title: Destabilase from the medicinal leech is a representative of a novel family of lysozymes.
abstract: Intrinsic lysozyme-like activity was demonstrated for destabilase from the medicinal leech supported by (1) high specific lysozyme activity of the highly purified destabilase, (2) specific inhibition of the lysozyme-like activity by anti-destabilase antibodies, and (3) appreciable lysozyme-like activity in insect cells infected with recombinant baculoviruses carrying cDNAs encoding different isoforms of destabilase. Several isoforms of destabilase constitute a protein family at least two members of which are characterized by lysozyme activity. The corresponding gene family implies an ancient evolutionary history of the genes although the function(s) of various lysozymes in the leech remains unclear. Differences in primary structures of the destabilase family members and members of known lysozyme families allow one to assign the former to a new family of lysozymes. New proteins homologous to destabilase were recently described for Caenorhabditis elegans and bivalve mollusks suggesting that the new lysozyme family can be widely distributed among invertebrates. It remains to be investigated whether the two enzymatic activities (isopeptidase and lysozyme-like) are attributes of one and the same protein.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117871, Moscow, Russia. leech@humgen.siobc.ras.ru
authors.forename: L L
authors.initials: LL
authors.lastname: Zavalova
authors.forename: I P
authors.initials: IP
authors.lastname: Baskova
authors.forename: S A
authors.initials: SA
authors.lastname: Lukyanov
authors.forename: A V
authors.initials: AV
authors.lastname: Sass
authors.forename: E V
authors.initials: EV
authors.lastname: Snezhkov
authors.forename: S B
authors.initials: SB
authors.lastname: Akopov
authors.forename: I I
authors.initials: II
authors.lastname: Artamonova
authors.forename: V S
authors.initials: VS
authors.lastname: Archipova
authors.forename: V A
authors.initials: VA
authors.lastname: Nesmeyanov
authors.forename: D G
authors.initials: DG
authors.lastname: Kozlov
authors.forename: S V
authors.initials: SV
authors.lastname: Benevolensky
authors.forename: V I
authors.initials: VI
authors.lastname: Kiseleva
authors.forename: A M
authors.initials: AM
authors.lastname: Poverenny
authors.forename: E D
authors.initials: ED
authors.lastname: Sverdlov
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D016367:Baculoviridae / Q000235:genetics; D019759:Carbon-Nitrogen Lyases / Q000378:metabolism; D002460:Cell Line; D018076:DNA, Complementary / Q000235:genetics; D010450:Endopeptidases / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D015870:Gene Expression; D007527:Isoenzymes / Q000737:chemistry; D007865:Leeches / Q000201:enzymology*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D000906:Antibodies; D018076:DNA, Complementary; D007527:Isoenzymes; D009113:Muramidase; D010450:Endopeptidases; C045348:fibrin destabilase; D019759:Carbon-Nitrogen Lyases; C034300:isopeptidase