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J. Biol. Chem., Vol. 277, Issue 52, 51084, December 27, 2002

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Detailed kinetic analysis and identification of the nucleophile in -L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase.

Page 43670: In the right column, 15 lines from the bottom, the words "poor" and "better" should be interchanged. The correct sentences should read: "From Fig. 4a, it seems that, for the E175A acid-base mutant, with substrates bearing better leaving groups (pK_a < 6), the rate-limiting step is also the deglycosylation step. However, for substrates with poor leaving group ability (higher pK_a), a much greater dependence of the k_cat values on the leaving group ability of the substrate was observed, with a _1g value of 0.9."

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Shallom, D. Articles by Shoham, Y. Search for Related Content PubMed Articles by Shallom, D. Articles by Shoham, Y. Social Bookmarking                      What's this?