XPNPEP1: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (Bot: HTTP→HTTPS (v470))
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Xaa-Pro aminopeptidase 1''' is an [[enzyme]] that in humans is encoded by the ''XPNPEP1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7511| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = X-prolyl aminopeptidase (aminopeptidase P) 1, soluble
| HGNCid = 12822
| Symbol = XPNPEP1
| AltSymbols =; SAMP; XPNPEP; XPNPEPL; XPNPEPL1
| OMIM = 602443
| ECnumber = 
| Homologene = 6424
| MGIid = 2180003
| GeneAtlas_image1 = PBB_GE_XPNPEP1_208453_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_XPNPEP1_209045_at_tn.png
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0008235 |text = metalloexopeptidase activity}} {{GNF_GO|id=GO:0008451 |text = X-Pro aminopeptidase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7511
    | Hs_Ensembl = ENSG00000108039
    | Hs_RefseqProtein = NP_065116
    | Hs_RefseqmRNA = NM_020383
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 111614514
    | Hs_GenLoc_end = 111673259
    | Hs_Uniprot = Q9NQW7
    | Mm_EntrezGene = 170750
    | Mm_Ensembl = ENSMUSG00000025027
    | Mm_RefseqmRNA = NM_133216
    | Mm_RefseqProtein = NP_573479
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 53044495
    | Mm_GenLoc_end = 53091854
    | Mm_Uniprot = Q3TL27
  }}
}}
'''X-prolyl aminopeptidase (aminopeptidase P) 1, soluble''', also known as '''XPNPEP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7511| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
X-prolyl aminopeptidase (EC 3.4.11.9) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-prolyl aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and [[Tachykinin peptides|tachykinins]], as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. Deficiency of X-prolyl aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine (Blau et al., 1988).[supplied by OMIM]<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = X-prolyl aminopeptidase (EC 3.4.11.9) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-prolyl aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. Deficiency of X-prolyl aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine (Blau et al., 1988).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7511| accessdate = }}</ref>
}}


==References==
== Model organisms ==
{{reflist|2}}
 
==Further reading==
[[Model organism]]s have been used in the study of XPNPEP1 function. A conditional [[knockout mouse]] line called ''Xpnpep1<sup>tm1a(KOMP)Wtsi</sup>'' was generated at the [[Wellcome Trust Sanger Institute]].<ref name="mgp_reference">{{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 }}</ref> Male and female animals underwent a standardized [[phenotypic screen]]<ref name="IMPCsearch_ref">{{cite web |url=http://www.mousephenotype.org/data/search?q=Xpnpep1#fq=*:*&facet=gene |title=International Mouse Phenotyping Consortium}}</ref> to determine the effects of deletion.<ref name="pmid21677750">{{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 }}</ref><ref name="mouse_library">{{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 }}</ref><ref name="mouse_for_all_reasons">{{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 }}</ref><ref name="pmid23870131">{{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 }}</ref> Additional screens performed:  - In-depth immunological phenotyping<ref name="iii_ref">{{cite web |url= http://www.immunophenotyping.org/data/search?keys=Xpnpep1&field_gene_construct_tid=All |title=Infection and Immunity Immunophenotyping (3i) Consortium}}</ref> - in-depth bone and cartilage phenotyping<ref name="obcd_ref">{{cite web |url=http://www.boneandcartilage.com/ |title=OBCD Consortium}}</ref>
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: left;" |
|+ ''Xpnpep1'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| colspan=2; style="text-align: center;" | All data available at.<ref name="IMPCsearch_ref"/><ref name="iii_ref" /><ref name="obcd_ref"/>
 
|-
| Peripheral blood leukocytes 6 Weeks || bgcolor="#488ED3"|Normal
 
|-
| ''[[Haematology]]'' 6 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Insulin || bgcolor="#488ED3"|Normal
 
|-
| Homozygous viability at P14 || bgcolor="#C40000"|Abnormal
 
|-
| Homozygous Fertility || bgcolor="#488ED3"|Normal
 
|-
| Body weight || bgcolor="#C40000"|Abnormal
 
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
 
|-
| Grip strength || bgcolor="#488ED3"|Normal
 
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
 
|-
| [[Indirect calorimetry]] || bgcolor="#C40000"|Abnormal
 
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
 
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
 
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#C40000"|Abnormal
 
|-
| [[Radiography]] || bgcolor="#C40000"|Abnormal
 
|-
| Eye morphology || bgcolor="#488ED3"|Normal
 
|-
| [[Clinical chemistry]] || bgcolor="#C40000"|Abnormal
 
|-
| ''[[Haematology]]'' 16 Weeks || bgcolor="#488ED3"|Normal
 
|-
| Peripheral blood leukocytes 16 Weeks || bgcolor="#C40000"|Abnormal
 
|-
| Heart weight || bgcolor="#488ED3"|Normal
 
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal
 
|-
| Cytotoxic T Cell Function || bgcolor="#488ED3"|Normal
 
|-
| Spleen Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Mesenteric Lymph Node Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Bone Marrow Immunophenotyping || bgcolor="#488ED3"|Normal
 
|-
| Epidermal Immune Composition || bgcolor="#488ED3"|Normal
 
|-
|}
{{clear|left}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Vanhoof G, De Meester I, Goossens F, Hendriks D, Scharpé S, Yaron A | title = Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P | journal = Biochemical Pharmacology | volume = 44 | issue = 3 | pages = 479–87 | date = Aug 1992 | pmid = 1510698 | doi = 10.1016/0006-2952(92)90439-P }}
| citations =
* {{cite journal | vauthors = Blau N, Niederwieser A, Shmerling DH | title = Peptiduria presumably caused by aminopeptidase-P deficiency. A new inborn error of metabolism | journal = Journal of Inherited Metabolic Disease | volume = 11 Suppl 2 | issue =  | pages = 240–2 | year = 1988 | pmid = 3141711 | doi = 10.1007/BF01804246 }}
*{{cite journal | author=Vanhoof G, De Meester I, Goossens F, ''et al.'' |title=Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P. |journal=Biochem. Pharmacol. |volume=44 |issue= 3 |pages= 479-87 |year= 1992 |pmid= 1510698 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Blau N, Niederwieser A, Shmerling DH |title=Peptiduria presumably caused by aminopeptidase-P deficiency. A new inborn error of metabolism. |journal=J. Inherit. Metab. Dis. |volume=11 Suppl 2 |issue=  |pages= 240-2 |year= 1988 |pmid= 3141711 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Vanhoof G, Goossens F, Juliano MA, Juliano L, Hendriks D, Schatteman K, Lin AH, Scharpé S | title = Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P) | journal = Cytogenetics and Cell Genetics | volume = 78 | issue = 3-4 | pages = 275–80 | year = 1998 | pmid = 9465902 | doi = 10.1159/000134671 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Sprinkle TJ, Caldwell C, Ryan JW | title = Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with [[XPNPEP2]] | journal = Archives of Biochemistry and Biophysics | volume = 378 | issue = 1 | pages = 51–6 | date = Jun 2000 | pmid = 10871044 | doi = 10.1006/abbi.2000.1792 }}
*{{cite journal | author=Vanhoof G, Goossens F, Juliano MA, ''et al.'' |title=Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P). |journal=Cytogenet. Cell Genet. |volume=78 |issue= 3-4 |pages= 275-80 |year= 1998 |pmid= 9465902 |doi= }}
* {{cite journal | vauthors = Cottrell GS, Hooper NM, Turner AJ | title = Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme | journal = Biochemistry | volume = 39 | issue = 49 | pages = 15121–8 | date = Dec 2000 | pmid = 11106490 | doi = 10.1021/bi001585c }}
*{{cite journal | author=Sprinkle TJ, Caldwell C, Ryan JW |title=Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2. |journal=Arch. Biochem. Biophys. |volume=378 |issue= 1 |pages= 51-6 |year= 2000 |pmid= 10871044 |doi= 10.1006/abbi.2000.1792 }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nature Biotechnology | volume = 21 | issue = 5 | pages = 566–9 | date = May 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
*{{cite journal | author=Cottrell GS, Hooper NM, Turner AJ |title=Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme. |journal=Biochemistry |volume=39 |issue= 49 |pages= 15121-8 |year= 2001 |pmid= 11106490 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-10-stub}}

Latest revision as of 03:19, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Xaa-Pro aminopeptidase 1 is an enzyme that in humans is encoded by the XPNPEP1 gene.[1]

Function

X-prolyl aminopeptidase (EC 3.4.11.9) is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-prolyl aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. Deficiency of X-prolyl aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine (Blau et al., 1988).[supplied by OMIM][1]

Model organisms

Model organisms have been used in the study of XPNPEP1 function. A conditional knockout mouse line called Xpnpep1tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[2] Male and female animals underwent a standardized phenotypic screen[3] to determine the effects of deletion.[4][5][6][7] Additional screens performed: - In-depth immunological phenotyping[8] - in-depth bone and cartilage phenotyping[9]

References

  1. ↑ 1.0 1.1 "Entrez Gene: XPNPEP1 X-prolyl aminopeptidase (aminopeptidase P) 1, soluble".
  2. ↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  3. ↑ 3.0 3.1 "International Mouse Phenotyping Consortium".
  4. ↑ 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 (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  5. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  6. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  7. ↑ 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 (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  8. ↑ 8.0 8.1 "Infection and Immunity Immunophenotyping (3i) Consortium".
  9. ↑ 9.0 9.1 "OBCD Consortium".

Further reading

  • Vanhoof G, De Meester I, Goossens F, Hendriks D, Scharpé S, Yaron A (Aug 1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P". Biochemical Pharmacology. 44 (3): 479–87. doi:10.1016/0006-2952(92)90439-P. PMID 1510698.
  • Blau N, Niederwieser A, Shmerling DH (1988). "Peptiduria presumably caused by aminopeptidase-P deficiency. A new inborn error of metabolism". Journal of Inherited Metabolic Disease. 11 Suppl 2: 240–2. doi:10.1007/BF01804246. PMID 3141711.
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Vanhoof G, Goossens F, Juliano MA, Juliano L, Hendriks D, Schatteman K, Lin AH, Scharpé S (1998). "Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P)". Cytogenetics and Cell Genetics. 78 (3–4): 275–80. doi:10.1159/000134671. PMID 9465902.
  • Sprinkle TJ, Caldwell C, Ryan JW (Jun 2000). "Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2". Archives of Biochemistry and Biophysics. 378 (1): 51–6. doi:10.1006/abbi.2000.1792. PMID 10871044.
  • Cottrell GS, Hooper NM, Turner AJ (Dec 2000). "Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme". Biochemistry. 39 (49): 15121–8. doi:10.1021/bi001585c. PMID 11106490.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.


Retrieved from "https://www.wikidoc.org/index.php?title=XPNPEP1&oldid=1414336"