A multinuclear NMR study of the active site of an endoglucanase from a strain of Bacillus. Use of Trp residues as structural probes.
Kawaminami S, Takahashi H, Ito S, Arata Y, Shimada I.
Kawaminami S, et al.
J Biol Chem. 1999 Jul 9;274(28):19823-8. doi: 10.1074/jbc.274.28.19823.
J Biol Chem. 1999.
PMID: 10391926
Free article.
In the hydrolytic reaction catalyzed by an endoglucanase from a Bacillus strain (endoglucanase K), 2 of 12 Trp residues, Trp174 and Trp243, are responsible for binding of the substrate and/or for the catalysis (Kawaminami, S., Ozaki, K., Sumitomo, N., Hayashi, Y., I …
In the hydrolytic reaction catalyzed by an endoglucanase from a Bacillus strain (endoglucanase K), 2 of 12 Trp residues, Trp174 and Trp243, …