IPR012864
Cysteine oxygenase/2-aminoethanethiol dioxygenase
InterPro entry
Short name | PCO/ADO |
Overlapping homologous superfamilies |
Description
This entry includes cysteine oxidases (PCOs) from plants and 2-aminoethanethiol dioxygenases (ADOs) from animals. PCOs oxidize N-terminal cysteine residues, thus preparing the protein for N-end rule pathway-mediated proteasomal degradation
[1]. ADO is responsible for endogenous cysteamine dioxygenase activity
[2].
References
1.Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway. Weits DA, Giuntoli B, Kosmacz M, Parlanti S, Hubberten HM, Riegler H, Hoefgen R, Perata P, van Dongen JT, Licausi F. Nat Commun 5, 3425, (2014). View articlePMID: 24599061
2.Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. Dominy JE Jr, Simmons CR, Hirschberger LL, Hwang J, Coloso RM, Stipanuk MH. J. Biol. Chem. 282, 25189-98, (2007). View articlePMID: 17581819
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
Representative structure
7lvz: Crystal structure of ADO