Alaninska aminopeptidaza

Alaninska aminopeptidaza
Identifikatori
EC broj 3.4.11.2
CAS broj 9054-63-1
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
PMC articles
PubMed articles
NCBI Protein search
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Alaninska aminopeptidaza‎
Dostupne strukture
4FYQ, 4FYR, 4FYS, 4FYT
Identifikatori
SimboliANPEP; APN; CD13; GP150; LAP1; P150; PEPN
Vanjski IDOMIM: 151530 MGI: 96749 HomoloGene: 68163 GeneCards: ANPEP Gene
EC broj3.4.11.2
Ontologija gena
Molekularna funkcija aktivnost aminopeptidaze
receptorska aktivnost
aktivnost metalopeptidaze
vezivanje jona cinka
vezivanje peptida
Celularna komponenta intermedijarni kompartman Goldžijevog endoplazmatični retikuluma
citozol
integralno sa ćelijskom membranom
spoljašnja strana membrane
Biološki proces angiogeneza
proteoliza
metabolički proces ćelijskih aromatičnih jedinjenja
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez29016790
EnsemblENSG00000166825ENSMUSG00000039062
UniProtP15144P97449
RefSeq (mRNA)NM_001150.2NM_008486.2
RefSeq (protein)NP_001141.2NP_032512.2
Lokacija (UCSC)Chr 15:
90.33 - 90.36 Mb
Chr 7:
79.82 - 79.85 Mb
PubMed pretraga[1][2]

Alaninska aminopeptidaza (EC 3.4.11.2) je enzim koji se koristi kao biomarker za detekciju oštećenja bubrega. On se može koristiti u dijagnozi pojedinih tipova bubrežnih poremećaja. Ona je prisutna u visokim nivoima u urinu, kad postoji problem sa bubrezima.

Aminopeptidaza N je locirana u malim crevima i renalnoj mikrovilarnoj membrani, kao i drugim ćelijskim membranama. U tankim crevima aminopeptidaza N učestvuje u finalnom stupnju varenja peptida generisanih hidrolizom proteina gastričnim i pankreatičkim proteazama. Njena funkcija u epitelu i drugim tipovima ćelija nije potpuno razjašnjena. Veliki ekstracelularni karboksiterminalni domen sadrži pentapeptidnu konsenzus sekvencu koja je karakteristična za članove zink-vezujuće metaloproteinazne superfamilije. Poređenjem sekvence sa poznatim enzimima ove klase je pokazalo da su CD13 i aminopeptidaza N identični.[1]

Reference

  1. „Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)”. 

Literatura

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 
  • Yeager CL, Ashmun RA, Williams RK, et al. (1992). „Human aminopeptidase N is a receptor for human coronavirus 229E”. Nature 357 (6377): 420–2. DOI:10.1038/357420a0. PMID 1350662. 
  • Shapiro LH, Ashmun RA, Roberts WM, Look AT (1991). „Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells”. J. Biol. Chem. 266 (18): 11999–2007. PMID 1675638. 
  • O'Connell PJ, Gerkis V, d'Apice AJ (1991). „Variable O-glycosylation of CD13 (aminopeptidase N)”. J. Biol. Chem. 266 (7): 4593–7. PMID 1705556. 
  • Watt VM, Willard HF (1990). „The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis”. Hum. Genet. 85 (6): 651–4. DOI:10.1007/BF00193592. PMID 1977688. 
  • Look AT, Peiper SC, Rebentisch MB, et al. (1986). „Molecular cloning, expression, and chromosomal localization of the gene encoding a human myeloid membrane antigen (gp150)”. J. Clin. Invest. 78 (4): 914–21. DOI:10.1172/JCI112680. PMC 423717. PMID 2428842. 
  • Look AT, Ashmun RA, Shapiro LH, Peiper SC (1989). „Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N”. J. Clin. Invest. 83 (4): 1299–307. DOI:10.1172/JCI114015. PMC 303821. PMID 2564851. 
  • Olsen J, Cowell GM, Kønigshøfer E, et al. (1988). „Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA”. FEBS Lett. 238 (2): 307–14. DOI:10.1016/0014-5793(88)80502-7. PMID 2901990. 
  • Kruse TA, Bolund L, Grzeschik KH, et al. (1988). „Assignment of the human aminopeptidase N (peptidase E) gene to chromosome 15q13-qter”. FEBS Lett. 239 (2): 305–8. DOI:10.1016/0014-5793(88)80940-2. PMID 2903074. 
  • Tokioka-Terao M, Hiwada K, Kokubu T (1985). „Purification and characterization of aminopeptidase N from human plasma”. Enzyme 32 (2): 65–75. PMID 6149934. 
  • Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y (1995). „Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N”. Biol. Chem. Hoppe-Seyler 376 (7): 397–400. DOI:10.1515/bchm3.1995.376.7.397. PMID 7576235. 
  • Favaloro EJ, Browning T, Facey D (1993). „CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated”. Exp. Hematol. 21 (13): 1695–701. PMID 7902291. 
  • Núñez L, Amigo L, Rigotti A, et al. (1993). „Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids”. FEBS Lett. 329 (1-2): 84–8. DOI:10.1016/0014-5793(93)80199-5. PMID 8102610. 
  • Söderberg C, Giugni TD, Zaia JA, et al. (1993). „CD13 (human aminopeptidase N) mediates human cytomegalovirus infection”. J. Virol. 67 (11): 6576–85. PMC 238095. PMID 8105105. 
  • Kolb AF, Maile J, Heister A, Siddell SG (1996). „Characterization of functional domains in the human coronavirus HCV 229E receptor”. J. Gen. Virol.. 77 ( Pt 10): 2515–21. PMID 8887485. 
  • Norén K, Hansen GH, Clausen H, et al. (1997). „Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity”. Exp. Cell Res. 231 (1): 112–8. DOI:10.1006/excr.1996.3455. PMID 9056417. 
  • Kolb AF, Hegyi A, Siddell SG (1997). „Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N”. J. Gen. Virol.. 78 ( Pt 11): 2795–802. PMID 9367365. 
  • Hegyi A, Kolb AF (1998). „Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N”. J. Gen. Virol.. 79 ( Pt 6): 1387–91. PMID 9634079. 
  • Dong X, An B, Salvucci Kierstead L, et al. (2000). „Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells”. J. Immunol. 164 (1): 129–35. PMID 10605003. 
  • Pasqualini R, Koivunen E, Kain R, et al. (2000). „Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis”. Cancer Res. 60 (3): 722–7. PMID 10676659. 
  • Renold A, Cescato R, Beuret N, et al. (2000). „Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface”. J. Biol. Chem. 275 (13): 9290–5. DOI:10.1074/jbc.275.13.9290. PMID 10734069. 

Vanjske veze

  • The MEROPS online database for peptidases and their inhibitors Arhivirano 2019-09-25 na Wayback Machine-u
  • MeSH CD13+Antigens
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1-50
CD1 (a-c, 1A, 1D, 1E) • CD2 • CD3 (γ, δ, ε) • CD4 • CD5 • CD6 • CD7 • CD8 (a) • CD9 • CD10 • CD11 (a, b, c) • CD13 • CD14 • CD15 • CD16 (A, B) • CD18 • CD19 • CD20 • CD21 • CD22 • CD23 • CD24 • CD25 • CD26 • CD27 • CD28 • CD29 • CD30 • CD31 • CD32 (A, B) • CD33 • CD34 • CD35 • CD36 • CD37 • CD38 • CD39 • CD40 • CD41 • CD42 (a, b, c, d) • CD43 • CD44 • CD45 • CD46 • CD47 • CD48 • CD49 (a, b, c, d, e, f) • CD50
51-100
CD51 • CD52 • CD53 • CD54 • CD55 • CD56 • CD57 • CD58 • CD59 • CD61 • CD62 (E, L, P) • CD63 • CD64 (A, B, C) • CD66 (a, b, c, d, e, f) • CD68 • CD69 • CD70 • CD71 • CD72 • CD73 • CD74 • CD78 • CD79 (a, b) • CD80 • CD81 • CD82 • CD83 • CD84 • CD85 (a, d, e, h, j, k) • CD86 • CD87 • CD88 • CD89 • CD90 • CD91- CD92 • CD93 • CD94 • CD95 • CD96 • CD97 • CD98 • CD99 • CD100
101-150
CD101 • CD102 • CD103 • CD104 • CD105 • CD106 • CD107 (a, b) • CD108 • CD109 • CD110 • CD111 • CD112 • CD113 • CD114 • CD115 • CD116 • CD117 • CD118 • CD119 • CD120 (a, b) • CD121 (a, b) • CD122 • CD123 • CD124 • CD125 • CD126 • CD127 • CD129 • CD130 • CD131 • CD132 • CD133 • CD134 • CD135 • CD136 • CD137 • CD138 • CD140b • CD141 • CD142 • CD143 • CD144 • CD146 • CD147 • CD148 • CD150
151-200
CD151 • CD152 • CD153 • CD154 • CD155 • CD156 (a, b, c) • CD157 • CD158 (a, d, e, i, k) • CD159 (a, c) • CD160 • CD161 • CD162 • CD163 • CD164 • CD166 • CD167 (a, b) • CD168 • CD169 • CD170 • CD171 • CD172 (a, b, g) • CD174 • CD177 • CD178 • CD179 (a, b) • CD181 • CD182 • CD183 • CD184 • CD185 • CD186 • CD191 • CD192 • CD193 • CD194 • CD195 • CD196 • CD197 • CDw198 • CDw199 • CD200
201-250
CD201 • CD202b • CD204 • CD205 • CD206 • CD207 • CD208 • CD209 • CDw210 (a, b) • CD212 • CD213a (1, 2) • CD217 • CD218 (a, b) • CD220 • CD221 • CD222 • CD223 • CD224 • CD225 • CD226 • CD227 • CD228 • CD229 • CD230 • CD233 • CD234 • CD235 (a, b) • CD236 • CD238 • CD239 • CD240CE • CD241 • CD243 • CD244 • CD246 • CD247- CD248 • CD249
251-300
CD252 • CD253 • CD254 • CD256 • CD257 • CD258 • CD261 • CD262 • CD264 • CD265 • CD266 • CD267 • CD268 • CD269 • CD271 • CD272 • CD273 • CD274 • CD275 • CD276 • CD278 • CD279 • CD280 • CD281 • CD282 • CD283 • CD284 • CD286 • CD288 • CD289 • CD290 • CD292 • CDw293 • CD294 • CD295 • CD297 • CD298 • CD299
301-350
CD300A • CD301 • CD302 • CD303 • CD304 • CD305 • CD306 • CD307 • CD309 • CD312 • CD314 • CD315 • CD316 • CD317 • CD318 • CD320 • CD321 • CD322 • CD324 • CD325 • CD326 • CD328 • CD329 • CD331 • CD332 • CD333 • CD334 • CD335 • CD336 • CD337 • CD338 • CD339 • CD340 • CD344 • CD349 • CD350
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3.4.11-19: Eksopeptidaza
3.4.11
Aminopeptidaza (Alanin, Arginil, Aspartil, Cistinil, Leucil, Glutamil, Metionil (1, 2), O)
3.4.13
Dipeptidaza (1, 2, 3)
3.4.14
Dipeptidil peptidaza (Katepsin C, Dipeptidil peptidaza-4)  Tripeptidil peptidaza (Tripeptidil peptidaza I, Tripeptidil peptidaza II)
3.4.15
3.4.16
Karboksipeptidaze serinskog tipa: Katepsin A  DD-transpeptidaza
3.4.17
Metalokarboksipeptidaze: Karboksipeptidaza (A, A2, B, C, E, Glutamat II)
Drugi/negrupisni
Metaloeksopeptidaza
3.4.21-24: Endopeptidaza
Serinske peptidaze  Cisteinska proteaza  Aspartatna proteaza  Metaloendopeptidaze
Druge/negrupisane: Sekretaza amiloidnog prekursornog proteina (Alfa-sekretaza, Beta-sekretaza 1, Beta-sekretaza 2, Gama sekretaza)
3.4.99: Nepoznato
Stafilokinaza
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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Teme
Tipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6