Compensatory binding of an asparagine residue to the coordination-unsaturated type I Cu center in bilirubin oxidase mutants
スポンサーリンク
概要
- 論文の詳細を見る
Met467, the axial ligand to type I Cu in a multicopper oxidase, Myrothecium verrucaria bilirubin oxidase was substituted with a non-coordinating Phe and Leu to transform the spectral and magnetic properties and oxidase activities of the enzyme into those of fungal laccases, but the mutated type I Cu center showed properties characteristic of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459 as evidenced by a double mutation. © 2008 Elsevier Inc. All rights reserved.
- Academic Pressの論文
- 2008-07-04
Academic Press | 論文
- The protein content of an adaptor protein, STAP-2 is controlled by E3 ubiquitin ligase Cbl
- STAP-2 is phosphorylated at tyrosine-250 by Brk and modulates Brk-mediated STAT3 activation
- The IL-6 family of cytokines modulates STAT3 activation by desumoylation of PML through SENP1 induction
- Sumoylation of Smad3 stimulates its nuclear export during PIASy-mediated suppression of TGF-β signaling
- KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression