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Crystal Structure of Dihydropyrimidinase from Tetraodon nigroviridis with Lysine Carboxylation: Metal Requirement for Post-translational Modification and Function

Chen, C. and Hsieh, Y. and Yang, Y. and Chan, S. I. (2014) Crystal Structure of Dihydropyrimidinase from Tetraodon nigroviridis with Lysine Carboxylation: Metal Requirement for Post-translational Modification and Function. Journal of Biological Inorganic Chemistry, 19 (S1). S91. ISSN 0949-8257. https://resolver.caltech.edu/CaltechAUTHORS:20140425-084531804

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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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://link.springer.com/article/10.1007%2Fs00775-014-1095-8PublisherArticle
http://dx.doi.org/10.1007/s00775-014-1095-8DOIArticle
http://rdcu.be/v4zWPublisherFree ReadCube access
ORCID:
AuthorORCID
Chan, S. I.0000-0002-5348-2723
Additional Information:© 2014 Springer.
Issue or Number:S1
Record Number:CaltechAUTHORS:20140425-084531804
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20140425-084531804
Official Citation:J Biol Inorg Chem. 2014 Mar;19 Suppl 1:1-696. doi: 10.1007/s00775-014-1095-8. XVI(th) International Conference on Biological Inorganic Chemistry
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:45212
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:25 Apr 2014 16:02
Last Modified:03 Oct 2019 06:28

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