1.3.1.33 C103S the BchN subunit variant shows 0.5% residual activity and is essentially inactive 687688 1.3.1.33 C104A no detectable effect on the import of protein to plastid and processing in darkness 676012 1.3.1.33 C166A no detectable effect on the import of protein to plastid and processing in darkness 676012 1.3.1.33 C195A mutant, constructed for the identification of the protochlorophyllide binding site 700943 1.3.1.33 C199/C226S mutant, mutation of the absolutely conserved cysteine residues 699004 1.3.1.33 C199S kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type 699004 1.3.1.33 C199S mutant, Cys199 has a relatively minor role in catalysis 699004 1.3.1.33 C199S/C226S kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 2fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type 699004 1.3.1.33 C21S the BchN subunit variant shows 0.5% residual activity and is essentially inactive 687688 1.3.1.33 C222A mutant, constructed for the identification of the protochlorophyllide binding site 700943 1.3.1.33 C226S kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) 4fold increased compared to wild-type 699004 1.3.1.33 C226S mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions 699004 1.3.1.33 C226S the formed protochlorophyllide species in C226S must differ compared to those formed in wild-type enzyme, for example, by attachment of the hydride at C18 rather than C17 762601 1.3.1.33 C276A decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C276 constitutes the protochlorophyllide binding site in the active centre of enzyme 676012 1.3.1.33 C276A the mutant is hypersensitive to high-light conditions during greening 741184 1.3.1.33 C303A decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C303 constitutes a low affinity protochlorophyllide binding site involved in assembly and stabilization of imported enzyme inside etioplasts 676012 1.3.1.33 C33A mutant, constructed for the identification of the protochlorophyllide binding site 700943 1.3.1.33 C37S kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) increased compared to wild-type, Kd (protochlorophyllide) equal to wild-type 699004 1.3.1.33 C37S mutant, Cys37 has a relatively minor role in catalysis 699004 1.3.1.33 C37S/C199S kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) comparable to wild-type 699004 1.3.1.33 C37S/C199S mutant, mutation of the absolutely conserved cysteine residues 699004 1.3.1.33 C37S/C199S/C226S kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type 699004 1.3.1.33 C37S/C199S/C226S mutant, mutation of the absolutely conserved cysteine residues 699004 1.3.1.33 C37S/C226S kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type 699004 1.3.1.33 C37S/C226S mutant, mutation of the absolutely conserved cysteine residues 699004 1.3.1.33 C46S the BchN subunit variant shows 0.5% residual activity and is essentially inactive 687688 1.3.1.33 C85A mutant, constructed for the identification of the protochlorophyllide binding site 700943 1.3.1.33 Cys303A the mutant is hypersensitive to high-light conditions during greening 741184 1.3.1.33 F233L mutant enzyme shows around 40% of wild-type activity 763023 1.3.1.33 F233Y mutant enzyme shows around 40% of wild-type activity 763023 1.3.1.33 F237Y as in the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is red-shifted by about 12 nm compared to free protochlorophyllide 763023 1.3.1.33 F240Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide 763023 1.3.1.33 F244Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide 763023 1.3.1.33 F247Y distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide 763023 1.3.1.33 G19A the mutant shows wild type value for turnover number 740894 1.3.1.33 H236A the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 H394A mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring 726394 1.3.1.33 K197A mutant, constructed for analysing the role of the conserved active site lysine 698913 1.3.1.33 K197Q mutant, constructed for analysing the role of the conserved active site lysine 698913 1.3.1.33 K197R mutant, constructed for analysing the role of the conserved active site lysine 698913 1.3.1.33 K42A the mutant shows wild type value for turnover number 740894 1.3.1.33 N149V the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 N39V the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 N90A the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 R321A inactive 740022 1.3.1.33 R38V the mutant shows wild type value for turnover number 740894 1.3.1.33 S16C the mutant shows wild type value for turnover number 740894 1.3.1.33 S189A the mutant shows wild type value for turnover number 740894 1.3.1.33 T145A the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 T147F the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 T147S the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 T230A the mutant shows wild type value for turnover number 740894 1.3.1.33 T230F the mutant shows reduced value for turnover number compared to the wild type enzyme 740894 1.3.1.33 T230S the mutant shows wild type value for turnover number 740894 1.3.1.33 T316A/T317A inactive 740022 1.3.1.33 Y189F mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue 696150 1.3.1.33 Y193A mutant, constructed for analysing the role of the conserved active site tyrosine 698913 1.3.1.33 Y193F mutant, constructed for analysing the role of the conserved active site tyrosine 698913 1.3.1.33 Y193S mutant, constructed for analysing the role of the conserved active site tyrosine 698913 1.3.1.33 Y94F the mutant shows wild type value for turnover number 740894