ABSTRACT
[...]heme-copper oxidases from Rhodobacter sphaeroides underwent single amino acid substitutions, including N139D, which resulted in the elimination of proton pumping activity and an increase in steady-state activity rather than an inhibitory effect (Pawate et al. 2002). [...]ACC deaminase must begin the cyclopropane ring opening reaction without the availability of an R-carbanionic intermediate. [...]ACC deaminase from Pseudomonas sp. Site-specific docking with ACC was performed for each mutated structure, and the T199S mutant produced binding energy of -4.3 kcal/mol, whereas the E295G mutant was found to have a binding energy of -4.9 kcal/mol. [...]the E295G mutant, in which glutamic acid is substituted with glycine at the 295th position, was chosen