Published March 2014
| public
Journal Article
Crystal Structure of Dihydropyrimidinase from Tetraodon nigroviridis with Lysine Carboxylation: Metal Requirement for Post-translational Modification and Function
- Creators
- Chen, C.
- Hsieh, Y.
- Yang, Y.
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Chan, S. I.
Chicago
Abstract
Lysine carboxylation, a post-translational, facilitates metal coordination for specific enzymatic activities. We have determined structures of the vertebrate dihydropyrimidinase from Tetraodon nigroviridis (TnDhp) in various states: the apo enzyme as well as two forms of the holo enzyme with one and two metals at the catalytic site.
Additional Information
© 2014 Springer.Additional details
- Eprint ID
- 45212
- DOI
- 10.1007/s00775-014-1095-8
- Resolver ID
- CaltechAUTHORS:20140425-084531804
- Created
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2014-04-25Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field