Sequence of PEPT_LACLL
EC Number:3.4.11.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
release of the N-terminal residue from a tripeptide
Other sequences found for EC No. 3.4.11.4
General information:
Sequence
0 MKYEKLLPRF LEYVKVNTRS DENSTTTPST QALVEFAHKM GEDMKALGLK DVHYLESNGY
60 VIGTIPANTD KKVRKIGLLA HLDTADFNAE GVNPQILENY DGESVIKLGD TEFTLDPKDF
120 PNLKNYKGQT LVHTDGTTLL GSDDKSGVAE IMTLADYLLN INPDFEHGEI RVGFGPDEEI
180 GVGADKFDVA DFDVDFAYTV DGGPLGELQY ETFSAAGAVI EFQGKNVHPG TAKNTMVNAL
240 QLAIDYHNAL PEFDRPEKTE GREGFFHLLK LDGTPEEARA QYIIRDHEEG KFNERKALMQ
300 EIADKMNAEL GQNRVKPVIK DQYYNMAQII EKDMSIIDIA KKAMENLDIV PIIEPIRGGT
360 DGSKISFMGL PTPNLFAGGE NMHGRFEFVS VQTMEKAVDT LLEIIRLNNE VVK
Download this sequence
Download all sequences for 3.4.11.4
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
203682
Mori S.,Mori K.,Suzuki I.,Kasumi T.
Phylogenetic analysis of Lactococcus lactis subspecies based on decoding the sequence of the pepT tripeptidase gene, the pepV dipeptidase gene and 16S rRNA.
Syst. Appl. Microbiol.
27
414-422
2004
203683
Mori S.,Nirasawa S.,Komba S.,Kasumi T.
Characterization and kinetic analysis of enzyme-substrate recognition by three recombinant lactococcal tripeptidases.
Biochim. Biophys. Acta
1748
26-34
2005
203684
Mori S.,Sumino S.,Kasumi T.
Substrate specificity of a tripeptidase as a metalloenzyme purified from Lactococcus lactis subsp. lactis biovar. diacetylactis ATCC 13675.
J. Biosci. Bioeng.
93
360-366
2002