A practical approach for computing the active site of the ribonucleoside hydrolase of E. coli encoded by rihC.
We predict the potential active and catalytic sites, the transition state and how it is stabilized, and the mechanism of rihC ribonucleoside hydrolase of E. coli. Our approach is based on well-known primary sequence analysis techniques. A canonically associated extreme value distribution is used to assess the significance of the prediction. Parameters for the extreme value distribution are computed directly from data. Our practical approach is consistent with known results in the literature. We obtain BLOSUM matrices in a way that is intrinsically tied to the data base, and we employ user-friendly techniques that should be applicable to a range of medically significant scenarios.
Farone
Anthony
A
Middle Tennessee State University, Murfreesboro, Tennessee 37132, USA. afarone@mtsu.edu
Farone
Mary
M
Kline
Paul
P
Quinn
Terrance
T
Sinkala
Zachariah
Z
D000465:Algorithms; D020134:Catalytic Domain / Q000235:genetics; D019295:Computational Biology; D016831:Crithidia fasciculata / Q000201:enzymology / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics*; D005798:Genes, Bacterial; D009699:N-Glycosyl Hydrolases / Q000737:chemistry* / Q000235:genetics*; D020539:Sequence Analysis, Protein / Q000706:statistics & numerical data*
D029968:Escherichia coli Proteins; D009699:N-Glycosyl Hydrolases; C422989:RihC protein, E coli; C096466:inosine-uridine hydrolase