Effects of Site-Directed Mutagenesis of the Loop Residue of the N-Terminal Domain Gly117 of Thermolysin on Its Catalytic Activity

Effects of Mutations of Thermolysin, Asn116 to Asp and Asp150 to Glu, on Salt-Induced Activation and Stabilization

“…[10][11][12][13][14][15] Mutation Asp150!Glu increases activity. 18) In this study, this mutation reduced NaCl-induced activation (Fig. 3), indicating that salt-induced activation is replaced by Asp150!Glu to some extent.…”

“…12) We have identified several mutations that increase the hydrolytic activity for FAGLA and ZDFM. [16][17][18][19] Of such mutations, Asn116!Asp 19) (here the mutation of Asn116 to Asp is designated as Asn116!Asp, and the thermolysin variant bearing the mutation of Asn116! Asp as N116D) and Asp150!Glu 17) exhibited the strongest effects.…”

Effects of Conversion of the Zinc-Binding Motif Sequence of Thermolysin, HEXXH, to That of Dipeptidyl Peptidase III, HEXXXH, on the Activity and Stability of Thermolysin

“…Expression of thermolysin variants in E. coli was carried out as described previously. 20,21) Briefly, the mature sequence of thermolysin containing the pelB leader sequence at its N-terminus and the pre-prosequence of thermolysin were expressed in JM109 cells.…”

Effects of Mutations of Lys41 and Asp102 of Bacteriorhodopsin

“…7,[24][25][26] It has been found that carboxylic residues in the proton-conducting cytoplasmic and extracellular half-channels, D96, D85, E194, and E204 are involved in the photocycle and proton transfer. Negatively charged D85 is part of the counterion to the protonated Schiff base and proton acceptor.…”