ライフサイエンスコーパス: scissile

1 With respect to the scissile -1/+1 phosphodiester bond, template nucleobases

2 Lys86 and Lys201 interact with the left arm scissile adenine base differently than in structures tha

3 catalytic core domain of MutY show that the scissile adenine is extruded from the DNA helix to be bo

4 between these molecules in the region of the scissile amide bond of MSmB and provides structural evid

5 y a structural rearrangement that places the scissile amide into an oxyanion hole and forces the nucl

6 site zinc ion together bind and activate the scissile amide linkage of acetyllysine.

7 onal asymmetry of abasic interference on the scissile and nonscissile strands highlights the importan

8 analog indole at individual positions of the scissile and nonscissile strands on the rate of single-t

9 basic lesions at individual positions of the scissile and nonscissile strands on the rate of single-t

10 specificity depends on the stability of the scissile base-sugar bond by determining the maximal acti

11 ptide was developed based on the fibronectin scissile bond (269)RAA downward arrowVal(272), and this

12 a double latch structure that sequesters the scissile bond (between Arg(234) and Lys(235)) and minimi

13 d to an unfolded state, in which the cryptic scissile bond (Y1605-M1606) is exposed and can then be p

14 tes for the ubiquitins on either side of the scissile bond allow hOtu1 to discriminate among differen

15 pproximately 9-10 residues C-terminal of the scissile bond and acts as an inducer of conformational f

16 not require a specific distance between the scissile bond and auxiliary substrate binding sites.

17 propeptide cleavage, thereby identifying the scissile bond and characterizing the basic amino acids r

18 ding of the VWF A2 domain, which exposes the scissile bond and exosite for interaction with complemen

19 ysis requires mechanical force to expose the scissile bond and is regulated by a calcium-binding site

20 nt of cleavage-optimal residues flanking the scissile bond and modulate the mechanism for procofactor

21 Mutations of the residues at the scissile bond and mutations and deletions at the termina

22 g salt bridge is then released, exposing the scissile bond and permitting factor D cleavage.

23 of enzyme-mediated scission at the opposite scissile bond and was sufficient to stimulate the format

24 The native structure revealed a scissile bond angle (tau) of 158 degrees, which is close

25 The residues N-terminal to the scissile bond are important in determining rates of hydr

26 ophilic attack on the carbonyl carbon of the scissile bond are present; it is also the first peptidog

27 ible that quinolone interactions at a single scissile bond are sufficient to distort both strands of

28 indicating a slower rate of cleavage of the scissile bond Arg180-Val181.

29 te composition to the C-terminal side of the scissile bond as well as interactions of larger substrat

30 ngly dependent on the sequence preceding the scissile bond as well as position.

31 a general acid to cause the breakdown of the scissile bond at the N-terminal splicing junction.

32 membrane alpha-helices, which results in the scissile bond being positioned adjacent to a glutamate-a

33 is remarkable that the peptide spanning the scissile bond binds to but bypasses cleavage by the enzy

34 nserved A9 and A10 bases reside close to the scissile bond but make distinct contributions to catalys

35 ement of two residues that contribute to the scissile bond by Ala did not eliminate cleavage, but rat

36 pin ribozyme-vanadate complex, indicated the scissile bond can adopt a variety of conformations resul

37 or CG bp at the pb position adjacent to the scissile bond can suppress cleavage without inhibiting b

38 ility were most likely caused by alternative scissile bond choices by tissue-specific gamma-secretase

39 B and TeNT: residues adjacent to the site of scissile bond cleavage (cleavage region) and residues lo

40 ', P3, and P5 sites of SNAP25 contributed to scissile bond cleavage by LC/A, whereas the P1' and P2 s

41 he P1' and P2 sites of SNAP25 contributed to scissile bond cleavage by LC/E.

42 Three additional residues participate in scissile bond cleavage of SNAP25 by LC/E.

43 d loose transition structures with extensive scissile bond cleavage.

44 the active site of the enzyme and across the scissile bond contribute to defining the rate of process

45 indicate that the presence of a nick at one scissile bond dramatically increases the rate of cleavag

46 riants were prepared with mutations swapping scissile bond flanking sequences in the heavy chain indi

47 and the S3 pocket optimize alignment of the scissile bond for cleavage.

48 of the catalytic ribose 2'-hydroxyl with the scissile bond for cleavage.

49 ine) folded properly, but exhibited nonideal scissile bond geometries (tau ranging from 118 degrees t

50 e stability and regulate the exposure of the scissile bond in full-length VWF.

51 tep of splicing and for maintaining the (-1) scissile bond in its unusual conformation.

52 or conformational change to expose the first scissile bond in prothrombin, which is the likely event

53 nding site and resultant displacement of the scissile bond in the active site results in the observed

54 force is transduced from the polymer to the scissile bond in the mechanophore (i.e., mechanochemical

55 Cleavage of the Tyr(1605)-Met(1606) scissile bond in the VWF A2 domain depends on a Glu(1660

56 presence of the quinolone CP-115,953 at one scissile bond increased the extent of enzyme-mediated sc

57 rtially coordinated and that cleavage at one scissile bond increases the degree of cleavage at the ot

58 In the crystal structure, the scissile bond is located within the double-stranded DNA,

59 The scissile bond is not correctly positioned for hydrolysis

60 form of CPD was determined and revealed the scissile bond Leu(3428)-Ala(3429) captured in the cataly

61 horothioate substitution is installed at the scissile bond normally cleaved by the HHRz, Pt(II) cross

62 tween the stereochemical permutation and the scissile bond of the mechanophore.

63 The scissile bond of the substrate must be activated for bon

64 on of the cleavage specificity of the Arg506 scissile bond on the A2 domain of factor Va.

65 eavage by human topoisomerase IIalpha at the scissile bond on the opposite strand.

66 rmational changes in C4 are induced, and its scissile bond region becomes ordered and inserted into t

67 n GLP-1 and GIP, a single thioamide near the scissile bond renders these peptides up to 750-fold more

68 sights into nucleic acid geometry around the scissile bond required for hydrolysis.

69 ermined by a combination of stalk length and scissile bond sequence.

70 tended peptide sequences before or after the scissile bond showed endopeptidase to be superior to dip

71 of the metalloprotease domain of ADAMTS13 in scissile bond specificity, we identified 3 variable regi

72 odification of the downstream helix affected scissile bond specificity.

73 yl, so as to enable the nitrogen atom of the scissile bond to accept the proton that is necessary for

74 he enzyme and facilitate presentation of the scissile bond to the active site of the catalyst.

75 ed to result in greater cleavage than if the scissile bond was at the CH1 end of the hinge.

76 orts the binding loop in the vicinity of the scissile bond was found to be important both for enzyme

77 that replaced the 3'-bridging oxygen of the scissile bond with a sulfur atom (i.e. 3'-bridging phosp

78 non-bridging oxygen atoms at (and near) the scissile bond with sulfur atoms.

79 fs that are required for the cleavage of the scissile bond within an active site.

80 VWF) unfolding which exposes the Y1605-M1606 scissile bond within the VWF A2 domain for cleavage by A

81 nning Thr(432)-Gly(445) (i.e. containing the scissile bond) reduced versican-V1 processing.

82 (at the +2 or +3 position 3' relative to the scissile bond), 3,N(4)-ethenodeoxycytidine, 3,N(4)-ethen

83 idues immediately prior to and following the scissile bond).

84 f short amino acid sequences surrounding the scissile bond, -Pro(12)-Asn(13)-, indicated that P2 Gly

85 hydrophobic amino acids on both sides of the scissile bond, and catalytic properties.

86 NA and DNA IBS1 targets, presentation of the scissile bond, and stabilization of the structure by met

87 s a hydroxyethylamine moiety in place of the scissile bond, binds in two equivalent antiparallel orie

88 Adjacent to the scissile bond, four bases are stacked in a tightly sandw

89 intact fibronectin at the Ala(271)/Val(272) scissile bond, generating an approximately 30-kd fragmen

90 ds the leucine 10 residues C-terminal to the scissile bond, is critical for collagenolysis and repres

91 neurotoxin (TeNT) cleave VAMP-2 at the same scissile bond, their mechanism(s) of VAMP-2 recognition

92 bunit favors acidic residues proximal to the scissile bond, while the alpha subunit prefers small or

93 promiscuity at P3 and on the P' side of the scissile bond.

94 he transition state and leaving group of the scissile bond.

95 ained a 3'-bridging phosphorothiolate at the scissile bond.

96 posure of the ADAMTS13 binding sites and the scissile bond.

97 ce for BoNT F substrate recognition near the scissile bond.

98 ility when lesions are positioned around the scissile bond.

99 and hydrophobic groups on either side of the scissile bond.

100 (Asp(19-22) in humans) preceding the Lys-Ile scissile bond.

101 ntermolecular contacts on either side of the scissile bond.

102 rates that contain an activated, non-natural scissile bond.

103 s small or aromatic amino acids flanking the scissile bond.

104 ry in extracellular domain 3 upstream of the scissile bond.

105 ues on both prime and non-prime sides of the scissile bond.

106 (525) or by an antibody to the region of the scissile bond.

107 lates well with the force experienced by the scissile bond.

108 the active site that binds tRNA far from the scissile bond.

109 tion is often present in the vicinity of the scissile bond.

110 recognizes the C4 C345C domain 60 A from the scissile bond.

111 and reveals cryptic exosites as well as the scissile bond.

112 in conjunction with the phosphate 3' to the scissile bond; the same Lys is also hydrogen bonded with

113 ve site suggested that Asp195 may facilitate scissile-bond activation and that His247 is oriented to

114 ues and divalent cations are responsible for scissile-bond cleavage.

115 uential presentation and cleavage of the two scissile bonds in prothrombin activation is accomplished

116 ting the cleavages of both Arg336 and Arg562 scissile bonds in the cofactor.

117 t CA and UA dinucleotides, preferentially at scissile bonds located more than five nucleotides away f

118 , the human enzyme appears to ligate the two scissile bonds of a cleavage site in a nonconcerted fash

119 ent cleavages of the two spatially separated scissile bonds of FIX.

120 quired for optimal cleavage rates of the two scissile bonds of FIX.

121 urface for optimum proteolytic attack on the scissile bonds of membrane-bound protein substrates such

122 The fact that there are two scissile bonds per double-stranded DNA break implies tha

123 core sequence of amino acids surrounding the scissile bonds responsible for governing the relative pr

124 for etoposide, which must be present at both scissile bonds to stabilize a double-stranded DNA break.

125 contribution of prime residues flanking the scissile bonds to the enhanced rates.

126 , interacts with the sequences distal to the scissile bonds whereas the CTD beta1-beta2 loop binds to

127 ated in large part by sequences flanking the scissile bonds.

128 of polymers bearing three putatively "weak" scissile bonds: the carbon-nitrogen bond of an azobisdia

129 When sulfur is in the scissile bridging position, a highly associative transit

130 ne mass unit is added to the carbon end of a scissile C-H bond and when one mass unit is added to the

131 hydroxylation that correlated well with the scissile C-H bond energy, indicating a homolytic hydroge

132 hat substrate binding forces the substrate's scissile carboxylate group into the neighborhood of seve

133 DCase) furnishes a counterion that helps the scissile carboxylate group of the substrate leave water

134 The mechanical strength of scissile chemical bonds plays a role in material failure

135 inner-sphere metal interactions made by the scissile DNA phosphate and conserved Asp90 carboxylate a

136 ne metal ion shifts away from binding at the scissile DNA phosphate to a position near the 3'-adjacen

137 the small subunit and the nicked ends of the scissile DNA strand, mimicking the previously unseen tra

138 ntaining Ara-C at the +1 position of the non-scissile DNA strand.

139 S the specificity for a 3'-O location of the scissile ester bond could be forced to the 2'-position b

140 c through the glycine carbonyl oxygen of its scissile G approximately VV triplet.

141 e differently than in structures that have a scissile guanine.

142 ect of fluorine substitution adjacent to the scissile isopeptide bond.

143 alled as an electrophilic replacement of the scissile isopeptide bond.

144 particular interest is the activation of non-scissile mechanophores in which latent reactivity can be

145 In Flp, the base immediately 5' to the scissile MeP strongly influences the choice between the

146 k) is correlated with the instability of the scissile O-P bond through computed bond lengths.

147 rgely formed bond to the nucleophile and the scissile P-S bond is little changed.

148 We mutated residues in and around the scissile P1-P1' bond in PCI and alpha1AT, resulting in s

149 eases cleave the serpin reactive center loop scissile P1-P1' bond, resulting in serpin-protease suici

150 The (1)J(NC') coupling constant for the (-1) scissile peptide bond at the N-extein-intein junction wa

151 ity to both the active site Cys(184) and the scissile peptide bond between threonine and glycine.

152 loy a splicing pathway in which the upstream scissile peptide bond is consecutively rearranged into t

153 The protonation of the scissile peptide bond nitrogen by a hydronium ion is an

154 We suggest that NRho plays a role in scissile peptide bond selectivity by optimally positioni

155 The thermodynamic stability of the scissile peptide bond was not dependent on CTRC or Leu-8

156 ature, a highly strained conformation at the scissile peptide bond, had been identified and was hypot

157 e analogues in which an oxirane replaces the scissile peptide bond.

158 ks the re face of the carbonyl carbon of the scissile peptide bond.

159 - so that the Pd(II) complex approaches the scissile peptide bond.

160 t resists APN degradation due to a distorted scissile peptide bond.

161 d residue located directly N-terminal to the scissile peptide bond.

162 dence that the adenine immediately 3' to the scissile phosphate (A1) acts as a general acid.

163 revious work showed that substitution of the scissile phosphate (P) by methylphosphonate (MeP) permit

164 ious work we showed that substitution of the scissile phosphate (P) by the charge neutral methylphosp

165 VRR nuc) domain, enabling FAN1 to incise the scissile phosphate a few bases distant from the junction

166 Optimal positioning of the scissile phosphate additionally required active site con

167 Five of the metals bind within 12 A of the scissile phosphate and coordinate the majority of the ox

168 y be required for correct positioning of the scissile phosphate and coordination of catalytic residue

169 interaction with the 3'-bridging atom of the scissile phosphate and facilitates DNA scission by the b

170 ltured in isolation, and it shows an ordered scissile phosphate and nucleotide 5' to the cleavage sit

171 ed at 3.1-A resolution exhibits a disordered scissile phosphate and nucleotide 5' to the cleavage sit

172 the HHRz cleavage site may include both the scissile phosphate and the 2' nucleophile.

173 del suggests that the pro-R(P) oxygen of the scissile phosphate and the 2'-hydroxyl nucleophile are i

174 Trp330 also assists in the activation of the scissile phosphate and the departure of the 5'-hydroxyl

175 Positions of the scissile phosphate and two catalytic metal ions are inte

176 e optimal spacing between the 5' end and the scissile phosphate appears to be eight nucleotides for R

177 c attack on the conformationally constrained scissile phosphate at the intron-3'-exon junction.

178 r, a single phosphorothioate in place of the scissile phosphate blocks cleavage; the phosphorothioate

179 form an A-helix for correct positing of the scissile phosphate bond for cleavage in RNAi.

180 a fully assembled active site including the scissile phosphate bound by a divalent metal ion cofacto

181 ied at the end of the active site, while the scissile phosphate bridges two active site Mg(2+) ions.

182 nt is mediated by nucleophilic attack on the scissile phosphate by a conserved tyrosine residue, form

183 Substitution of the scissile phosphate by an electrically neutral methylphos

184 by replacement of the 5'-oxygen atom at the scissile phosphate by sulfur (5'-PS), which is a much be

185 eway, and double-base unpairing flanking the scissile phosphate control precise flap incision by the

186 ft in position together with movement of the scissile phosphate deeper into the active site cleft.

187 Placement of the scissile phosphate diester in the active site required t

188 The first site is the scissile phosphate diester linkage and nucleotides downs

189 nt manganese rescue was not observed for the scissile phosphate diester linkage implying that electro

190 double nucleotide unpairing that places the scissile phosphate diester on active site divalent metal

191 unpairing the 5'-end of duplex to permit the scissile phosphate diester to contact catalytic divalent

192 interactions that successively position the scissile phosphate for bottom-strand cleavage at the DNA

193 hree-base interaction may be to position the scissile phosphate for cleavage, rather than to directly

194 with a role for the metal in positioning the scissile phosphate for cleavage.

195 esized to be required for positioning of the scissile phosphate for DNA cleavage to take place.

196 atalysis depends acutely on proper metal and scissile phosphate geometry.

197 nt metal ion and the 3'-bridging atom of the scissile phosphate greatly enhances enzyme-mediated DNA

198 eaturing a common, novel conformation of the scissile phosphate group as compared to all previous Eco

199 oxygen atom of the phosphate group 3' to the scissile phosphate group.

200 joining in native DNA substrates containing scissile phosphate groups.

201 S1 nucleotide) or 3' (S1' nucleotide) of the scissile phosphate had large effects on substrate utiliz

202 t 1.95 A, reveals an Mg(2+) ion bound to the scissile phosphate in a position corresponding to Mg(B)

203 ning of the catalytic serine relative to the scissile phosphate in the active site.

204 om in place of the 3'-bridging oxygen of the scissile phosphate in the presence of Mg2+, Mn2+, or Ca2

205 igration of one proton from the water to the scissile phosphate in the transition state.

206 A Mn2+ binding site on the scissile phosphate is also disrupted in the E45A structu

207 tereospecific phosphorothioate effect at the scissile phosphate is consistent with a significant stab

208 The scissile phosphate is well placed to interact with the p

209 rate helix docking event that constrains the scissile phosphate linkage and positions G8 and A38 for

210 tonated C75 to the nonbridging oxygen of the scissile phosphate occurs to stabilize the phosphorane i

211 sult from placing an acidic residue near the scissile phosphate of the bound ssDNA.

212 tors in allowing metal interactions with the scissile phosphate of the mHHRz.

213 I domain, which can be extended to place the scissile phosphate of the target strand adjacent to the

214 Ruler to form a protein-DNA complex with the scissile phosphate positioned at the active site for opt

215 catalysis, the nucleophile is aligned with a scissile phosphate positioned proximal to the A-9 phosph

216 ependent DNA deformations that influence the scissile phosphate positioning and reactivity.

217 Each scissile phosphate that is two base pairs from the cross

218 cond metal ion and a nonbridging atom of the scissile phosphate that stimulates DNA cleavage mediated

219 ics; neutralizing the negative charge on the scissile phosphate through methylphosphonate (MeP) subst

220 by compensatory charge neutralization of the scissile phosphate via methylphosphonate (MeP) modificat

221 roup (the non-bridging 3'-oxygen atom of the scissile phosphate) during the hydrolysis reaction.

222 PPT positions -2, -4 and +1 (relative to the scissile phosphate) substantially reduces (+)-strand pri

223 tive site and the non-bridging oxygen of the scissile phosphate, a feature found previously also for

224 taining the complete intron, both exons, the scissile phosphate, and all of the functional groups imp

225 s state, the nucleophile is in line with the scissile phosphate, and the N1 position of G33 and N3 po

226 coordinated by a conserved aspartate and the scissile phosphate, as observed in the restriction endon

227 a U-1 forms the most robust kink around the scissile phosphate, exposing it to the catalytic C75 in

228 2') to G40 is concomitant with attack of the scissile phosphate, followed by the remainder of the cle

229 ting SRL, containing a 3'-sulfur atom at the scissile phosphate, reacts at a fully diffusion-limited

230 R(p) oxygen of the phosphate group 3' of the scissile phosphate, suggesting possible roles for these

231 The scissile phosphate, the first bond in the duplex DNA adj

232 the modeled G53 2'-OH group that attacks the scissile phosphate, thus suggesting a direct role in gen

233 The citrate fills the binding site for the scissile phosphate, wherein it is coordinated by Arg237,

234 cleophile requiring a closer approach to the scissile phosphate, which in turn increases the barrier.

235 interaction with the 3'-bridging atom of the scissile phosphate, while the other (M(2)(2+)) is believ

236 ng oligodeoxynucleotides substituted, at the scissile phosphate, with isomeric phosphorothioates and

237 eractions with the nonbridging oxygen of the scissile phosphate.

238 imal position for nucleophilic attack of the scissile phosphate.

239 nd its ligands, a water molecule attacks the scissile phosphate.

240 inate manganese and a sulfate mimetic of the scissile phosphate.

241 OPRIM (topoisomerase/primase) domain and the scissile phosphate.

242 s incompatible with an in-line attack to the scissile phosphate.

243 that neutralizes the negative charge on the scissile phosphate.

244 ing oxygen or the nonbridging oxygens of the scissile phosphate.

245 its exocyclic N2 interacts directly with the scissile phosphate.

246 to interact with a nonbridging oxygen of the scissile phosphate.

247 interaction with the 3'-bridging atom of the scissile phosphate.

248 ucleophile's proton during its attack on the scissile phosphate.

249 o the active site, mimicking the charge of a scissile phosphate.

250 B and bringing the nucleophile close to the scissile phosphate.

251 the hydroxyl for in-line displacement at the scissile phosphate.

252 rectly ligated to the pro-S(p) oxygen of the scissile phosphate.

253 ubstrate through a nonbridging oxygen of the scissile phosphate.

254 ge of RNA through transesterification of the scissile phosphate.

255 contacts with the RNA strand adjacent to the scissile phosphate.

256 erine, leading to nucleophilic attack on the scissile phosphate.

257 hance the interaction of the enzyme with the scissile phosphate.

258 ated to the non-bridging oxygen atoms of the scissile phosphate; for the latter, additional evidence

259 The scissile phosphates are found midway between their posit

260 more ambiguous third site bridges the A9 and scissile phosphates in a manner consistent with that of

261 Cleavage events at the scissile phosphates on complementary strands of the dupl

262 aining a phosphoramidate substitution at the scissile phosphates were resistant to cleavage by the en

263 Intercalation at the scissile phosphodiester (between the +1 and -1 base pair

264 We find that resolution is optimal when the scissile phosphodiester (Tp/N) is located two nucleotide

265 The residues in ONC that are proximal to the scissile phosphodiester bond (His10, Lys31, and His97) a

266 activity (type II) that directly targets the scissile phosphodiester bond in DNA.

267 The scissile phosphodiester bond is located immediately 3' o

268 ed at the catalytic center, bringing the two scissile phosphodiester bonds into close proximity.

269 widely spaced IN active sites to access the scissile phosphodiester bonds.

270 philic water molecules thought to attack the scissile phosphodiester bonds.

271 6-deoxyadenosine (dA) positions flanking the scissile phosphodiester slow the rate of DNA religation

272 II recognizes its substrates and selects the scissile phosphodiester(s) by recognizing specific RNA s

273 nternal loop, in which is located the single scissile phosphodiester.

274 of the tyrosine nucleophile (Tyr-274) at the scissile phosphodiester.

275 icked-site substrate at the positions of the scissile phosphodiesters result in abolition or inhibiti

276 water molecule to the phosphorus atom of the scissile phosphoester bond, with the attacking water bei

277 s via an in-line-attack by CYT 17 O2' on the scissile phosphorous (ADE 1.1 P), and is therefore consi

278 with an abortive 3'-terminal dC close to the scissile position in the enzyme active site, providing i

279 design, the adenosine ribonucleotide at the scissile position of the 8-17 DNAzyme was replaced by 2'

280 bstrates containing a phosphate group at the scissile position.

281 troducing tetrahydrofuran lesions around the scissile PPT/unique 3'-sequence junction indicate that t

282 This new platform can also be used to screen scissile ribozymes for improved catalysis.

283 the AT(1)R-associated short form suggested a scissile site located within the Arg(363)-Arg(393) regio

284 delivery to the active site of the selected scissile sites further implicates the existence of a pre

285 ed to determine the timing of three selected scissile sites in lambdaN approaching the proteolytic si

286 ts the "almost complete" delivery of all the scissile sites in lambdaN to the proteolytic site in an

287 The subsequent cleavage of the scissile sites in lambdaN, however, appears to lack a sp

288 eptide bond cleavage and the delivery of the scissile sites near the amino- versus carboxyl-terminal

289 Distortion of the scissile strand at the -4 position 5' to the cleavage si

290 ns become energetically more damaging as the scissile strand is shortened from 32 to 24 and 18 nucleo

291 rand in the context of duplexes in which the scissile strand length was progressively shortened.

292 -Oxo substitutions at the -1 position in the scissile strand slowed single-turnover cleavage by a fac

293 s effects of eliminating the +2T base on the scissile strand were rectified by introducing the nonpol

294 aced the -1N, +1T, +2T, and +4C bases of the scissile strand, but abasic lesions at +5C and +3C had l

295 basic sites within the CCCTT sequence of the scissile strand, but an abasic lesion at the 5'-OH nucle

296 e for a cytosine at the (-1) position on the scissile strand.

297 n combined with 8-oxoA at position -1 in the scissile strand.

298 eus cleaves LPXTG-containing proteins at the scissile T-G peptide bond and ligates protein-LPXT to th

299 The scissile T-G peptide bond is positioned between the acti

300 leavage by analyzing the conformation of the scissile X-Pro peptide bond, and by comparing the rate c