| IED ID | IndEnz0018001596 |
| Enzyme Type ID | peroxidase001596 |
| Protein Name |
3-methyl-L-tyrosine peroxygenase EC 1.11.2.5 |
| Gene Name | sfmD |
| Organism | Streptomyces lavendulae |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Streptomycetales Streptomycetaceae Streptomyces Streptomyces lavendulae |
| Enzyme Sequence | MTAPADTVHPAGQPDYVAQVATVPFRLGRPEELPGTLDELRAAVSARAGEAVRGLNRPGARTDLAALLAATERTRAALAPVGAGPVGDDPSESEANRDNDLAFGIVRTRGPVAELLVDAALAALAGILEVAVDRGSDLEDAAWQRFIGGFDALLGWLADPHSAPRPATVPGAGPAGPPVHQDALRRWVRGHHVFMVLAQGCALATACLRDSAARGDLPGAEASAAAAEALMRGCQGALLYAGDANREQYNEQIRPTLMPPVAPPKMSGLHWRDHEVLIKELAGSRDAWEWLSAQGSERPATFRAALAETYDSHIGVCGHFVGDQSPSLLAAQGSTRSAVGVIGQFRKIRLSALPEQPATQQGEPS |
| Enzyme Length | 365 |
| Uniprot Accession Number | B0CN28 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=3-methyl-L-tyrosine + H2O2 = 5-hydroxy-3-methyl-L-tyrosine + H2O; Xref=Rhea:RHEA:41432, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:78239, ChEBI:CHEBI:78241; EC=1.11.2.5; Evidence={ECO:0000269|PubMed:22187429}; |
| DNA Binding | |
| EC Number | 1.11.2.5 |
| Enzyme Function | FUNCTION: Heme-containing peroxygenase that mediates the hydroxylation of 3-methyl-L-tyrosine (3-Me-Tyr) into 3-hydroxy-5-methyl-L-tyrosine (3-OH-5-Me-Tyr) in biosynthesis of saframycin A, a potent antitumor antibiotic that belongs to the tetrahydroisoquinoline family. Involved in biosynthesis of 3-hydroxy-5-methyl-O-methyltyrosine (3-OH-5-Me-OMe-Tyr), a core structure of saframycin A. {ECO:0000269|PubMed:19494690, ECO:0000269|PubMed:22187429}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:22187429}; |
| Pathway | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19494690, ECO:0000269|PubMed:22187429}. |
| nucleotide Binding | |
| Features | Beta strand (2); Chain (1); Helix (11); Mutagenesis (4); Region (1); Turn (3) |
| Keywords | 3D-structure;Antibiotic biosynthesis;Heme;Iron;Metal-binding;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 6VDP; 6VDQ; 6VDZ; 6VE0; |
| Mapped Pubmed ID | 34163669; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,191 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.64 mM for 3-methyl-L-tyrosine {ECO:0000269|PubMed:22187429}; KM=1 mM for tyrosine {ECO:0000269|PubMed:22187429}; Note=kcat is 17.8 min(-1) with 3-methyl-L-tyrosine as substrate. kcat is 12.3 min(-1) with L-tyrosine as substrate. {ECO:0000269|PubMed:22187429}; |
| Metal Binding | |
| Rhea ID | RHEA:41432 |
| Cross Reference Brenda | 1.11.2.5; |