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- Totsuka, A.; Fukazawa, C.
- European journal of biochemistry 1996 v.240 no.3 pp. 655-659
- triose-phosphate isomerase, etc ; X-ray diffraction; active sites; beta-amylase; binding capacity; essential amino acids; mechanism of action; mutants; site-directed mutagenesis; soybeans; starch; Show all 11 Subjects
- ... Soybean beta-amylase, comprising a (beta/alpha)8-barrel core with a mobile loop, similar to that of triose phosphate isomerase, was mutated by site-directed mutagenesis at residues Glu380 and Leu383. X-ray crystallographic findings suggest that Glu380 is the counterpart of the catalytic site (Glu186) and that Leu383, located near the active-site cavity, forms an inclusion complex with cyclomaltohe ...