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Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.

Publication ,  Journal Article
Tschantz, WR; Digits, JA; Pyun, HJ; Coates, RM; Casey, PJ
Published in: J Biol Chem
January 26, 2001

Prenylated proteins contain either a 15-carbon farnesyl or a 20-carbon geranylgeranyl isoprenoid covalently attached via a thioether bond to a cysteine residue at or near their C terminus. As prenylated proteins comprise up to 2% of the total protein in eukaryotic cells, and the thioether bond is a stable modification, their degradation raises a metabolic challenge to cells. A lysosomal enzyme termed prenylcysteine lyase has been identified that cleaves prenylcysteines to cysteine and an unidentified isoprenoid product. Here we show that the isoprenoid product of prenylcysteine lyase is the C-1 aldehyde of the isoprenoid moiety (farnesal in the case of C-15). The enzyme requires molecular oxygen as a cosubstrate and utilizes a noncovalently bound flavin cofactor in an NAD(P)H-independent manner. Additionally, a stoichiometric amount of hydrogen peroxide is produced during the reaction. These surprising findings indicate that prenylcysteine lyase utilizes a novel oxidative mechanism to cleave thioether bonds and provide insight into the unique role this enzyme plays in the cellular metabolism of prenylcysteines.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

January 26, 2001

Volume

276

Issue

4

Start / End Page

2321 / 2324

Location

United States

Related Subject Headings

  • Sulfides
  • Models, Chemical
  • Lysosomes
  • Hydrogen Peroxide
  • Flavin-Adenine Dinucleotide
  • Farnesol
  • Cysteine
  • Carbon-Sulfur Lyases
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences
 

Citation

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Tschantz, W. R., Digits, J. A., Pyun, H. J., Coates, R. M., & Casey, P. J. (2001). Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J Biol Chem, 276(4), 2321–2324. https://doi.org/10.1074/jbc.C000616200
Tschantz, W. R., J. A. Digits, H. J. Pyun, R. M. Coates, and P. J. Casey. “Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.J Biol Chem 276, no. 4 (January 26, 2001): 2321–24. https://doi.org/10.1074/jbc.C000616200.
Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ. Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J Biol Chem. 2001 Jan 26;276(4):2321–4.
Tschantz, W. R., et al. “Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.J Biol Chem, vol. 276, no. 4, Jan. 2001, pp. 2321–24. Pubmed, doi:10.1074/jbc.C000616200.
Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ. Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J Biol Chem. 2001 Jan 26;276(4):2321–2324.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

January 26, 2001

Volume

276

Issue

4

Start / End Page

2321 / 2324

Location

United States

Related Subject Headings

  • Sulfides
  • Models, Chemical
  • Lysosomes
  • Hydrogen Peroxide
  • Flavin-Adenine Dinucleotide
  • Farnesol
  • Cysteine
  • Carbon-Sulfur Lyases
  • Biochemistry & Molecular Biology
  • 34 Chemical sciences