Cloning, sequence analysis, and characterization of the ‘Lysyl Oxidase’ from Pichia Pastoris
| Autor: | David M. Dooley, Jason A. Kuchar |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Amine oxidase Protein Conformation Molecular Sequence Data Lysine Lysyl oxidase Crystallography X-Ray Spectrum Analysis Raman Biochemistry Pichia Pichia pastoris Protein-Lysine 6-Oxidase Inorganic Chemistry Animals Humans Amino Acid Sequence Cloning Molecular chemistry.chemical_classification Binding Sites biology Chemistry Circular Dichroism Electron Spin Resonance Spectroscopy Active site Substrate (chemistry) biology.organism_classification Recombinant Proteins Kinetics Enzyme biology.protein Diamine oxidase Sequence Alignment Copper |
| Zdroj: | Journal of Inorganic Biochemistry. 83:193-204 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/s0162-0134(00)00202-6 |
| Popis: | Lysyl oxidase from Pichia pastoris has been successfully overexpressed. EPR and resonance Raman experiments have shown that copper and TPQ are present, respectively. Lysyl oxidase from P. pastoris has a similar substrate specificity to the mammalian enzyme (both have been shown to oxidize peptidyl lysine residues) and is 30% identical to the human kidney diamine oxidase (the highest of any non-mammalian source). This enzyme also has a relatively broad substrate specificity compared to other amine oxidases. Molecular modeling data suggest that the substrate channel in lysyl oxidase from P. pastoris permits greater active site access than observed in structurally-characterized amine oxidases. This larger channel may account for the diversity of substrates that are turned over by this enzyme. |
| Databáze: | OpenAIRE |
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