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

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

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

6 minal processing may occur via a progressive carboxypeptidase.

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

8 rminal lysine residues of the heavy chain by carboxypeptidase.

9 d stems in mature peptidoglycan by an active carboxypeptidase.

10 inding the SARS-CoV-2 spike protein and as a carboxypeptidase.

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

12 within a novel family of mammalian cytosolic carboxypeptidases.

13 er of proteins, including the M14B subfamily carboxypeptidases.

14 d di-peptidylpeptidases, aminopeptidases and carboxypeptidases.

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

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

17 partoacylase is closely analogous to that of carboxypeptidases.

18 ic activities, including aminopeptidases and 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 uding Charcot-Leyden crystal galectin [CLC]; carboxypeptidase 3 [CPA3]; deoxyribonuclease 1-like 3 [D

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

24 ee selected candidates in complex with human carboxypeptidase A (CPA)1, allowed to decipher the struc

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

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

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

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

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

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

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

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

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

34 Last but not least, proteases, such as carboxypeptidase A, released by FcepsilonRI-activated MC

35 el of aspartoacylase based on zinc dependent carboxypeptidase A.

36 ical zinc hydrolases such as thermolysin and carboxypeptidase A.

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

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

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

40 se in Krt19 and a reduction in acinar genes (Carboxypeptidase A1, Amylase2a) on day 4 of the transdif

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

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

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

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

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

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

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

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

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

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

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

52 Tryptase and carboxypeptidase A3 expression in epithelial brushings a

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

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

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

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

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

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

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

60 ex-specific strata, while three other genes [carboxypeptidase A4 (CPA4), growth factor receptor bound

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

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

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

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

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

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

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

68 ases/esterases, GDSL lipases, proteases, Ser carboxypeptidases, ABHD protein, pectin acetylesterase,

69 The carboxypeptidase ACE2 is a homologue of angiotensin-conv

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

71 As a carboxypeptidase, ACE2 cleaves many biological substrate

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

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

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

75 reveals cell wall D,D-endopeptidase and D,D-carboxypeptidase activities.

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

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

78 iously, here we report the first instance of carboxypeptidase activity in a POP family member.

79 the POP family and confirmed the presence of carboxypeptidase activity in one of them.

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

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

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

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

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

85 PSMA's carboxypeptidase activity releases glutamate from vitami

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

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

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

89 erved structural adaptations that enable its carboxypeptidase activity, with a unique loop and two ar

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

91 In Arabidopsis, loss of the carboxypeptidase ALTERED MERISTEM PROGRAM1 (AMP1) produc

92 We determined the crystal structures of this carboxypeptidase, an S9C subfamily member from Deinococc

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

108 thase, papain-like cysteine protease, serine carboxypeptidase, and lipoxygenase2 were upregulated at

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

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

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

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

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

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

115 Carboxypeptidase B treatment decreased cell-dependent pl

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

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

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

119 Carboxypeptidase B-sensitive plasminogen binding sites p

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

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

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

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

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

125 thrombin-activatable fibrinolysis inhibitor (carboxypeptidase B2) activation in vitro, which may cont

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

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

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

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

130 In the heart, the serine carboxypeptidase cathepsin A (CatA) is distributed betwe

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

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

133 bules can be deglutamylated by the cytosolic carboxypeptidase CCP1.

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

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

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

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

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

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

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

141 agmentation and mistargeting of the vacuolar carboxypeptidase CPY/Prc1, resulting in an extracellular

142 Carboxypeptidase D (CPD) functions in the processing of

143 therapeutic targets were identified, such as carboxypeptidase D (CPD).

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

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

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

147 Carboxypeptidase D expression correlates with patient ou

148 Notably, we found that carboxypeptidase D is responsible for removal of a C-ter

149 es in patients with lung cancer, and loss of carboxypeptidase D reduced tumour growth.

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

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

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

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

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

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

156 , and mature DCV cargoes such as insulin and carboxypeptidase E (CPE) accumulate near the trans-Golgi

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

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

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

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

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

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

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

164 Carboxypeptidase E (CPE), an exopeptidase involved in pr

165 ation initiation factor 4gamma1 (eIF4G1) and carboxypeptidase E (CPE)-dependent proinsulin processing

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

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

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

169 tic processing by prohormone convertases and carboxypeptidase E.

170 tion functions of novel N-terminal-truncated carboxypeptidase E/neurotrophic factor-alphal variants i

171 PRQ requires the function of the carboxypeptidase EGL-21 and the calcium-activated protei

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

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

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

175 All cytosolic carboxypeptidases exhibit a monoglutamase activity when

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

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

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

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

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

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

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

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

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

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

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

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

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

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

190 Glutamate carboxypeptidase II (GCPII) encodes for intestinal folat

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

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

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

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

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

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

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

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

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

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

201 Glutamate carboxypeptidase II (GCPII), coded by the gene folate hy

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

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

204 , 2-PMPA) is a potent inhibitor of glutamate carboxypeptidase II which has demonstrated robust neurop

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

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

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

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

209 ent hydroxamate-based inhibitor of glutamate carboxypeptidase II.

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

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

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

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

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

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

216 and VASH2-SVBP complexes function as tubulin carboxypeptidases in cardiomyocytes, with a predominant

217 VASH-SVBP complexes are active tubulin carboxypeptidases in cardiomyocytes.

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

219 CE2, PEP (prolyl-endopeptidase), PCP (prolyl-carboxypeptidase) in kidney biopsy homogenates in 11 hea

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

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

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

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

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

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

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

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

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

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

230 , all culminating in reduced gamma-secretase carboxypeptidase-like activity.

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

232 Aortic carboxypeptidase-like protein (ACLP) is a collagen-bindi

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

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

235 losteric pocket of domain IV that features a carboxypeptidase-like structural motif.

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

237 4 and 5), a Chymotrypsin (LuloChym1A) and a carboxypeptidase (LuloCpepA1), among others.

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

239 Carboxypeptidase M (CPM) is a membrane protein potential

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

241 A carboxypeptidase-mediated hydrolysis study was performed

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

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

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

245 Carboxypeptidase N (CPN) is a plasma zinc metalloproteas

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

247 Carboxypeptidase N immediately digested 6 amino acids fr

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

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

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

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

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

253 The DL-carboxypeptidase Pgp1 important for C. jejuni helical mo

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

255 y of peptidases exemplified by the glutamate carboxypeptidase PSMA.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

270 anobacteria were identified as inhibitors of carboxypeptidase TAFIa.

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

272 ostate-specific membrane antigen (PSMA) is a carboxypeptidase that is overexpressed in prostate cance

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

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

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

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

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

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

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

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

281 pulation of tubulin tyrosine ligase (TTL) or carboxypeptidase (Vasohibins-SVBP) activities to constit

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

299 cational glycosylation was also observed for carboxypeptidase Y-derived reporter proteins that contai

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