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Enzyme from the medicinal leech ( Hirudo medicinalis ) that specifically splits endo‐ϵ(‐γ‐Glu)‐Lys isopeptide bonds: cDNA cloning and protein primary structure
Author(s) -
Fradkov Arkady,
Berezhnoy Sergey,
Barsova Ekaterina,
Zavalova Lyudmila,
Lukyanov Sergey,
Baskova Isolda,
Sverdlov Eugene D.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00644-8
Subject(s) - hirudo medicinalis , complementary dna , peptide sequence , leech , protein primary structure , biochemistry , amino acid , biology , protein sequencing , microbiology and biotechnology , cloning (programming) , gene , world wide web , computer science , programming language
Earlier we detected a novel enzymatic activity in salivary gland secretion of the medicinal leech, splitting isopeptide bonds between the glutamine γ‐carboxamide and lysine ϵ‐amino group. This activity is due to destabilase. We described its partial amino acid sequence and sequences of two closely related cDNAs, but none of them perfectly matched the protein isolated. Here we report the isolation and sequence peculiarities of the third cDNA of the family as well as the complete sequence of the destabilase protein. The inferred mature protein product of this cDNA matches the independently determined destabilase protein sequence. It contains 115 amino acid residues including 14 highly conserved Cys residues and is formed from a precursor containing specific leader peptide.