ライフサイエンスコーパス: carboxypeptidase

1 s AEG-1) and PGCP (encoding plasma glutamate carboxypeptidase).

2 d di-peptidylpeptidases, aminopeptidases and carboxypeptidases).

3 inding protein-like 2 (AGBL2), a cytoplasmic carboxypeptidase.

4 minal processing may occur via a progressive carboxypeptidase.

5 ses pcd, and Nna1 is a highly conserved zinc carboxypeptidase.

6 rminal lysine residues of the heavy chain by carboxypeptidase.

7 d stems in mature peptidoglycan by an active carboxypeptidase.

8 st that DacA-1 is V. cholerae's principal DD-carboxypeptidase.

9 as dual activity, acting as an amidase and a carboxypeptidase.

10 of alpha- and beta-secretases, and resident carboxypeptidase.

11 ge for some members of the M14A subfamily of carboxypeptidases.

12 cells and in mutants lacking one or more D,D-carboxypeptidases.

13 partoacylase is closely analogous to that of carboxypeptidases.

14 idic residue is not conserved in the various carboxypeptidases.

15 proteins that are homologous to known serine carboxypeptidases.

16 ic activities, including aminopeptidases and carboxypeptidases.

17 within a novel family of mammalian cytosolic carboxypeptidases.

18 er of proteins, including the M14B subfamily carboxypeptidases.

19 a disruption in the gene encoding cytosolic carboxypeptidase 1 (CCP1).

20 mutation within the gene encoding cytosolic carboxypeptidase 1 (CCP1/Nna1), which has homology to me

21 l region of beta3-tubulin, whereas cytosolic carboxypeptidase 1 shortens the side chain without cleav

22 Cytosolic carboxypeptidase 5 (CCP5) is a member of a subfamily of

23 ic extracts more than 80 years ago and named carboxypeptidase A (CPA; now known as CPA1).

24 ology in mice, at least in part by releasing carboxypeptidase A and possibly other proteases, which c

25 tifying protein targets of namalide selected carboxypeptidase A as the third highest scoring hit.

26 ogs containing l-Lys or l-allo-Ile inhibited carboxypeptidase A at submicromolar concentrations.

27 Furthermore, serglycin, tryptase, and carboxypeptidase A messenger RNA transcripts were detect

28 The A. aegypti carboxypeptidase A promoter was used to express the IR R

29 ine (D-PEN) catalyzes zinc(II) transfer from carboxypeptidase A to chelators such as thionein and EDT

30 modeling (periostin, POSTN), and mast cells (carboxypeptidase A, CPA3).

31 mast cell protease 1, cationic trypsinogen, carboxypeptidase A, IL-5, and phospholipase Cgamma.

32 The racemic amino acid was resolved by carboxypeptidase A-catalyzed hydrolysis of the N-trifluo

33 el of aspartoacylase based on zinc dependent carboxypeptidase A.

34 ical zinc hydrolases such as thermolysin and carboxypeptidase A.

35 that of zinc-dependent hydrolases related to carboxypeptidases A.

36 thiol group with N-ethyl-maleimide and using carboxypeptidase-A to stabilize the R-quaternary conform

37 fferentiation of progenitor cells expressing carboxypeptidase A1 (CPA1) and neurogenin 3 (NEUROG3).

38 ule content proteins amylase, prolipase, pro-carboxypeptidase A1, pro-elastase II, chymotrypsinogen B

39 se B, and Zn(2+) reduction (hZnT8RW) induced carboxypeptidase A1.

40 nsense variant rs199695765 in CPA2, encoding carboxypeptidase A2, was highly associated with pancreat

41 tain snakes and that mouse mast cell-derived carboxypeptidase A3 (CPA3) can contribute to this effect

42 ressed under the control of a segment of the carboxypeptidase A3 (Cpa3) promoter.

43 f circulating basophils; whole-blood FCER1A, carboxypeptidase A3 (CPA3), and L-histidine decarboxylas

44 luding Charcot-Leydon crystal protein (CLC); carboxypeptidase A3 (CPA3); deoxyribonuclease I-like 3 (

45 s tryptase (p<0.0001), chymase (p=0.02), and carboxypeptidase A3 (p=0.02) in severe asthma.

46 ase (r = .75), the mast cell-specific marker carboxypeptidase A3 (r = .74), and uPGD-M (r = 0.74).

47 tryptases, mMCP-6 and mMCP-7, or MC-specific carboxypeptidase A3 activity are not protected.

48 racterized by the expression of tryptase and carboxypeptidase A3 but not chymase.

49 e mast cell proteases tryptase, chymase, and carboxypeptidase A3 by using real-time PCR and measured

50 Tryptase and carboxypeptidase A3 expression in epithelial brushings a

51 n combined with IL-33 increased tryptase and carboxypeptidase A3 immunostaining in mast cell precurso

52 luding proteases of tryptase-, chymase-, and carboxypeptidase A3 type that are electrostatically boun

53 The expression of chymase, carboxypeptidase A3, cathepsin G, granzyme B, and the tr

54 With regard to carboxypeptidase A3, it was confirmed that the enzyme wa

55 d that protein extracts from wild type (WT), carboxypeptidase A3-, and MCPT6-deficient mice and MCs a

56 the tryptase mouse mast cell protease-6, and carboxypeptidase A3.

57 and -4; and an elastase, mMCP-5; along with carboxypeptidase-A3 (CPA3).

58 The complex between human carboxypeptidase A4 and NvCI has been crystallized and d

59 s an extended and novel interface with human carboxypeptidase A4, responsible for inhibitory constant

60 Carboxypeptidase A5 (cpa5), a MC-specific enzyme, is exp

61 otch receptor expression in cells expressing carboxypeptidase A5 (cpa5), a zebrafish mast cell-specif

62 Carboxypeptidase A6 (CPA6) is a member of the A/B subfam

63 Carboxypeptidase A6 (CPA6) is a member of the M14 metall

64 Carboxypeptidase A6 (CPA6) is an extracellular matrix-bo

65 The carboxypeptidase ACE2 is a homologue of angiotensin-conv

66 ACE-related carboxypeptidase (ACE2) may counterbalance the angiotens

67 angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane pr

68 , we report a fluorometric method to measure carboxypeptidase activities that cleave the proline-phen

69 nd preserved TAFI-mediated anti-inflammatory carboxypeptidase activities toward bradykinin and presum

70 ndicates reduced PG cross-linking, increased carboxypeptidase activities, increased N-deacetylation,

71 ertion in csd6, which we demonstrated has ld-carboxypeptidase activity and cleaves monomeric tetrapep

72 lasses of PBP, class C LMM-PBPs show high dd-carboxypeptidase activity and rapidly hydrolyze syntheti

73 Purified His-tagged NtSCP1 had carboxypeptidase activity in vitro.

74 de processing for MHC class I by introducing carboxypeptidase activity into the process.

75 ferase activity of class A PBP1b and the D,D-carboxypeptidase activity of DacA in addition to the L,D

76 nd MIP-1095 potently inhibited the glutamate carboxypeptidase activity of PSMA (K(i) = 4.6 +/- 1.6 nm

77 SVBP, exhibited robust and specific Tyr/Phe carboxypeptidase activity on microtubules.

78 Finally, expression of PSMA mutants lacking carboxypeptidase activity reduced the impact of PSMA exp

79 PSMA's carboxypeptidase activity releases glutamate from vitami

80 ctedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic

81 stem pentapeptide (the substrate for the dd-carboxypeptidase activity) and the 4,3-cross-linked pept

82 e absence of tripeptides, consistent with ld-carboxypeptidase activity, which was confirmed biochemic

83 units, suggesting the presence of dd- and ld-carboxypeptidase activity.

84 plasma significantly reduces the SDF-1alpha carboxypeptidase activity.

85 Here, we show that a defect in the putative carboxypeptidase ALTERED MERISTEM PROGRAM1 (AMP1) causes

86 uggesting that meropenem inhibits both a D,D-carboxypeptidase and an L,D-transpeptidase.

87 meso-2,6-diaminopimelic acid in both the DD-carboxypeptidase and DD-endopeptidase activities of a cl

88 422) were mutated, and the effect on both DD-carboxypeptidase and DD-endopeptidase activities was det

89 ding protein (LMM-PBP) and possesses both dd-carboxypeptidase and dd-endopeptidase activity.

90 e demonstrated that NG1686 possesses both dd-carboxypeptidase and endopeptidase activities.

91 PBP4 is a bifunctional enzyme having both dd-carboxypeptidase and endopeptidase activities.

92 C, respectively), is believed to catalyze DD-carboxypeptidase and endopeptidase reactions in vivo.

93 ers, with turnover number similar to that of carboxypeptidase and substrate specificity slightly lowe

94 Substrates for both the dd-carboxypeptidase and the 4,3-endopeptidase activities we

95 domain from Streptomyces albus G D-Ala-D-Ala carboxypeptidase and to the N-terminal prodomain of huma

96 are believed to catalyze d-alanyl-d-alanine carboxypeptidase and transpeptidase reactions in vivo.

97 gical media but show efficient processing by carboxypeptidases and efficiently yield the free nucleos

98 ases, the endoproteases that work along with carboxypeptidases and other modifying enzymes, such as t

99 to prevent both the PG-stem modification by carboxypeptidases and the cell wall degradation by autol

100 tter features, overexpression of cytoplasmic carboxypeptidase, and aberrant expression of CD30, toget

101 e N (CPN, also known as kininase I, arginine carboxypeptidase, and anaphylotoxin inactivator).

102 l for ligand recognition and catalysis by DD-carboxypeptidases, and suggest a coupling of conformatio

103 E 10/10 in which macrophages overexpress the carboxypeptidase angiotensin-converting enzyme (ACE).

104 Thrombin-activatable carboxypeptidase B (CPB), also called thrombin-activatab

105 Plasma carboxypeptidase B (CPB), which is activated by the thro

106 the crystal structure of porcine pancreatic carboxypeptidase B (pp-CpB) in complex with a variety of

107 s B, C and F bound to the surrogate protease carboxypeptidase B revealed the binding modes of these l

108 ral product inhibitors in a modified porcine carboxypeptidase B revealed their binding mode and provi

109 The cap is subsequently removed with carboxypeptidase B to yield mature biologically active I

110 Carboxypeptidase B treatment decreased cell-dependent pl

111 the enzymatic activity and concentration of Carboxypeptidase B was developed.

112 ombining targeted specific proteolysis using carboxypeptidase B with a proteomics approach using two-

113 to 2.05-A resolution and demonstrate robust carboxypeptidase B-like activity for the enzyme.

114 Carboxypeptidase B-sensitive plasminogen binding sites p

115 ys]Pg activation kinetics with wild-type SK, carboxypeptidase B-treated SK, and a COOH-terminal Lys41

116 We found a complement-related peptidase, carboxypeptidase B1 (Cpb1), to be required for caspase-1

117 n oxidative modification and inactivation of carboxypeptidase B1 (CPB1).

118 lopeptidases, reflected in low expression of carboxypeptidase B1, prevented optimal Ag-specific CD4(+

119 proteolytic cleavage by thrombin and plasma carboxypeptidase B2 (CPB2) at a highly conserved cleavag

120 d N-terminal fragment (OPN-R), thrombin- and carboxypeptidase B2-double-cleaved N-terminal fragment (

121 structure is similar to that of dipeptide ld-carboxypeptidase, but with an additional loop proximal t

122 ignature catalytic triad found in all serine carboxypeptidases, but its biological function is comple

123 Analogous to the active site of Zn(2+) carboxypeptidases, calnuc has two high affinity (K(d) ap

124 fied in the mouse genome and named cytosolic carboxypeptidase (CCP) 2 through 6.

125 CCP1) defines the 6-member cytosolic carboxypeptidase (CCP) family that metabolizes polygluta

126 bules can be deglutamylated by the cytosolic carboxypeptidase CCP1.

127 persistent MT growth requires the cytosolic carboxypeptidase CCPP-6, which promotes Delta2 modificat

128 The cytosolic carboxypeptidases (CCPs) are a subfamily of metalloenzym

129 em163S by plasmin to chem158K, followed by a carboxypeptidase cleavage, leads to the most active isof

130 te that BRS1 is a secreted and active serine carboxypeptidase, consistent with the hypothesis suggest

131 ementing the actions of well known digestive carboxypeptidases CPA and CPB.

132 Human digestive carboxypeptidases CPA1, CPA2, and CPB1 are secreted by t

133 Peptidoglycan modifying carboxypeptidases (CPs) are important determinants of ba

134 expressing vps27(S613A), MVB sorting of the carboxypeptidase Cps1 and of the alpha-factor receptor S

135 Carboxypeptidase D (CPD) functions in the processing of

136 related duck hepatitis B virus (DHBV), duck carboxypeptidase D (DCPD) has been proposed as the speci

137 Duck carboxypeptidase D (DCPD) interacts with the full-length

138 monomeric transthyretin-like domain of human carboxypeptidase D aggregates under close to physiologic

139 but at the same time they put proteins like carboxypeptidase D at risk of aggregation in biological

140 cted over temperature for D-alanyl-D-alanine carboxypeptidases (dac1 and dac2), DEAD-box RNA helicase

141 We purified a candidate D,D-carboxypeptidase DacB2 and showed that meropenem indeed

142 s of tubulin glutamyl ligase and cytoplasmic carboxypeptidase deglutamylase enzymes maintain organell

143 hows close structural similarity to those of carboxypeptidases despite only 10-13% sequence identity

144 Cathepsin A (CatA) is a serine carboxypeptidase distributed between lysosomes, cell mem

145 Modeling suggests that the carboxypeptidase domain folds into a structure that rese

146 nied by downregulation of genes encoding for carboxypeptidase E (CPE) and Interleukin 1B (IL1B) in th

147 ferent peptide precursor processing enzymes: carboxypeptidase E (CPE) and the prohormone convertases

148 med a yeast two-hybrid screen and identified carboxypeptidase E (CPE) as a binding partner for the mi

149 t on the expression of the convertase enzyme carboxypeptidase E (CPE) by inhibition of the eukaryotic

150 (here called Pomc-Foxo1(-/-) mice) increases Carboxypeptidase E (Cpe) expression, resulting in select

151 The carboxypeptidase E (CPE) gene is expressed in human lens

152 We have previously shown that carboxypeptidase E (CPE) is a novel regulator of the can

153 two basic residues in the sorting receptor, carboxypeptidase E (CPE).

154 y structure of BDNF and the sorting receptor carboxypeptidase E directs this neurotrophin to the regu

155 g by regulating cap-dependent translation of carboxypeptidase E in a 4EBP2/eIF4E-dependent manner.

156 ignificant suppression of mRNA abundance for carboxypeptidase E, 14-3-3 protein and phosphoprotein en

157 ation enzymes, prohormone convertases (PCs), carboxypeptidase E, and peptidyl alpha-amidating enzyme,

158 phic factor-alpha1 (NF-alpha1; also known as carboxypeptidase E, CPE), concomitant with enhanced fibr

159 ay: a cohort of pancreatic enzymes (trypsin, carboxypeptidase, elastase, and others) not previously r

160 an deacetylase encoded by pgdA, the putative carboxypeptidase encoded by pbpX, the orphan response re

161 ty, but rather through targeting the tubulin carboxypeptidase enzyme onto specific MTs.

162 All cytosolic carboxypeptidases exhibit a monoglutamase activity when

163 lude five members that are similar to serine carboxypeptidases from a variety of organisms, including

164 e results suggest that specific reduction of carboxypeptidase function of gamma-secretase leads to th

165 at all result in drastic reduction of normal carboxypeptidase function.

166 re, we describe a bacterial protein effector-carboxypeptidase G2 (CPG2) reporter system for fluoresce

167 rus to deliver the prodrug-activating enzyme carboxypeptidase G2 (CPG2) to tumors in a single systemi

168 r the gene for the prodrug-activating enzyme carboxypeptidase G2 (CPG2) to tumors.

169 formed by the action of the bacterial enzyme carboxypeptidase G2 (CPG2).

170 (NSAR), and the member of the M20 peptidase/carboxypeptidase G2 family is N-succinyl-L-amino acid hy

171 acceptor, and a member of the M20 peptidase/carboxypeptidase G2 family.

172 PSMA acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, i

173 Only four of six mammalian cytosolic carboxypeptidases had been enzymatically characterized.

174 s in schizophrenia and to quantify glutamate carboxypeptidase II (GCP II) in order to explore a role

175 Two representative glutamate carboxypeptidase II (GCP II) inhibitors, 2-(hydroxypenta

176 The expression of glutamate carboxypeptidase II (GCP II) is reduced in selective bra

177 However, the catalytic enzyme glutamate carboxypeptidase II (GCP II) rapidly hydrolyzes NAAG int

178 ter NAAG hydrolysis with exogenous glutamate carboxypeptidase II (GCP II) using high-performance liqu

179 The NAAG hydrolyzing enzyme, glutamate carboxypeptidase II (GCP II), activity was normal in the

180 ted for their abilities to inhibit glutamate carboxypeptidase II (GCP II).

181 ude transferrin receptor 2 (TfR2), glutamate carboxypeptidase II (GCP2 or PSMA), N-acetylated alpha-l

182 Glutamate carboxypeptidase II (GCPII) encodes for intestinal folat

183 Inhibition of glutamate carboxypeptidase II (GCPII) has been shown to be neuropr

184 d, low molecular weight ligands of glutamate carboxypeptidase II (GCPII) have demonstrated efficacy i

185 The neuropeptidase glutamate carboxypeptidase II (GCPII) hydrolyzes N-acetyl-L-aspart

186 A series of thiol-based glutamate carboxypeptidase II (GCPII) inhibitors have been synthes

187 olactones derived from thiol-based glutamate carboxypeptidase II (GCPII) inhibitors were evaluated as

188 We then evaluated glutamate carboxypeptidase II (GCPII) inhibitors, known to increas

189 Glutamate carboxypeptidase II (GCPII) is an exopeptidase that cata

190 Inhibition of glutamate carboxypeptidase II (GCPII) is effective in preclinical

191 Human glutamate carboxypeptidase II (GCPII) is involved in neuronal sign

192 glutamate by the catalytic enzyme glutamate carboxypeptidase II (GCPII) reducing presynaptic inhibit

193 Because glutamate carboxypeptidase II (GCPII) regulates both folate absorp

194 active site as well as exosites of glutamate carboxypeptidase II (GCPII), a prostate cancer marker, p

195 duced folate carrier 1 (RFC1), and glutamate carboxypeptidase II (GCPII).

196 ke 2 (NAALADL2) is a member of the glutamate carboxypeptidase II family, best characterized by prosta

197 , 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has demonstrated robust neurop

198 lytic mechanism similar to that of glutamate carboxypeptidase II yet distinct substrate specificity.

199 ALADL1 gene, is a close homolog of glutamate carboxypeptidase II, a metallopeptidase that has been in

200 Inhibitors of glutamate carboxypeptidase II, an enzyme that inactivates NAAG fol

201 The Arabidopsis BRS1 gene encodes a serine carboxypeptidase II-like protein.

202 ent hydroxamate-based inhibitor of glutamate carboxypeptidase II.

203 than its closest human homologue, glutamate carboxypeptidase III (GCPIII).

204 isolated cDNAs for two extracellular serine carboxypeptidase III genes from tobacco (Nicotiana tabac

205 r, these results identify REP34 as an active carboxypeptidase, implicate the enzyme as a potential ke

206 e for the long sought-after tubulin tyrosine carboxypeptidase important in the regulation of microtub

207 The distribution of PBP5, the major D,D-carboxypeptidase in Escherichia coli, was mapped by immu

208 port for a role of an extracellular type III carboxypeptidase in the control of cell elongation.

209 g protein 6 (PBP6) is one of the two main DD-carboxypeptidases in Escherichia coli, which are implica

210 her than with low-molecular-weight endo- and carboxypeptidases, indicating that MreC might act as a s

211 mor inhibition was not through its canonical carboxypeptidase inhibitor activity.

212 esenchymal phenotype, and is a transmembrane carboxypeptidase inhibitor that interacts with ATP/GTP b

213 splayed by the C-terminal tails of different carboxypeptidase inhibitors represents a relevant exampl

214 B (spd_0549), which we showed encodes an L,D-carboxypeptidase involved in PG maturation.

215 ProTides showing diminished carboxypeptidase lability translated to poor anti-HIV ag

216 In contrast, three genes encoding serine carboxypeptidase-like (SCPL) acyltransferases [SCPL5, SC

217 nome encodes 51 proteins annotated as serine carboxypeptidase-like (SCPL) enzymes.

218 Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided int

219 r the same conditions, the endopeptidase and carboxypeptidase-like activities of the four gamma-secre

220 a40 by hk14, the light-chain antibody having carboxypeptidase-like activity, alters aggregation of Ab

221 ontrast, the APH1 subunit mainly affects the carboxypeptidase-like activity, with APH1B complexes fav

222 h alpha-secretase-like activity and one with carboxypeptidase-like activity.

223 difying cytochrome P450 SAD2, and the serine carboxypeptidase-like acyl transferase SAD7), which form

224 Aortic carboxypeptidase-like protein (ACLP) is an extracellular

225 In this study, we demonstrate that aortic carboxypeptidase-like protein (ACLP), a collagen-associa

226 r as well as the CArG box-independent aortic carboxypeptidase-like protein promoter.

227 richia coli is a membrane-bound cell wall dd-carboxypeptidase, localized in the outer leaflet of the

228 4 and 5), a Chymotrypsin (LuloChym1A) and a carboxypeptidase (LuloCpepA1), among others.

229 owed that the protein-protein interaction of carboxypeptidase M (CPM) and kinin B1 receptor (B1R) enh

230 Carboxypeptidase M (CPM) is a membrane protein potential

231 receptor (B1R) heterodimerizes with membrane carboxypeptidase M (CPM), facilitating receptor signalin

232 A carboxypeptidase-mediated hydrolysis study was performed

233 We tested this idea in E. coli by using a DD-carboxypeptidase mutant that accumulates pentapeptides i

234 Notably, dacB mutants, similar to dacA (D,D-carboxypeptidase) mutants, exhibited defects in cell sha

235 We discovered that plasma carboxypeptidase N (CPN) and B (CPB or activated thrombi

236 Carboxypeptidase N (CPN) is a plasma zinc metalloproteas

237 lysine from SDF-1alpha and identified it as carboxypeptidase N (CPN, also known as kininase I, argin

238 Carboxypeptidase N immediately digested 6 amino acids fr

239 ng enzyme (ACE), aminopeptidase P (APP), and carboxypeptidase N/M (CPN)] by means of logistic regress

240 e the enzymatic and structural properties of carboxypeptidase O (CPO), a previously uncharacterized a

241 antigen (PSMA) is a membrane-bound glutamate carboxypeptidase overexpressed in many forms of prostate

242 When the dd-carboxypeptidase PBP 5 was deleted, thereby producing ce

243 In addition, the combined loss of three DD-carboxypeptidases, PBPs 5 and 6 and DacD, also impaired

244 A PG dl-carboxypeptidase Pgp1 essential for maintenance of C. je

245 Prolyl carboxypeptidase (PRCP), a serine protease, is widely ex

246 y of peptidases exemplified by the glutamate carboxypeptidase PSMA.

247 tes from the canonical funnelin structure of carboxypeptidases, putatively resulting in a catalytic r

248 aromatic boronic acid inhibitors of the D,D-carboxypeptidase R39 from Actinomadura sp. strain.

249 chlamydial CPn0902, annotated as NlpD, is a carboxypeptidase, rather than an amidase activator, whic

250 of Escherichia coli is known to perform a dd-carboxypeptidase reaction on the bacterial peptidoglycan

251 dine, the residue found in prototypical zinc carboxypeptidases, resulted in decreased enzyme activity

252 a yeast biosynthetic membrane cargo protein, carboxypeptidase S (CPS), into the interior of an endoso

253 tein that modifies the yeast vacuolar enzyme carboxypeptidase S (Cps1), the polyphosphatase Ppn1/Phm5

254 orting of integral membrane proteins such as carboxypeptidase S (Cps1p) into the luminal vesicles of

255 eraries of cargo proteins that include yeast carboxypeptidase S, the epithelial sodium channel ENaC,

256 rowth sensitivities with functional screens (carboxypeptidase secretion and Alcian Blue binding) reve

257 it is unknown whether these three cytosolic carboxypeptidases share identical enzymatic properties a

258 ey uptake was dramatically decreased after a carboxypeptidase-specific peptide linker (Gly-Lys) had b

259 addition, to reduce excess kidney uptake, a carboxypeptidase-specific sequence Gly-Lys was incorpora

260 -alanine, 1, is a very specific and reactive carboxypeptidase substrate of the Streptomyces R61 dd-pe

261 s were determined using a panel of synthetic carboxypeptidase substrates, indicating a preference of

262 are acyltransferases rather than true serine carboxypeptidases suggests that some or all of the remai

263 anobacteria were identified as inhibitors of carboxypeptidase TAFIa.

264 The identity of the tubulin tyrosine carboxypeptidase (TCP) responsible for detyrosination ha

265 ichia coli is a well-characterized d-alanine carboxypeptidase that serves as a prototypical enzyme to

266 ivatable fibrinolysis inhibitor (TAFIa) is a carboxypeptidase that stabilizes fibrin clots by removin

267 talloenzymes within the larger M14 family of carboxypeptidases that have been implicated in the post-

268 onists of the B2R and must be processed by a carboxypeptidase to generate B1R agonists des-Arg(9)-bra

269 rulent PAI proteins (Fic; D-alanyl-D-alanine-carboxypeptidase; transposase) dated the divergence even

270 Carboxypeptidase treatment of either PS-2 or PS-3, subco

271 Surprisingly, carboxypeptidase treatment of PS-1 also inhibited 26 S p

272 ing groups and provides strong support for a carboxypeptidase-type mechanism for the hydrolysis of th

273 ncomycin resistance operons encode VanXY D,D-carboxypeptidase, which hydrolyzes both di- and pentapep

274 ific alterations in the balance of these two carboxypeptidases, which are involved in the control of

275 PSMA is a carboxypeptidase with two important enzymatic functions,

276 RAM1 (AMP1) is a member of the M28 family of carboxypeptidases with a pivotal role in plant developme

277 We suggest that digestive carboxypeptidases with sequence similarity to the classi

278 inaris, LcL) with the carbohydrate moiety of carboxypeptidase Y (CaY) was studied using both atomic f

279 In addition, sorting of carboxypeptidase Y (CPY) to the vacuole was delayed, and

280 hagy, whereas complex II is required for the carboxypeptidase Y (CPY)-to-vacuole pathway.

281 ERAD, we studied a new misfolded variant of carboxypeptidase Y (CPY).

282 can protect its s10 part against cleavage by carboxypeptidase Y (CPY).

283 d protein mimics zeolin or a mutated form of carboxypeptidase Y (CPY*) also induced autophagy in an I

284 In yeast, a mutant of carboxypeptidase Y (CPY*) was found to be a luminal ER s

285 Finally, using misfolded yeast carboxypeptidase Y and chicken ovalbumin as glycoprotein

286 o redirect the vacuolar destination of plant carboxypeptidase Y and other proteins in Arabidopsis sus

287 of linear peptides from the ERAD substrate, carboxypeptidase Y G255R (CPY*), and binds a model unfol

288 Most surprisingly, Och1p can use either the carboxypeptidase Y or AP-3 pathways to reach the vacuole

289 s and for proper protein sorting through the carboxypeptidase Y pathway.

290 ntial for endosome-to-Golgi retrieval of the carboxypeptidase Y receptor Vps10p.

291 ase experiments monitoring the maturation of carboxypeptidase Y reveal that oxidative folding is grea

292 HX20 affected protein sorting as measured by carboxypeptidase Y secretion in yeast mutants grown at a

293 whole Arabidopsis seedlings also resulted in carboxypeptidase Y secretion, indicating that the drug h

294 for the ERAD of CPY* (a misfolded version of carboxypeptidase Y that has five disulfide bonds).

295 ogy and defects related to the maturation of carboxypeptidase Y that is not dependent on the catalyti

296 ent alpha-factor maturation and transport of carboxypeptidase Y to the vacuole.

297 anisms; overexpressing VipA has an effect on carboxypeptidase Y trafficking, whereas VipD interferes

298 e in yeast causes defects in both growth and carboxypeptidase Y trafficking/processing.

299 aturation of isomerase-requiring substrates (carboxypeptidase Y) is impaired.

300 ell wall assembly, and delayed maturation of carboxypeptidase Y.