AI Article Synopsis
- The study identifies a copper amine oxidase from Pichia pastoris as a non-mammalian lysyl oxidase, contrasting with the mammalian version that contains a unique lysine tyrosylquinone cofactor.
- Recent efforts revealed the active-site peptide of P. pastoris lysyl oxidase as a phenylhydrazone derivative, which shares a conserved sequence with other amine oxidases containing topa quinone.
- The resonance Raman spectra of the enzyme and its derivatives match those of a topa quinone model, confirming that P. pastoris lysyl oxidase functions as a topa quinone enzyme.
Article Abstract
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, 1078-1084]. 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.
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| http://dx.doi.org/10.1016/s0014-5793(96)01245-8 | DOI Listing |
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