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Sequence of CBPD_LOPSP

EC Number:3.4.17.22

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
metallocarboxypeptidase D
P83852
Lophonetta specularioides
380
43292
Reaction
releases C-terminal Arg and Lys from polypeptides
Other sequences found for EC No. 3.4.17.22

General information:

Sequence
show sequence in fasta format
  0 QAVQPVDFRH HHFSDMEIFL RRYANEYPSI TRLYSVGKSV ELRELYVMEI SDNPGIHEAG
 60 EPEFKYIGNM HGNEVVGREL LLNLIEYLCK NFGTDPEVTD LVQSTRIHIM PSMNPDGYEK
120 SQEGDRGGTV GRNNSNNYDL NRNFPDQFFQ VTDPPQPETL AVMSWLKTYP FVLSANLHGG
180 SLVVNYPFDD DEQGIAIYSK SPDDAVFQQL ALSYSKENKK MYQGSPCKDL YPTEYFPHGI
240 TNGAQWYNVP GGMQDWNYLN TNCFEVTIEL GCVKYPKAEE LPKYWEQNRR SLLQFIKQVH
300 RGIWGFVLDA TDGRGILNAT ISVADINHPV TTYKDGDYWR LLVQGTYKVT ASARGYDPVT
360 KTVEVDSKGG VQVNFTLSRT
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
14135
Gomis-Rueth F.-X.,Companys V.,Qian Y.,Fricker L.D.,Vendrell J.,Aviles F.X.,Coll M.
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily.
EMBO J.
18
5817-5826
1999
14136
Aloy P.,Companys V.,Vendrell J.,Aviles F.X.,Fricker L.D.,Coll M.,Gomis-Rueth F.-X.
The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases.
J. Biol. Chem.
276
16177-16184
2001