@article {1017,
	title = {Substrate specificity and kinetic framework of a DNAzyme with an expanded chemical repertoire: a putative RNaseA mimic that catalyzes RNA hydrolysis independent of a divalent metal cation},
	journal = {Nucleic Acids Research},
	volume = {32},
	number = {22},
	year = {2004},
	note = {ISI Document Delivery No.: 887METimes Cited: 24Cited Reference Count: 71},
	pages = {6660-6672},
	type = {Article},
	abstract = {This work addresses the binding, cleavage and dissociation rates for the substrate and products of a synthetic RNaseA mimic that was combinatorially selected using chemically modified nucleoside triphosphates. This trans-cleaving DNAzyme, 9(25)-11t, catalyzes sequence-specific ribophosphodiester hydrolysis in the total absence of a divalent metal cation, and in low ionic strength at pH 7.5 and in the presence of EDTA. It is the first such sequence capable of multiple turnover. 9(25)-11t consists of 31 bases, 18 of which form a catalytic domain containing 4 imidazole and 6 allylamino modified nucleotides. This sequence cleaves the 15 nt long substrate, S1, at one embedded ribocytosine at the eighth position to give a 5{\textquoteright}-product terminating in a 2{\textquoteright},3{\textquoteright}-phosphodiester and a 3{\textquoteright}-product terminating in a 5{\textquoteright}-OH. Under single turnover conditions at 24degreesC, 9(25)-11t displays a maximum first-order rate constant, k(cat), of 0.037 min(-1) and a catalytic efficiency, k(cat)/K-m, of 5.3 x 10(5) M-1 min(-1). The measured value of k(cat) under catalyst excess conditions agrees with the value of k(cat) observed for steady-state multiple turnover, implying that slow product release is not rate limiting with respect to multiple turnover. The substrate specificity of 9(25)-11t was gauged in terms of k(cat) values for substrate sequence variants. Base substitutions on the scissile ribose and at the two bases immediately downstream decrease k(cat) values by a factor of 4 to 250, indicating that 9(25)-11t displays significant sequence specificity despite the lack of an apparent Watson-Crick base-pairing scheme for recognition.},
	keywords = {CATIONS, CLEAVING DNA ENZYME, CYTOSOLIC FREE MAGNESIUM, HAIRPIN RIBOZYME CLEAVAGE, HAMMERHEAD, IMIDAZOLYL FUNCTIONALITIES, IN-VITRO SELECTION, MONOVALENT, NUCLEIC-ACIDS, NUCLEOSIDE TRIPHOSPHATES, SEQUENCE-SPECIFIC CLEAVAGE},
	isbn = {0305-1048},
	url = {<Go to ISI>://000226309400036},
	author = {Ting, R. and Thomas, J. M. and Lermer, L. and Perrin,David M.}
}
@article {430,
	title = {Toward an RNaseA mimic: a DNAzyme with imidazoles and cationic amines},
	journal = {Journal of the American Chemical Society},
	volume = {124},
	number = {34},
	year = {2002},
	note = {ISI Document Delivery No.: 586GJTimes Cited: 41Cited Reference Count: 52},
	month = {Aug},
	pages = {9960-9961},
	type = {Article},
	keywords = {CATALYTIC REPERTOIRE, CATIONS, CLEAVING DNA ENZYME, FUNCTIONALITIES, HAMMERHEAD, IN-VITRO SELECTION, MONOVALENT, NUCLEIC-ACIDS, RIBOZYME, SEQUENCE-SPECIFIC CLEAVAGE, SITE-SPECIFIC CLEAVAGE},
	isbn = {0002-7863},
	url = {<Go to ISI>://000177576000001},
	author = {Lermer, L. and Roupioz, Y. and Ting, R. and Perrin,David M.}
}
