Enzyme from the medicinal leech (Hirudo medicinalis) that specifically splits endo‐ϵ(‐γ‐Glu)‐Lys isopeptide bonds: cDNA cloning and protein primary structure

FEBS Letters

Berezhnoy, Sergey³  Barsova, Ekaterina³  Baskova, Isolda²  Zavalova, Lyudmila³  Fradkov, Arkady³  Lukyanov, Sergey³  Sverdlov, Eugene D.¹ 

[1] Institute of Molecular Genetics, Russian Academy of Sciences, 123182 Moscow, Russian Federation;Biological Faculty, Moscow State University, 119899 Moscow, Russian Federation;Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117871 Moscow, Russian Federation

关键词: Protein sequence;    Gene family;    Gene characterization;    ϵ-(γ-Glu)-Lys;    Isopeptidase;    Medicinal leech;   

DOI  :  10.1016/0014-5793(96)00644-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown