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26 kDa endochitinase from barley seeds: an interaction of the ionizable side chains essential for catalysis.
Ohnishi T, Juffer AH, Tamoi M, Skriver K, Fukamizo T. Ohnishi T, et al. Among authors: fukamizo t. J Biochem. 2005 Nov;138(5):553-62. doi: 10.1093/jb/mvi154. J Biochem. 2005. PMID: 16272567
The transition temperature of thermal unfolding (T(m)) of R215A was lower than that of the wild type protein by about 6.2 degrees C. ...A similar interaction network was previously found in chitosanase from Streptomyces sp. N174 [Fukamizo et al. (2000) J. Biol. Chem …
The transition temperature of thermal unfolding (T(m)) of R215A was lower than that of the wild type protein by about 6.2 degrees C. …
Hen-egg-white lysozyme modified with histamine. State of the imidazolylethyl group covalently attached to the binding site and its effect on the sugar-binding ability.
Fukamizo T, Hatta T, Goto S. Fukamizo T, et al. Eur J Biochem. 1995 Jul 1;231(1):56-64. Eur J Biochem. 1995. PMID: 7628485 Free article.
The chemical modification of Asp101 which is located at the upper end-most site (site A) of the binding cleft of hen egg white lysozyme affects the sugar residue binding of the midmost site (site C) in addition to that of site A, and results in the considerable decrease in the en …
The chemical modification of Asp101 which is located at the upper end-most site (site A) of the binding cleft of hen egg white lysozyme affe …
148 results