Structural highlights
Function
HISX_BRUSU Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity).
Publication Abstract from PubMed
l-histidinol dehydrogenase from Brucella suis (BsHDH) is an enzyme involved in the histidine biosynthesis pathway which is absent in mammals, thus representing a very interesting target for the development of anti-Brucella agents. In this paper we report the crystallographic structure of a mutated form of BsHDH both in its unbound form and in complex with a nanomolar inhibitor. These studies provide the first structural background for the rational design of potent HDH inhibitors, thus offering new hints for clinical applications.
Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis.,D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Kohler S, Ascione G, Monti SM, Winum JY, De Simone G Biochimie. 2013 Oct 17. pii: S0300-9084(13)00349-0. doi:, 10.1016/j.biochi.2013.09.028. PMID:24140957[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Kohler S, Ascione G, Monti SM, Winum JY, De Simone G. Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. Biochimie. 2013 Oct 17. pii: S0300-9084(13)00349-0. doi:, 10.1016/j.biochi.2013.09.028. PMID:24140957 doi:http://dx.doi.org/10.1016/j.biochi.2013.09.028
