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Identification of the disulfide bonds of lysyl oxidase

  • Basic Neurosciences, Genetics and Immunology - Short Communication
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Abstract

Proteolytic digestion of bovine aortic lysyl oxidase followed by tandem mass spectrometry has enabled assignment of all five disulfide bonds. The results indicate that the enzyme has a very stable central core containing three disulfide bonds, the lysyl tyrosyl quinone cross-link and the copper. This core is well isolated from solvent with the result that the oxidized (normal) form of the enzyme is remarkably resistant to proteolysis and is unusually stable at high temperatures and in the presence of denaturants.

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Fig. 1

Abbreviations

ABC:

Ammonium bicarbonate

BNPS-Skatole:

2-(2-Nitrophenylsulfenyl)-3-methyl-3-bromoindolenine

LC/MS/MS:

Tandem mass spectrometry

LOX:

Lysyl oxidase

LOXL:

Lysyl oxidase-like protein

LTQ:

Lysyl tyrosyl quinone

TFA:

Trifluoroacetic acid

TPQ:

Topaquinone

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Acknowledgments

This work was partially supported by grant R15 GM49392-01A1 from the National Institutes of Health and by a grant from Nuclea Biotechnologies. We would like to thank Edward J. Brush and Chunyan Qiu for assistance in the early stages of this work and Ming-zhong Sun and Zhiping Zhu for helpful discussions.

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  1. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St, Worcester, MA, 01610-1477, USA

    Xi Chen & Frederick T. Greenaway

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  1. Xi Chen
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  2. Frederick T. Greenaway
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Correspondence to Frederick T. Greenaway.

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Chen, X., Greenaway, F.T. Identification of the disulfide bonds of lysyl oxidase. J Neural Transm 118, 1111–1114 (2011). https://doi.org/10.1007/s00702-010-0560-y

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