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Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels

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Abstract

Cysteine catabolism in mammals is dependent upon cysteine dioxygenase (CDO), an enzyme that adds molecular oxygen to the sulfur of cysteine, converting the thiol to a sulfinic acid known as cysteinesulfinic acid (3-sulfinoalanine). CDO is one of the most highly regulated metabolic enzymes responding to diet that is known. It undergoes up to 45-fold changes in concentration and up to 10-fold changes in catalytic efficiency. This provides a remarkable responsiveness of the cell to changes in sulfur amino acid availability: the ability to decrease CDO activity and conserve cysteine when cysteine is scarce and to rapidly increase CDO activity and catabolize cysteine to prevent cytotoxicity when cysteine supply is abundant. CDO in both liver and adipose tissues responds to changes in dietary intakes of protein and/or sulfur amino acids over a range that encompasses the requirement level, suggesting that cysteine homeostasis is very important to the living organism.

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Abbreviations

CDO:

Cysteine dioxygenase

SDS-PAGE:

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis

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Acknowledgments

This work was supported by National Institute of Diabetes and Digestive and Kidney Diseases through Public Health Service Grant # DK056649 (to MHS).

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Authors and Affiliations

  1. Division of Nutritional Sciences, Cornell University, 227 Savage Hall, Ithaca, NY, 14853, USA

    M. H. Stipanuk, I. Ueki, J. E. Dominy Jr, C. R. Simmons & L. L. Hirschberger

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  1. M. H. Stipanuk
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  2. I. Ueki
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  3. J. E. Dominy Jr
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  4. C. R. Simmons
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  5. L. L. Hirschberger
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Correspondence to M. H. Stipanuk.

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Stipanuk, M.H., Ueki, I., Dominy, J.E. et al. Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels. Amino Acids 37, 55–63 (2009). https://doi.org/10.1007/s00726-008-0202-y

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  • DOI: https://doi.org/10.1007/s00726-008-0202-y

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