title: Herinase: a novel bi-functional fibrinolytic protease from the monkey head mushroom, Hericium erinaceum.
abstract: Herinase, a new bi-functional fibrinolytic metalloprotease, was purified from a medicinal and edible mushroom Hericium erinaceum. The enzyme was monomeric with a molecular mass of 51 kDa. Analysis of fibrin zymography showed an active band with a similar molecular mass. The N-terminal sequence of herinase VPSSFRTTITDAQLRG was highly distinguished from known fibrinolytic enzymes. Moreover, the enzyme activity was strongly inhibited by EDTA and EGTA, indicating that herinase is a metalloprotease. Herinase exhibited high specificity for the substrate t-PA followed by plasmin. The K(m) and V(max) values for H-D-Ile-Pro-Arg-PNA were found to be 4.7 mg and 26.7 U/ml respectively. Similarly, fibrin plate assays revealed that it was able to degrade fibrin clot directly and also able to activate plasminogen. Herinase provoked a rapid degradation of fibrin and fibrinogen α chains and slower degradation of γ chains. It had no activity on the β chains of fibrin and fibrinogen. This result suggests that herinase could possibly contain higher amount of α-fibrinogenase. The activity of herinase was stimulated by metal ions such as Ca(2+), Mg(2+), and Mn(2+), but inhibited by Cu(2+), Fe(2+), and Zn(2+). Herinase exhibited maximum activity at 30 °C and pH 7.0. These results demonstrate that herinase could be a novel fibrinolytic enzyme.
authors.affiliation: Department of Biotechnology, Chosun University, 375 Seosuk-dong, Dong-gu, Gwangju 501-759, Republic of Korea.
authors.forename: Bong-Suk
authors.initials: BS
authors.lastname: Choi
authors.forename: Kumar
authors.initials: K
authors.lastname: Sapkota
authors.forename: Jun-Hui
authors.initials: JH
authors.lastname: Choi
authors.forename: Chang-ho
authors.initials: CH
authors.lastname: Shin
authors.forename: Seung
authors.initials: S
authors.lastname: Kim
authors.forename: Sung-Jun
authors.initials: SJ
authors.lastname: Kim
mesh_terms: D000363:Agaricales / Q000201:enzymology; D000595:Amino Acid Sequence; D002413:Cations, Divalent / Q000494:pharmacology; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism; D005342:Fibrinolysis / Q000187:drug effects; D005343:Fibrinolytic Agents / Q000302:isolation & purification / Q000378:metabolism; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D045726:Metalloproteases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013379:Substrate Specificity; D013696:Temperature; D010959:Tissue Plasminogen Activator / Q000378:metabolism
chemical_list: D002413:Cations, Divalent; D005343:Fibrinolytic Agents; D005656:Fungal Proteins; D005337:Fibrin; D005340:Fibrinogen; D045726:Metalloproteases; C583945:herinase, Hericium erinaceum; D010959:Tissue Plasminogen Activator; D005341:Fibrinolysin