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- Author:
- Isupov, Michail N., et al. ; Urusova, Darya V.; Antonyuk, Svetlana; Kachalova, Galina S.; Obmolova, Galina; Vagin, Alexei A.; Lebedev, Andrey A.; Burenkov, Gleb P.; Dauter, Zbigniew; Bartunik, Hans D.; Lamzin, Victor S.; Melik-Adamyan, William R.; Mueller, Thomas D.; Schnackerz, Klaus D.; Show all 14 Authors
- Source:
- Biochimica et biophysica acta 2012 v.1824 no.3 pp. 422-432
- ISSN:
- 1878-1454
- Subject:
- Escherichia coli; active sites; ammonia; catalytic activity; crystal structure; data collection; hydrogen bonding; models; oxygen; pyridoxal; pyruvic acid; schiff bases; serine dehydratase
- Abstract:
- ... D-Serine dehydratase from Escherichia coli is a member of the β-family (fold-type II) of the pyridoxal 5′-phosphate-dependent enzymes, catalyzing the conversion of D-serine to pyruvate and ammonia. The crystal structure of monomeric D-serine dehydratase has been solved to 1.97Å-resolution for an orthorhombic data set by molecular replacement. In addition, the structure was refined in a monoclinic ...
- DOI:
- 10.1016/j.bbapap.2011.10.017
-
http://dx.doi.org/10.1016/j.bbapap.2011.10.017