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 abilization of reaction intermediates at the scissile alkene.

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

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

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

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

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

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

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

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

11 d the eight residues flanking the prelamin A scissile bond (TRSY LLGN) to all other 19 amino acids, c

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

41 d loose transition structures with extensive scissile bond cleavage.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

56 ge at Gly(2196)-Leu(2197) We noted that this scissile bond is in the linker between fibronectin modul

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

58 The scissile bond is not correctly positioned for hydrolysis

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

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

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

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

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

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

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

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

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

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

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

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

71 odification of the downstream helix affected scissile bond specificity.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

99 ility when lesions are positioned around the scissile bond.

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

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

102 ntermolecular contacts on either side of the scissile bond.

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

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

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

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

107 (525) or by an antibody to the region of 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 in conjunction with the phosphate 3' to the scissile bond; the same Lys is also hydrogen bonded with

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

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

113 Moreover, we identified multiple additional scissile bonds in an N-terminal linker region of LTBP4 t

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

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

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

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

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

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

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

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

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

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

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

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

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

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

128 rtion is dictated by the polarization of the scissile C-C bond.

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

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

131 an inhibitor carbonyl carbon that mimics the scissile carbonyl of substrates is pyramidalized and jus

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

163 ) in the active site that interacts with the scissile phosphate and anchors the general base guanine

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

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

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

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

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

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

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

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

172 O2' nucleophile, and the conformation at the scissile phosphate and the position of the general base

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

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

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

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

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

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

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

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

181 Substitution of the scissile phosphate by an electrically neutral methylphos

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

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

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

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

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

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

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

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

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

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

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

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

194 cond hydrated Mg(2+) ion that approaches the scissile phosphate from its binding site in the pre-clea

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

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

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

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

199 joining in native DNA substrates containing scissile phosphate groups.

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

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

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

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

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

205 movement of protein and DNA, delivering the scissile phosphate into the rearranged active site.

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

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

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

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

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

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

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

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

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

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

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

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

218 ween the two catalytic sites, in order for a scissile phosphate to attract a metal ion to the A-site

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

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

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

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

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

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

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

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

227 2') to G40 is concomitant with attack of the scissile phosphate, followed by the remainder of the cle

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

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

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

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

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

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

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

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

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

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

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

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

240 that neutralizes the negative charge on the scissile phosphate.

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

242 rial EndoV binds only 2 or 3 nt flanking the scissile phosphate.

243 eractions with the nonbridging oxygen of the scissile phosphate.

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

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

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

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

248 imal position for nucleophilic attack of the scissile phosphate.

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

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

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

252 ubstrate through a nonbridging oxygen of the scissile phosphate.

253 its exocyclic N2 interacts directly with the scissile phosphate.

254 ucleophile's proton during its attack on 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 ated to the non-bridging oxygen atoms of the scissile phosphate; for the latter, additional evidence

258 The scissile phosphates are found midway between their posit

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

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

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

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

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

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

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

266 The scissile phosphodiester bond is located immediately 3' o

267 mal structure, integrase gains access to the scissile phosphodiester bonds by lifting DNA off the his

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 1Cas9, the active site is seen poised at the scissile phosphodiester linkage of the target strand, pr

272 6-deoxyadenosine (dA) positions flanking the scissile phosphodiester slow the rate of DNA religation

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

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

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

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

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

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

279 bstrates containing a phosphate group at the scissile position.

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

281 limited by modest force-free stability or a scissile response that caps mechanoacid generation at on

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