Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.
Tanaka J, Fukamizo T, Ohnuma T.
Tanaka J, et al. Among authors: ohnuma t.
Glycobiology. 2017 May 1;27(5):477-485. doi: 10.1093/glycob/cwx016.
Glycobiology. 2017.
PMID: 28204489
From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degre …
From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic re …