Alanine aminopeptidase

An Error has occurred retrieving Wikidata item for infobox Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene.

Function

Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.^[1] AAP is also used by some viruses as a receptor to which these viruses bind to and then enter cells. It is a receptor for human coronavirus 229E, feline coronavirus serotype II (FCoV-II), TGEV, PEDV,^[2] canine coronavirus genotype II (CCoV-II)^[3] as well as several Deltacoronaviruses.^[4]

References

↑ "Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)".
↑ Jaimes JA, Millet JK, Stout AE, André NM, Whittaker GR (January 2020). "A Tale of Two Viruses: The Distinct Spike Glycoproteins of Feline Coronaviruses". Viruses. 12 (1): 83. doi:10.3390/v12010083. PMC 7019228. PMID 31936749.
↑ Licitra BN, Whittaker GR, Dubovi EJ, Duhamel GE (December 2014). "Genotypic characterization of canine coronaviruses associated with fatal canine neonatal enteritis in the United States". Journal of Clinical Microbiology. 52 (12): 4230–4238. doi:10.1128/JCM.02158-14. PMC 4313292. PMID 25253797.
↑ Liang QZ, Wang B, Ji CM, Hu F, Qin P, Feng Y, et al. (February 2023). "Chicken or Porcine Aminopeptidase N Mediates Cellular Entry of Pseudoviruses Carrying Spike Glycoprotein from the Avian Deltacoronaviruses HKU11, HKU13, and HKU17". Journal of Virology. 97 (2): e0194722. doi:10.1128/jvi.01947-22. PMC 9973037. PMID 36656013.

Yeager CL, Ashmun RA, Williams RK, Cardellichio CB, Shapiro LH, Look AT, et al. (June 1992). "Human aminopeptidase N is a receptor for human coronavirus 229E". Nature. 357 (6377): 420–422. Bibcode:1992Natur.357..420Y. doi:10.1038/357420a0. PMC 7095410. PMID 1350662.
Shapiro LH, Ashmun RA, Roberts WM, Look AT (June 1991). "Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells". The Journal of Biological Chemistry. 266 (18): 11999–12007. doi:10.1016/S0021-9258(18)99056-3. PMID 1675638.
O'Connell PJ, Gerkis V, d'Apice AJ (March 1991). "Variable O-glycosylation of CD13 (aminopeptidase N)". The Journal of Biological Chemistry. 266 (7): 4593–4597. doi:10.1016/S0021-9258(20)64364-2. PMID 1705556.
Watt VM, Willard HF (October 1990). "The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis". Human Genetics. 85 (6): 651–654. doi:10.1007/BF00193592. PMID 1977688. S2CID 19678944.
Look AT, Peiper SC, Rebentisch MB, Ashmun RA, Roussel MF, Lemons RS, et al. (October 1986). "Molecular cloning, expression, and chromosomal localization of the gene encoding a human myeloid membrane antigen (gp150)". The Journal of Clinical Investigation. 78 (4): 914–921. doi:10.1172/JCI112680. PMC 423717. PMID 2428842.
Look AT, Ashmun RA, Shapiro LH, Peiper SC (April 1989). "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N". The Journal of Clinical Investigation. 83 (4): 1299–1307. doi:10.1172/JCI114015. PMC 303821. PMID 2564851.
Olsen J, Cowell GM, Kønigshøfer E, Danielsen EM, Møller J, Laustsen L, et al. (October 1988). "Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA". FEBS Letters. 238 (2): 307–314. Bibcode:1988FEBSL.238..307O. doi:10.1016/0014-5793(88)80502-7. PMID 2901990.
Kruse TA, Bolund L, Grzeschik KH, Ropers HH, Olsen J, Sjöström H, et al. (November 1988). "Assignment of the human aminopeptidase N (peptidase E) gene to chromosome 15q13-qter". FEBS Letters. 239 (2): 305–308. Bibcode:1988FEBSL.239..305K. 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. doi:10.1159/000469453. PMID 6149934.
Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y (July 1995). "Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N". Biological Chemistry Hoppe-Seyler. 376 (7): 397–400. doi:10.1515/bchm3.1995.376.7.397. PMID 7576235.
Favaloro EJ, Browning T, Facey D (December 1993). "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated". Experimental Hematology. 21 (13): 1695–1701. PMID 7902291.
Núñez L, Amigo L, Rigotti A, Puglielli L, Mingrone G, Greco AV, et al. (August 1993). "Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids". FEBS Letters. 329 (1–2): 84–88. Bibcode:1993FEBSL.329...84N. doi:10.1016/0014-5793(93)80199-5. PMID 8102610. S2CID 23782523.
Söderberg C, Giugni TD, Zaia JA, Larsson S, Wahlberg JM, Möller E (November 1993). "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection". Journal of Virology. 67 (11): 6576–6585. doi:10.1128/JVI.67.11.6576-6585.1993. PMC 238095. PMID 8105105.
Kolb AF, Maile J, Heister A, Siddell SG (October 1996). "Characterization of functional domains in the human coronavirus HCV 229E receptor". The Journal of General Virology. 77 (10): 2515–2521. doi:10.1099/0022-1317-77-10-2515. PMID 8887485.
Norén K, Hansen GH, Clausen H, Norén O, Sjöström H, Vogel LK (February 1997). "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity". Experimental Cell Research. 231 (1): 112–118. doi:10.1006/excr.1996.3455. PMID 9056417.
Kolb AF, Hegyi A, Siddell SG (November 1997). "Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N". The Journal of General Virology. 78 (11): 2795–2802. doi:10.1099/0022-1317-78-11-2795. PMID 9367365.
Hegyi A, Kolb AF (June 1998). "Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N". The Journal of General Virology. 79 (6): 1387–1391. doi:10.1099/0022-1317-79-6-1387. PMID 9634079.
Dong X, An B, Salvucci Kierstead L, Storkus WJ, Amoscato AA, Salter RD (January 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". Journal of Immunology. 164 (1): 129–135. doi:10.4049/jimmunol.164.1.129. PMID 10605003.
Pasqualini R, Koivunen E, Kain R, Lahdenranta J, Sakamoto M, Stryhn A, et al. (February 2000). "Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis". Cancer Research. 60 (3): 722–727. PMC 4469333. PMID 10676659.
Renold A, Cescato R, Beuret N, Vogel LK, Wahlberg JM, Brown JL, et al. (March 2000). "Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface". The Journal of Biological Chemistry. 275 (13): 9290–9295. doi:10.1074/jbc.275.13.9290. PMID 10734069.

External links

The MEROPS online database for peptidases and their inhibitors: M01.001 Archived 2019-09-25 at the Wayback Machine
CD13+Antigens at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Human ANPEP genome location and ANPEP gene details page in the UCSC Genome Browser.

Stub icon

This hydrolase article is a stub. You can help Wikipedia by expanding it.

[entrez-1] "Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)".

[2] Jaimes JA, Millet JK, Stout AE, André NM, Whittaker GR (January 2020). "A Tale of Two Viruses: The Distinct Spike Glycoproteins of Feline Coronaviruses". Viruses. 12 (1): 83. doi:10.3390/v12010083. PMC 7019228. PMID 31936749.

[3] Licitra BN, Whittaker GR, Dubovi EJ, Duhamel GE (December 2014). "Genotypic characterization of canine coronaviruses associated with fatal canine neonatal enteritis in the United States". Journal of Clinical Microbiology. 52 (12): 4230–4238. doi:10.1128/JCM.02158-14. PMC 4313292. PMID 25253797.

[4] Liang QZ, Wang B, Ji CM, Hu F, Qin P, Feng Y, et al. (February 2023). "Chicken or Porcine Aminopeptidase N Mediates Cellular Entry of Pseudoviruses Carrying Spike Glycoprotein from the Avian Deltacoronaviruses HKU11, HKU13, and HKU17". Journal of Virology. 97 (2): e0194722. doi:10.1128/jvi.01947-22. PMC 9973037. PMID 36656013.

[1]

[2]

[3]

[4]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d 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 CD180 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 CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 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 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Alanine aminopeptidase

Contents

Function

References

Further reading

External links

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

In other projects

In other languages