Identification of the quinone cofactor in a lysyl oxidase from Pichia pastoris

FEBS Letters

Dooley, David M.²  Dove, Joanne E.³  Klinman, Judith P.³  Kuchar, Jason²  Smith, Alan J.¹  Brown, Doreen E.² 

[1] Beckman Center, B062, Stanford University, Stanford, CA 94305-5425, USA;Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 95717, USA;Departments of Chemistry and Molecular and Cellular Biology, University of California, Berkeley, CA 94720, USA

关键词: Amine oxidase;    Lysyl oxidase;    Topa quinone;    Copper protein;   

DOI  :  10.1016/S0014-5793(96)01245-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A copper amine oxidase from Pichia pastoris is the only known non-mammalian lysyl oxidase [Tur, S.S. and Lerch, K. (1988) FEBS Lett. 238, 74–76]. Recently, the cofactor in mammalian lysyl oxidase has been identified as a novel lysine tyrosylquinone moiety [Wang, S.X., Mure, M., Medzihradszky, K.F., Burlingame, A.L., Brown, D.E., Dooley, D.M., Smith, A.J., Kagan, H.M. and Klinman, J.P. (1996) Science 273, 1078–1082]. In order to identify the cofactor in P. pastoris lysyl oxidase, we have isolated the phenylhydrazone-derivative of the active-site peptide. This peptide has the active-site sequence conserved among topa quinone containing amine oxidases. The resonance Raman spectra of the phenylhydrazone derivatives of the enzyme, active-site peptide, and a topa quinone model compound are essentially identical. Collectively, these results establish that P. pastoris lysyl oxidase is a topa quinone enzyme.

【 授权许可】

Unknown