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词条 DNPEP
释义

  1. Function

  2. Model organisms

  3. References

  4. Further reading

  5. External links

{{Infobox_gene}}Aspartyl aminopeptidase is an enzyme that in humans is encoded by the DNPEP gene.[1][2]

Function

The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins.[2]

Model organisms

Model organisms have been used in the study of DNPEP function. A conditional knockout mouse line called Dnpeptm1e(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute.[3] Male and female animals underwent a standardized phenotypic screen[4] to determine the effects of deletion.[5][6][7][8] Additional screens performed: - In-depth immunological phenotyping[9]{{clear|left}}

References

1. ^{{cite journal | vauthors = Wilk S, Wilk E, Magnusson RP | title = Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase | journal = The Journal of Biological Chemistry | volume = 273 | issue = 26 | pages = 15961–70 | date = Jun 1998 | pmid = 9632644 | pmc = | doi = 10.1074/jbc.273.26.15961 }}
2. ^{{cite web | title = Entrez Gene: DNPEP aspartyl aminopeptidase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23549| accessdate = }}
3. ^{{cite journal |title=The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice |author=Gerdin AK |year=2010 |journal=Acta Ophthalmologica|volume=88 |pages=925–7|doi=10.1111/j.1755-3768.2010.4142.x }}
4. ^{{cite web |url=http://www.mousephenotype.org/data/search?q=Dnpep#fq=**&facet=gene |title=International Mouse Phenotyping Consortium}}
5. ^{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}
6. ^{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}
7. ^{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}
8. ^{{cite journal | vauthors = White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP | title = Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes | journal = Cell | volume = 154 | issue = 2 | pages = 452–64 | date = Jul 2013 | pmid = 23870131 | pmc = 3717207 | doi = 10.1016/j.cell.2013.06.022 }}
9. ^{{cite web |url= http://www.immunophenotyping.org/data/search?keys=Dnpep&field_gene_construct_tid=All |title=Infection and Immunity Immunophenotyping (3i) Consortium}}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
  • {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M |authorlink30=Huda Zoghbi| title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
  • {{cite journal | vauthors = Prieto I, Hermoso F, de Gasparo M, Vargas F, Alba F, Segarra AB, Banegas I, Ramírez M | title = Angiotensinase activities in the kidney of renovascular hypertensive rats | journal = Peptides | volume = 24 | issue = 5 | pages = 755–60 | date = May 2003 | pmid = 12895663 | doi = 10.1016/S0196-9781(03)00121-9 | citeseerx = 10.1.1.379.1582 }}
  • {{cite journal | vauthors = Wilk S, Wilk E, Magnusson RP | title = Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase | journal = Archives of Biochemistry and Biophysics | volume = 407 | issue = 2 | pages = 176–83 | date = Nov 2002 | pmid = 12413488 | doi = 10.1016/S0003-9861(02)00494-0 }}
{{refend}}

External links

  • The MEROPS online database for peptidases and their inhibitors: M18.002
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1 : EC 3.4.11

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