EC Number   |
General Information |
Reference |
|---|
   1.10.3.2 | evolution |
the enzyme belongs to the blue multicopper oxidase superfamily |
726424 |
| 1.10.3.2 | malfunction |
changes in the C-terminus of MaL caused major defects in protein production in both expression hosts |
697913 |
| 1.10.3.2 | malfunction |
elimination of the N-terminal sequence decreases the specific activity 15fold, which is partially restored in the presence of 1 M NaCl, and alters the secondary and tertiary structures and the pH dependence of optimal stability |
-, 746372 |
| 1.10.3.2 | metabolism |
the three copper sites play related but distinct roles in CueO oxidase activities. The internal Cu5 site is part of the essential electron transfer pathway connecting surface-exposed sites Cu6 and Cu7 to site T1. Both Cu6 and Cu7 are dominant substrate-docking-oxidation sites on the protein surface. The two surface-exposed sites Cu6 and Cu7 are the direct substrate-docking-oxidation sites for both oxidase functions and buried site Cu5 channels electrons from the oxidations to the Type 1 site of the multicopper oxidase machinery |
763429 |
| 1.10.3.2 | more |
a total of 52 genes encoding laccases (SvLAC1 to SvLAC52) are found in the genome of Setaria viridis, and phylogenetic analyses show that these genes are heterogeneously distributed among the characteristic six subclades of the family and are under relaxed selective constraints. Five SvLAC genes (SvLAC9, SvLAC13, SvLAC15, SvLAC50, and SvLAC52) fulfill the criteria established to identify lignin-related candidates: (1) phylogenetic proximity to previously characterized lignin-related laccases from other species, (2) similar expression pattern to that observed for lignin biosynthetic genes in the Setaria viridis elongating internode, and (3) high expression in Setaria viridis tissues undergoing active lignification |
765630 |
| 1.10.3.2 | more |
the enzyme has a high redox potential |
-, 746372 |
| 1.10.3.2 | more |
the laccase does not exert any antiproliferative activity against Hep-G2 or MCF-7 tumor cell lines at a concentration of 0.06 mM, but shows significant activity toward human immunodeficiency virus-1 reverse transcriptase with an IC50 of 60 nM |
725692 |
| 1.10.3.2 | more |
the laccase from Melanocarpus albomyces is a low redox potential enzyme. Structure-function study, mass spectrometry, overview |
724417 |
| 1.10.3.2 | more |
the laccase from Rhus vernicifera is a low redox potential enzyme. Structure-function study, mass spectrometry, overview |
724417 |
| 1.10.3.2 | more |
the laccase from Trametes hirsuta is a high redox potential enzyme. Structure-function study, mass spectrometry, overview |
-, 724417 |
