysin (N-acetylmuramic acid-L-alanine amidase).

2 efective in GPI anchoring through mutant GPI-amidase.

3 tein that we show here to be the Ntaq1 Nt(Q)-amidase.

4 tionally attributed to autolysis by the LytA amidase.

5 ole for AmiC as an N-acetylmuramyl-l-alanine amidase.

6 of the amiB gene, which encodes a cell wall amidase.

7 ation does not convert PGRP-S into an active amidase.

8 residue by a cwlD-encoded muramoyl-L-Alanine amidase.

9 protease blocker and inhibitor of anandamide amidase.

10 their hydrolytic stability toward anandamide amidase.

11 ver rate for each analog with respect to AEA amidase.

12 etylmuramidase and N-acetylmuramyl-L-alanine amidase.

13 nto the binding of substrates to hNit2/omega-amidase.

14 mor suppressor, recently identified as omega-amidase.

15 FtsN-dependent localization with its cognate amidase.

16 a zinc-dependent N-acetylmuramoyl-l-alanine amidase.

17 sequence is dissimilar to sequences of other amidases.

18 and cells, or are peptidoglycan (PGN)-lytic amidases.

19 thin a sequence signature motif of Ser-based amidases.

20 active sites found in several peptidases and amidases.

21 product resembles N-acetylmuramoyl-L-alanine amidases.

22 numerous proteases, lipases, esterases, and amidases.

23 e several functionally redundant periplasmic amidases.

24 tidases, soluble lytic transglycosylases and amidases.

25 easure the activity of mycothiol-S-conjugate amidase, a metal-dependent amidase that is a potential d

26 domain-containing N-acetylmuramyl-L-alanine amidase, a peptidoglycan remodelling enzyme implicated i

27 dy contribute to acid resistance (urease and amidase), acetone metabolism (acetone carboxylase), resi

28 The cysteine amidase, acid ceramidase (AC), hydrolyzes these substanc

29 this degenerate active site are critical for amidase activation in vivo and in vitro.

30 Our results thus suggest that amidase activation via EnvC in the periplasm is regulate

31 NlpD, is a carboxypeptidase, rather than an amidase activator, which is the case for E. coli NlpD.

32 ebrafish PGRPs have both peptidoglycan-lytic amidase activity and broad-spectrum bactericidal activit

33 The amidase activity associated with PGRP-LB may scavenge th

34 e anandamide transporter (FLAT), that lacked amidase activity but bound anandamide with low micromola

35 cherichia coli results in muramoyl L-Alanine amidase activity but no muramic delta-lactam formation.

36 he Ntan1(-/-) mouse strains lacked the Nt(N)-amidase activity but retained glutamine-specific Nt(Q)-a

37 f Rv1082, possesses weak mycothiol conjugate amidase activity but shows substantial deacetylation act

38 nces, tertiary structures, and activation of amidase activity by intramolecular autoproteolysis.

39 t a novel, more general method for measuring amidase activity by o-phthaldialdehyde (OPA) precolumn d

40 ed in Escherichia coli were found to display amidase activity by zymography.

41 Furthermore, we find that the PGRP-SC1a amidase activity can be substituted by exogenous additio

42 s of accessory proteins proposed to regulate amidase activity in cells.

43 Our results thus reveal a key role for amidase activity in cytokinetic ring contraction.

44 ine mutant PGRP-SC1a, we find that PGRP-SC1a amidase activity is not necessary for Toll signaling, bu

45 olysis has a Km value of 5.6 mm, the in vivo amidase activity is probably negligible.

46 Overall, our results suggest that cellular amidase activity is regulated spatially and temporally b

47 217A, S218A, S241A, and R243A, decreased the amidase activity of FAAH greater than 100-fold without d

48 The amidase activity of lysozyme is needed for abrupt lysis

49 amidases, is required and sufficient for the amidase activity of PGRP-L, although its activity (in th

50 onserved in T7 amidase) are required for the amidase activity of PGRP-L, whereas three other amino ac

51 omega-Amidase activity toward alpha-ketoglutaramate and alpha-

52 The kinetics of the amidase activity were monitored using Pro-Phe-Arg-pNA, i

53 provides a potential mechanism for coupling amidase activity with the contraction of the FtsZ cytosk

54 and non-cross-linked peptides indicative of amidase activity, and we provided the first evidence tha

55 lthough required, are not sufficient for the amidase activity, because changing them to the "active"

56 mised esterase activity but severely reduced amidase activity, indicating that the amidase and estera

57 In contrast to PGRPs with PGN-lytic amidase activity, no zinc ion is present in the PGN-bind

58 nvelope in part by controlling peptidoglycan amidase activity, which confers bacterial resistance to

59 and pPGRP-L2 have N-acetylmuramoyl-L-alanine amidase activity.

60 of the purified zymogen and generation of an amidase activity.

61 pha, PGRP-Ibeta, and PGRP-S, do not have the amidase activity.

62 tial role in autoproteolysis to activate the amidase activity.

63 tral role in both autoproteolysis and in its amidase activity.

64 eptidase as well as N-acetylmuramyl-L-alanyl amidase activity.

65 articipate in cell separation by stimulating amidase activity.

66 s, we did not detect any YbAnbu peptidase or amidase activity.

67 es in FAAH has been shown to severely reduce amidase activity; however, how these residues contribute

68 BLAST search shows that the closest-related amidases almost exclusively target Clostridia.

69 s performed by the N-acetylmuramyl-l-alanine amidase AmiA, which cleaves the bond between the carbohy

70 the important Escherichia coli cell division amidase AmiA.

71 e control of cell division hydrolases called amidases (AmiA, AmiB and AmiC) required for Escherichia

72 t substrates, the N-acetylmuramoyl-l-alanine amidases, AmiA and AmiC, and the cell division protein,

73 ion of the genes encoding the two additional amidases, amiA and amiC, does not compensate for the out

74 defective for the N-acetylmuramyl-l-alanine amidases: AmiA, AmiB, and AmiC.

75 Septal PG splitting is mediated by the amidases: AmiA, AmiB, and AmiC.

76 to the division site well before its cognate amidase AmiB.

77 gen Vibrio cholerae, encode only a single PG amidase, AmiB.

78 Periplasmic amidases AmiC and AmiA, secreted by the twin arginine tr

79 Unlike the periplasmic murein amidases, AmiD did not participate in cell separation.

80 The mycothiol S-conjugate amidase (amidase) responsible for cleaving MSmB was puri

81 y the pneumococcal N-acetylmuramyl-L-alanine amidase (amidase), the glycan strands of the peptidoglyc

82 The amidase AmpD degrades peptidoglycan monomers by removing

83 Deamidation of N-terminal Gln by Nt(Q)-amidase, an N-terminal amidohydrolase, is a part of the

84 ubstrate and has dual activity, acting as an amidase and a carboxypeptidase.

85 In Arabidopsis, colocalization of NPA amidase and aminopeptidase (AP) activities, inhibition o

86 Glycosylasparaginase (GA) is an amidase and belongs to a novel family of N-terminal nucl

87 All known nitrilase superfamily amidase and carbamoylase structures have an additional g

88 ulates the expression of the major autolytic amidase and CsbB may function in peptidoglycan synthesis

89 ctions as both an N-acetylmuramoyl-L-alanine amidase and D-alanyl-glycine endopeptidase.

90 ow confirmed that AmiD is an anhMurNAc-l-Ala amidase and demonstrated that AmpD and AmiD are the only

91 e that one of the proteins (SpoIIP) has both amidase and endopeptidase activities, such that it remov

92 educed amidase activity, indicating that the amidase and esterase efficiencies of FAAH can be functio

93 he enzyme to function effectively as both an amidase and esterase in vivo.

94 Here we examined the mechanism that directs amidase and glucosaminidase to the cell division site on

95 idues 198 and 775 to generate a pro-peptide, amidase and glucosaminidase, respectively.

96 nd phenylalanine amide in the presence of an amidase and phosphatase, four distinct self-assembling m

97 uman PGRP-L is an N-acetylmuramoyl-l-alanine amidase and this function is conserved in prokaryotes, i

98 elong to the N-terminal nucleophile group of amidases and function through a novel proteolytic mechan

99 w amino acid sequence identity with reported amidases and is encoded by an IncP1-beta plasmid (pBAM1,

100 Because FtsN has a known role in recruiting amidases and is predicted to stimulate the activity of F

101 Here, we investigated the function of amidases and LytM proteins in the opportunistic pathogen

102 in vivo by substrate availability, and that amidases and RlpA work in tandem to degrade peptidoglyca

103 gest that the order in which cell separation amidases and their activators localize to the septal rin

104 to their susceptibility to nonspecific serum amidases and, thus, would be predicted to have a short d

105 ding amino acids (conserved in PGRP-L and T7 amidase) and Cys-419 (not conserved in T7 amidase) are r

106 e subunits, two cyclases, two oxygenases, an amidase, and remarkably, two acyl carrier proteins.

107 for potent inhibitors and enhancers of omega-amidase, and will assist in identifying biological inter

108 ae) secretes cell-lysing enzymes: esterases, amidases, and glycosylases, many of which degrade soil b

109 oiling conditions and were synthesized in an amidase- and sltY-independent manner.

110 biological phenotype [C1Inh, C4, spontaneous amidase, angiotensin-I-converting enzyme (ACE), aminopep

111 uccinamate) were employed in purifying omega-amidase approximately 3600-fold from rat liver cytosol.

112 active site and catalytic mechanism of Nt(Q)-amidase are similar to those of transglutaminases.

113 Three periplasmic N-acetylmuramoyl-l-alanine amidases are critical for hydrolysis of septal peptidogl

114 The results suggest that the amidases are necessary for continued peptidoglycan synth

115 Penicillin amidases are thought to function as scavengers for pheny

116 T7 amidase) and Cys-419 (not conserved in T7 amidase) are required for the amidase activity of PGRP-L

117 r amino acids, needed for the activity of T7 amidase, are not required for the activity of PGRP-L.

118 identify two lytic transglycosylases and an amidase as new divisome components that are recruited to

119 on is stimulated by the reversible relief of amidase autoinhibition governed by conserved subcomplexe

120 nutes in a process dependent on the suicidal amidase autolysin LytA.

121 An amidase-BbdA-converting BAM to 2,6-dichlorobenzoic acid

122 ococcal autolysin (N-acetylmuramyl-L-alanine amidase) but were cleaved by the muramidases CPL and cel

123 e of anandamide in those cells containing an amidase called fatty-acid amide hydrolase (FAAH) is hydr

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 Anandamide amidase catalyzes the hydrolysis of anandamide (AEA) to

127 The amidases cleave the amide bond between the lactyl group

128 present; it is also the first peptidoglycan amidase complex structure of an important human pathogen

129 CwlM, a protein homologous to peptidoglycan amidases, coordinates peptidoglycan synthesis with nutri

130 both enzymatic functions were essential, an amidase-dead mutant cDKO line was generated.

131 Importantly, the phenotype of amidase-defective P. aeruginosa cells also differed in i

132 amily of genes with sequence homology to the amidase domain of the high-MW SLP was identified in the

133 LytA revealed a potential substrate for the amidase domain within the cell wall where the formation

134 Based on the presence of conserved amidase domains, tsetse PGRP-LB may scavenge the peptido

135 4 collaborates with the major peptidoglycan amidases during cell separation.

136 a Zn2+-dependent N-acetylmuramoyl-l-alanine amidase (EC 3.5.1.28), an enzyme that hydrolyzes the ami

137 eptide-N(4)-(N-acetyl-beta-glucosaminyl) Asn amidase (EC 3.5.1.52)-released complex, and beta-elimina

138 casions, and that the resulting domesticated amidase effector (dae) genes have been preserved for hun

139 The type VI secretion amidase effector (Tae) proteins are potent bacteriocidal

140 sparagine-specific N-terminal amidase (Nt(N)-amidase), encoded by the Ntan1 gene.

141 nd found that two N-acetylmuramoyl-l-alanine amidases, encoded by amiA and amiC, elevated bacterial r

142 into four families composed of peptidoglycan amidase enzymes of differing specificities.

143 e also shown hydrolytic stability toward the amidase enzymes, responsible for the primary degradation

144 mous mutations for hydrolysis activity of an amidase expressed in E. coli with three different substr

145 Two of these enzymes, fatty-acyl amidases FAA I and FAA II, act sequentially on the N-lin

146 D are recruited to septal rings, whereas the amidases fail to localize.

147 The intracellular serine amidase, fatty acid amide hydrolase (FAAH), degrades a h

148 lglycerol lipase, N-acetylmuramoyl-L-alanine amidase, flagellin, outer membrane protein A, stringent

149 with three largely redundant cell separation amidases found in Escherichia coli (AmiA, AmiB, and AmiC

150 weak homology to N-acetyl muramoyl-L-alanine amidase from Bacillus subtilis, and both the native SLP

151 ch as hen egg white lysozyme and to the CwlA amidase from Bacillus subtilis.

152 the Glu, Lys, Cys "catalytic triad." In the amidase from Geobacillus pallidus, mutating this glutama

153 to have substrate specificity similar to the amidase from M. smegmatis.

154 heterologously expressed repeats of the AtlE amidase from Staphylococcus epidermidis suggest that the

155 ng residues, structurally conserved in other amidases from Gram-positive Firmicutes, are pivotal for

156 eased virulence in vivo, indicating that the amidase function is not absolutely required for viabilit

157 (transforming benzonitrile to benzamide) or amidase (further conversion of benzamide to benzoic acid

158 tein, with homology to the amiS genes of the amidase gene cluster and to UreI of Helicobacter hepatic

159 g8253 gene that we show here to encode Nt(Q)-amidase has defective long-term memory.

160 omega-Amidase has recently been shown to be identical to Nit2,

161 The physiological function of cell wall amidases has been investigated in several proteobacteria

162 Ami- cells form chains, indicating that the amidases help to split the septal murein.

163 Analysis of a deletion mutant lacking the amidase-homologous sequence, phi11(Delta181-381), reveal

164 e homology to known N-acetylmuramyl-L-alanyl amidases; however, their precise cleavage sites on the s

165 Cleavage of septal PG is mediated by PG amidases, hydrolytic enzymes that release peptide side c

166 nase, glucose-6-phosphate dehydrogenase, and amidase in both species but not urocanase, although the

167 o-N-acetylmuramic acid (anhMurNAc)-l-alanine amidase in Escherichia coli.

168 encoding the asparagine-specific N-terminal amidase in mice results in impaired spatial memory [26].

169 gene for a putative peptidoglycan-degrading amidase in N. gonorrhoeae.

170 ectly demonstrate the presence of anandamide amidase in these tissues, suggesting that the enzyme may

171 here is not only the first of any bacterial amidase in which both the PGN component and the water mo

172 tivity but retained glutamine-specific Nt(Q)-amidase, indicating that the two enzymes are encoded by

173 orophosphonate (MAFP), a specific anandamide amidase inhibitor, when administered to either ganglia w

174 It also cannot be used to study AEA amidase inhibitors that contain the arachidonic acid tai

175 e encodes a single N-acetylmuramyl-l-alanine amidase involved in cell separation (AmiC), as compared

176 idation of N-terminal Gln by the Ntaq1 Nt(Q)-amidase is a part of the Arg/N-end rule pathway, a ubiqu

177 with 100 microM MSmB, demonstrating that the amidase is highly specific for S-conjugates of mycothiol

178 indicated that an N-acetylmuramyl-l-alanine amidase is responsible for cell wall breakdown during au

179 L, homologous to bacteriophage and bacterial amidases, is required and sufficient for the amidase act

180 zyme as a member of a diverse group of alkyl amidases, known collectively as the "amidase signature f

181 Thus, hNit2/omega-amidase links sulfur metabolism to the tricarboxylic aci

182 In this study, we demonstrate that the amidase LytA, the main pneumococcal autolysin, inhibits

183 idoglycan hydrolases, consisting of multiple amidases, lytic transglycosylases, and endopeptidases.

184 tion, we find that the E. coli peptidoglycan amidases may have different substrate preferences.

185 detoxification enzyme mycothiol-S-conjugate amidase (MCA) and the mycothiol biosynthetic enzyme D-Gl

186 Mycothiol S-conjugate amidase (Mca) cleaves the amide bond of mycothiol S-conj

187 detoxification enzyme mycothiol- S-conjugate amidase (MCA) from Mycobacterium tuberculosis are report

188 ependent detoxification pathway utilizes the amidase (Mca) to cleave mycothiol S-conjugates to produc

189 To efficiently hydrolyze PG, the amidases must be activated by LytM domain factors.

190 arates daughter cells in an Escherichia coli amidase mutant.

191 eletion of penicillin-binding protein 5 from amidase mutants exacerbated the formation of twisted cha

192 Unexpectedly, amidase mutants lacking PBP 5 grew in long twisted chain

193 is preferentially hydrolyzed by the cysteine amidase N-acylethanolamine-hydrolyzing acid amidase (NAA

194 are terminated by the intracellular cysteine amidase, N-acylethanolamine acid amidase (NAAA).

195 The PEA-hydrolyzing amidase NAAA may provide a previously undescribed target

196 l)amides, a class of N-acylethanolamine acid amidase (NAAA) inhibitors endowed with anti-inflammatory

197 N-Acylethanolamine acid amidase (NAAA) is a lysosomal cysteine hydrolase involve

198 ve inhibitors of the N-acylethanolamine acid amidase (NAAA) potentially useful for the treatment of p

199 N-acylethanolamine acid amidase (NAAA), a cysteine hydrolase highly expressed in

200 cerol lipase (MAGL), N-acylethanolamine acid amidase (NAAA), or cyclooxygenase 2 (COX-2).

201 AAH) and N-acylethanolamine-hydrolyzing acid amidase (NAAA), which have been shown to break down the

202 amidase N-acylethanolamine-hydrolyzing acid amidase (NAAA), which is highly expressed in macrophages

203 olase or N-acylethanolamine-hydrolyzing acid amidase (NAAA).

204 ar cysteine amidase, N-acylethanolamine acid amidase (NAAA).

205 -studied N-acylethanolamine-hydrolyzing acid amidase (NAAA).

206 onoglyceride lipase, N-acylethanolamine acid amidase, NAPE-selective phospholipase D, and protein tyr

207 l help to characterize the function of omega-amidase/Nit2 in tumor suppression, will provide the basi

208 s lacking the asparagine-specific N-terminal amidase (Nt(N)-amidase), encoded by the Ntan1 gene.

209 1ab-R2ab) of the N-acetyl-muramoyl-L-alanine amidase of Atl are essential for binding of hTSP-1.

210 The N-acetylmuramoyl-l-alanine amidases of Escherichia coli (AmiA, B and C) are peripla

211 ncoded autolysin (N-acetylmuramoyl-L-alanine amidase) of Streptococcus pneumoniae is believed to play

212 omega-Amidase (omega-amidodicarboxylate amidohydrolase, EC 3.5

213 The results show that amidase operon expression is controlled by a novel type

214 Inducible expression of the aliphatic amidase operon in Pseudomonas aeruginosa is controlled b

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 ydrolytic half-reaction (in this instance an amidase reaction) and confirming that D226 is in the act

227 rolysis at the division site, accompanied by amidase recruitment.

228 Cell division amidases remain largely uncharacterized because substrat

229 We recently showed that the amidases require activation at the cytokinetic ring by p

230 hesis and degradation activities of FtsI and amidases respectively.

231 The mycothiol S-conjugate amidase (amidase) responsible for cleaving MSmB was purified to h

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 ids with 37% identity to rat FAAH within the amidase signature domain (18% over the entire length).

240 y acid amide hydrolase (FAAH) is a mammalian amidase signature enzyme that inactivates neuromodulator

241 ee serine residues that are conserved in all amidase signature enzymes (S217, S218, and S241 in FAAH)

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 e suggest that this enzyme, and possibly the amidase signature family as a whole, may hydrolyze amide

247 lase, is a recently discovered member of the amidase signature family that catalyzes the terminal rea

248 f alkyl amidases, known collectively as the "amidase signature family".

249 FAAH that are conserved among members of the amidase signature family, and have assessed their indivi

250 AH belongs to the amidase signature family, which is characterized by a co

251 nalysis suggests that MAH is a member of the amidase signature family, which is widespread in nature

252 arge class of hydrolytic enzymes termed the "amidase signature family," whose members are defined by

253 reviously identified in other members of the amidase signature family.

254 there are two distinct subgroups within the amidase signature family.

255 d specificity among divergent members of the amidase signature family.

256 ation interface that is not conserved in the amidase signature family.

257 is DNA sequences containing a characteristic amidase signature sequence (PS00571) were identified in

258 limited number of conserved residues in the amidase signature sequence of the enzyme, identifying Se

259 A-subunit, which displays the characteristic amidase signature sequence.

260 of approximately 130 amino acids termed the "amidase signature sequence." Recently, site-directed mut

261 Fatty acid amide hydrolase (FAAH), an amidase-signature family member, is an integral membrane

262 d in vitro (with human serum and recombinant amidase) study was performed in order to generate inform

263 nal fold is related to that of the cell wall amidase, T7 lysozyme, and contains a conserved zinc coor

264 c interaction of Hcp1 with the antibacterial amidase Tae4.

265 o the ring was mediated by an N-terminal non-amidase targeting domain and required the septal ring co

266 We detected the activity of Nt(Q)-amidase, termed Ntaq1, in mouse tissues, purified Ntaq1

267 LpxC is a zinc amidase that catalyses the second step of lipid A biosyn

268 ceramidase (AC) is an intracellular cysteine amidase that catalyzes the hydrolysis of the lipid messe

269 ristoyl]-GlcNAc deacetylase (LpxC) is a zinc amidase that catalyzes the second step of lipid A biosyn

270 e that PlyL is an N-acetylmuramoyl-L-alanine amidase that cleaves the cell wall of several Bacillus s

271 Acid ceramidase (AC) is a lysosomal cysteine amidase that controls sphingolipid signaling by lowering

272 T7 lysozyme is an amidase that cuts a bond in the peptidoglycan layer of t

273 ression of acid ceramidase (AC) - a cysteine amidase that hydrolyses the proapoptotic lipid ceramide

274 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and is c

275 2 (PGLYRP2) is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and is d

276 thiol-S-conjugate amidase, a metal-dependent amidase that is a potential drug target involved in the

277 Treatment of sacculi with an amidase that removes stem peptides enhanced SPOR domain

278 s during elongation and that the periplasmic amidases that aid in cell separation are minor players,

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 4)-GlcNAc, whereas N-acetylmuramyl-L-alanine amidase treatment of the cell wall solubilized surface p

289 The bifunctional trypanothione synthetase-amidase (TRYS) comprises two structurally distinct catal

290 izing enzymes: nitrile hydratase (NHase) and amidase versus nitrilase activity.

291 The activity of hNit2/omega-amidase was determined with alpha-ketoglutaramate and su

292 the radioligand, while stability toward the amidase was evaluated by comparing the Ki of each analog

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 at R1 and R2 are linked to the C-terminus of amidase, whereas R3 is located at the N-terminus of gluc

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