Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog.
Leonard PM, Grogan G.
Leonard PM, et al. Among authors: grogan g.
J Biol Chem. 2004 Jul 23;279(30):31312-7. doi: 10.1074/jbc.M403514200. Epub 2004 May 11.
J Biol Chem. 2004.
PMID: 15138275
Free article.
We have previously reported the structure of OCH (Whittingham, J. L., Turkenburg, J. P., Verma, C. S., Walsh, M. A., and Grogan, G. (2003) J. Biol. Chem. 278, 1744-1750), which suggested the involvement of five residues, His-45, His-122, His-145, Asp-154, and Glu-24 …
We have previously reported the structure of OCH (Whittingham, J. L., Turkenburg, J. P., Verma, C. S., Walsh, M. A., and Grogan, G …