Aminopeptidase N

Details

Name
Aminopeptidase N
Synonyms
  • 3.4.11.2
  • Alpha-aminoacylpeptide hydrolase
Gene Name
pepN
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0013024|Aminopeptidase N
MTQQPQAKYRHDYRAPDYQITDIDLTFDLDAQKTVVTAVSQAVRHGASDAPLRLNGEDLK
LVSVHINDEPWTAWKEEEGALVISNLPERFTLKIINEISPAANTALEGLYQSGDALCTQC
EAEGFRHITYYLDRPDVLARFTTKIIADKIKYPFLLSNGNRVAQGELENGRHWVQWQDPF
PKPCYLFALVAGDFDVLRDTFTTRSGREVALELYVDRGNLDRAPWAMTSLKNSMKWDEER
FGLEYDLDIYMIVAVDFFNMGAMENKGLNIFNSKYVLARTDTATDKDYLDIERVIGHEYF
HNWTGNRVTCRDWFQLSLKEGLTVFRDQEFSSDLGSRAVNRINNVRTMRGLQFAEDASPM
AHPIRPDMVIEMNNFYTLTVYEKGAEVIRMIHTLLGEENFQKGMQLYFERHDGSAATCDD
FVQAMEDASNVDLSHFRRWYSQSGTPIVTVKDDYNPETEQYTLTISQRTPATPDQAEKQP
LHIPFAIELYDNEGKVIPLQKGGHPVNSVLNVTQAEQTFVFDNVYFQPVPALLCEFSAPV
KLEYKWSDQQLTFLMRHARNDFSRWDAAQSLLATYIKLNVARHQQGQPLSLPVHVADAFR
AVLLDEKIDPALAAEILTLPSVNEMAELFDIIDPIAIAEVREALTRTLATELADELLAIY
NANYQSEYRVEHEDIAKRTLRNACLRFLAFGETHLADVLVSKQFHEANNMTDALAALSAA
VAAQLPCRDALMQEYDDKWHQNGLVMDKWFILQATSPAANVLETVRGLLQHRSFTMSNPN
RIRSLIGAFAGSNPAAFHAEDGSGYLFLVEMLTDLNSRNPQVASRLIEPLIRLKRYDAKR
QEKMRAALEQLKGLENLSGDLYEKITKALA
Number of residues
870
Molecular Weight
98917.975
Theoretical pI
4.95
GO Classification
Functions
aminopeptidase activity / identical protein binding / metallopeptidase activity / zinc ion binding
Processes
peptide catabolic process
Components
plasma membrane
General Function
Zinc ion binding
Specific Function
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0013025|Aminopeptidase N (pepN)
ATGACTCAACAGCCACAAGCCAAATACCGTCACGATTATCGTGCGCCGGATTACCAGATT
ACTGATATTGACTTGACCTTTGACCTCGACGCGCAAAAGACGGTCGTTACCGCGGTCAGC
CAGGCTGTCCGTCATGGTGCATCAGATGCTCCCCTTCGTCTCAACGGCGAAGACCTCAAA
CTGGTTTCTGTTCATATTAATGATGAGCCGTGGACCGCCTGGAAAGAAGAAGAGGGCGCA
CTGGTTATCAGTAATTTGCCGGAGCGTTTTACGCTTAAGATCATTAATGAAATAAGCCCG
GCGGCGAATACCGCGCTGGAAGGGCTTTATCAGTCAGGCGATGCGCTTTGCACCCAGTGT
GAAGCCGAAGGTTTCCGCCATATTACGTATTATCTCGACCGCCCGGACGTGCTGGCGCGT
TTTACCACCAAAATTATTGCCGATAAAATCAAATATCCCTTCCTGCTTTCCAATGGTAAC
CGCGTTGCGCAAGGCGAACTGGAAAACGGACGCCATTGGGTACAGTGGCAGGACCCGTTC
CCGAAACCGTGCTACCTGTTTGCGCTGGTGGCAGGCGACTTTGATGTACTGCGCGATACC
TTTACCACGCGTTCTGGTCGCGAAGTAGCACTGGAGCTGTACGTCGATCGCGGCAACCTT
GATCGCGCGCCGTGGGCGATGACCTCGCTGAAAAACTCCATGAAATGGGATGAAGAACGC
TTTGGCCTGGAGTATGACCTCGACATCTATATGATCGTCGCGGTGGATTTCTTCAATATG
GGCGCAATGGAGAATAAGGGGCTGAATATCTTTAACTCCAAATATGTGCTGGCCCGCACC
GACACCGCCACCGACAAAGATTACCTCGATATTGAACGCGTTATCGGCCATGAATATTTC
CATAACTGGACCGGTAACCGAGTGACCTGTCGCGACTGGTTCCAGCTCAGCCTGAAAGAA
GGTTTAACCGTCTTCCGCGATCAGGAGTTCAGCTCTGACCTTGGTTCCCGCGCAGTTAAC
CGCATCAATAATGTACGCACCATGCGCGGATTGCAGTTTGCAGAAGACGCCAGCCCGATG
GCGCACCCGATCCGCCCGGATATGGTCATTGAGATGAACAACTTCTACACCCTGACCGTT
TACGAGAAGGGCGCGGAAGTGATTCGCATGATCCACACCCTGCTTGGCGAAGAAAACTTC
CAGAAAGGGATGCAGCTTTATTTCGAGCGTCATGATGGTAGTGCAGCGACCTGTGACGAC
TTTGTGCAGGCGATGGAAGATGCGTCGAATGTCGATCTCTCCCATTTCCGCCGTTGGTAC
AGCCAGTCCGGTACACCGATTGTGACCGTCAAAGACGACTACAATCCGGAAACCGAGCAG
TACACCCTGACCATCAGCCAGCGCACGCCAGCCACGCCGGATCAGGCAGAAAAACAGCCG
CTGCATATTCCGTTTGCCATCGAACTGTATGATAACGAAGGCAAAGTGATCCCGTTGCAG
AAAGGCGGTCATCCGGTGAATTCCGTGCTGAACGTCACTCAGGCGGAACAGACCTTTGTC
TTTGATAATGTCTACTTCCAGCCGGTGCCTGCGCTGCTGTGCGAATTCTCTGCGCCAGTG
AAACTGGAATATAAGTGGAGCGATCAGCAACTGACCTTCCTGATGCGTCATGCGCGTAAT
GATTTCTCCCGCTGGGATGCGGCGCAAAGTTTGCTGGCAACCTACATCAAGCTGAACGTC
GCGCGTCATCAGCAAGGTCAGCCGCTGTCTCTGCCGGTGCATGTGGCTGATGCTTTCCGC
GCGGTACTGCTTGATGAGAAGATTGATCCAGCGCTGGCGGCAGAAATCCTGACGCTGCCT
TCTGTCAATGAAATGGCTGAATTGTTCGATATCATCGACCCGATTGCTATTGCCGAAGTA
CGCGAAGCACTCACTCGTACTCTGGCGACTGAACTGGCGGATGAGCTACTGGCTATTTAC
AACGCGAATTACCAGAGCGAGTACCGTGTTGAGCATGAAGATATTGCAAAACGCACTCTG
CGTAATGCCTGCCTGCGTTTCCTCGCTTTTGGTGAAACGCATCTGGCTGATGTGCTGGTG
AGCAAGCAGTTCCACGAAGCAAACAATATGACTGATGCGCTGGCGGCGCTTTCTGCGGCG
GTTGCCGCACAGCTGCCTTGCCGTGACGCGCTGATGCAGGAGTACGACGACAAGTGGCAT
CAGAACGGTCTGGTGATGGATAAATGGTTTATCCTGCAAGCCACCAGCCCGGCGGCGAAT
GTGCTGGAGACGGTGCGCGGCCTGTTGCAGCATCGCTCATTTACCATGAGCAACCCGAAC
CGTATTCGTTCGTTGATTGGCGCGTTTGCGGGCAGCAATCCGGCAGCGTTCCATGCCGAA
GATGGCAGCGGTTACCTGTTCCTGGTGGAAATGCTTACCGACCTCAACAGCCGTAACCCG
CAGGTGGCTTCACGTCTGATTGAACCGCTGATTCGCCTGAAACGTTACGATGCCAAACGT
CAGGAGAAAATGCGCGCGGCGCTGGAACAGTTGAAAGGGCTGGAAAATCTCTCTGGCGAT
CTGTACGAGAAGATAACTAAAGCACTGGCTTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP04825
UniProtKB Entry NameAMPN_ECOLI
GenBank Protein ID42353
GenBank Gene IDX04020
General References
  1. Foglino M, Gharbi S, Lazdunski A: Nucleotide sequence of the pepN gene encoding aminopeptidase N of Escherichia coli. Gene. 1986;49(3):303-9. [Article]
  2. McCaman MT, Gabe JD: The nucleotide sequence of the pepN gene and its over-expression in Escherichia coli. Gene. 1986;48(1):145-53. [Article]
  3. Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. McCaman MT, Gabe JD: Sequence of the promoter and 5' coding region of pepN, and the amino-terminus of peptidase N from Escherichia coli K-12. Mol Gen Genet. 1986 Jul;204(1):148-52. [Article]
  7. Bally M, Foglino M, Bruschi M, Murgier M, Lazdunski A: Nucleotide sequence of the promoter and amino-terminal encoding region of the Escherichia coli pepN gene. Eur J Biochem. 1986 Mar 17;155(3):565-9. [Article]
  8. Ito K, Nakajima Y, Onohara Y, Takeo M, Nakashima K, Matsubara F, Ito T, Yoshimoto T: Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition. J Biol Chem. 2006 Nov 3;281(44):33664-76. Epub 2006 Aug 2. [Article]
  9. Addlagatta A, Gay L, Matthews BW: Structural basis for the unusual specificity of Escherichia coli aminopeptidase N. Biochemistry. 2008 May 13;47(19):5303-11. doi: 10.1021/bi7022333. Epub 2008 Apr 17. [Article]
  10. Fournie-Zaluski MC, Poras H, Roques BP, Nakajima Y, Ito K, Yoshimoto T: Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250. Acta Crystallogr D Biol Crystallogr. 2009 Aug;65(Pt 8):814-22. doi: 10.1107/S090744490901779X. Epub 2009 Jul 17. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08506N-{(2S)-3-[(1R)-1-aminoethyl](hydroxy)phosphoryl-2-benzylpropanoyl}-L-phenylalanineexperimentalunknownDetails