| IED ID | IndEnz0015000108 |
| Enzyme Type ID | laccase000108 |
| Protein Name |
Laccase-like multicopper oxidase 1 LMCO EC 1.-.-.- |
| Gene Name | LMCO1 MYCTH_2063133 |
| Organism | Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Chaetomiaceae Thermothelomyces Thermothelomyces thermophilus (Myceliophthora thermophila) Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile) |
| Enzyme Sequence | MLLSKLSILLAKWLSVAVYAGTLVHDEQFIPDHILRVSVAQVPSACENREDVVVNGTSPGPAIHLLPGARTWIRVYNDMNDRNLSMHWHGLSQRFAPFSDGTPSATQWPIPPGHFFDYEILTEPEDAGTYFYHSHVGMQALSCTGPLIVEDCGSSPYHYDDERILLFQDHFQKSDLEMIQGLTSTQFTWTGETRGILLNGRGVSPNQAAVQGRPGEASGFFGSHRFSNFRAGDGTSNSWDGIRGDDQIEPPTDCTLPVIDVEPGKTYRLRFIGATGLSLLTMGFEDHNDLTIVQVDGSEYNAPVTVDHIQLGGGQRFDVLLRTKTAEELRCNGDKTTYFLQFETRDRPDPYRGYGVLRYNLGTPVPAAPTTPALTLPAEVNNWLEYTFQPLHPSSSLSPTAEEVTRRVILEAEQKIDPATGRLVWKLAHMTWTDMSRDKPVLVDIYERGEAAMPDYAAALTNYGWDPATKLFPAKKDEVLEIVIQNTGSHYSGASGIVETHPFHAHGQHFYDVGSGPGKYDPEANNAKLASLGYRPIKRDTTMVYRYGEGKVAPGEPAGWRAWRMKMNNPGVWMVHCHILAHMIMGMETIWVVGDAEDIVTIPLSVSQNYFTYGGSVYGNDTHAPEVYHYFDDTNKCCAAGAGDSEDSGH |
| Enzyme Length | 650 |
| Uniprot Accession Number | G2QFD0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Retains almost half of its activity in presence of high salt concentrations up to 100 mM NaCl (PubMed:30529567). Retains also more than 85% of its original activity in the presence of 1 mM EDTA, indicating a satisfactory resistance towards chelators, which is rare among metal-containing enzyme (PubMed:30529567). The activity drops significantly in the presence of NaN(3) or SDS (PubMed:30529567). Appears more active in the presence of methanol compared to ethanol, but acetone or DMSO addition severely affect remaining laccase activity (PubMed:30529567). {ECO:0000269|PubMed:30529567}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 2',3,4-trihydroxy-trans-chalcone + 2 H(+) + O2 = 2 3',4'-dihydroxyaurone + 2 H2O; Xref=Rhea:RHEA:63848, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:144744, ChEBI:CHEBI:144745; Evidence={ECO:0000269|PubMed:30529567};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63849; Evidence={ECO:0000269|PubMed:30529567}; |
| DNA Binding | |
| EC Number | 1.-.-.- |
| Enzyme Function | FUNCTION: Yellow laccase-like multicopper oxidase that is able to oxidize a variety of phenolic compounds including standard laccase substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567). Can be used for the bioconversion of 2',3,4-trihy-droxychalcone to 3',4'-dihydroxy-aurone, a bioactive aurone recently shown to possess inhibitory activity against several isoforms of the histone deacetylase complex (HDAC) (PubMed:30529567). {ECO:0000269|PubMed:30529567}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:30529567}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:30529567}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (3); Glycosylation (3); Metal binding (11); Signal peptide (1) |
| Keywords | Copper;Glycoprotein;Metal-binding;Oxidoreductase;Reference proteome;Repeat;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 72,050 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.37 mM for ABTS {ECO:0000269|PubMed:30529567}; KM=2.41 mM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:30529567}; |
| Metal Binding | METAL 87; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 89; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 133; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 135; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 501; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 504; /note=Copper 1; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 506; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 576; /note=Copper 3; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 577; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 578; /note=Copper 2; /evidence=ECO:0000250|UniProtKB:Q70KY3; METAL 582; /note=Copper 4; /evidence=ECO:0000250|UniProtKB:Q70KY3 |
| Rhea ID | RHEA:63848; RHEA:63849 |
| Cross Reference Brenda |