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Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase.
Mure M, Brown DE, Saysell C, Rogers MS, Wilmot CM, Kurtis CR, McPherson MJ, Phillips SE, Knowles PF, Dooley DM. Mure M, et al. Among authors: kurtis cr. Biochemistry. 2005 Feb 8;44(5):1568-82. doi: 10.1021/bi047988k. Biochemistry. 2005. PMID: 15683241
The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.
Rogers MS, Tyler EM, Akyumani N, Kurtis CR, Spooner RK, Deacon SE, Tamber S, Firbank SJ, Mahmoud K, Knowles PF, Phillips SE, McPherson MJ, Dooley DM. Rogers MS, et al. Among authors: kurtis cr. Biochemistry. 2007 Apr 17;46(15):4606-18. doi: 10.1021/bi062139d. Epub 2007 Mar 27. Biochemistry. 2007. PMID: 17385891 Free PMC article.
Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct.
Mure M, Kurtis CR, Brown DE, Rogers MS, Tambyrajah WS, Saysell C, Wilmot CM, Phillips SE, Knowles PF, Dooley DM, McPherson MJ. Mure M, et al. Among authors: kurtis cr. Biochemistry. 2005 Feb 8;44(5):1583-94. doi: 10.1021/bi0479860. Biochemistry. 2005. PMID: 15683242