2.8.1.6 C128A no enzyme activity 645607 2.8.1.6 C128A reduced cysteine desulfurase activity 645609 2.8.1.6 C128A reduced enzyme activity 645602 2.8.1.6 C188A cysteine desulfurase activity is reduced to 70% of the wild-type activity 645609 2.8.1.6 C188A no enzyme activity 645607 2.8.1.6 C188A reduced enzyme activity 645602 2.8.1.6 C188S enzyme is insoluble 645606 2.8.1.6 C276A normal enzyme activity 645602 2.8.1.6 C288A normal enzyme activity 645602 2.8.1.6 C288T normal enzyme activity 645606 2.8.1.6 C53A inactive, but still exhibits UV-visible spectrum of a [Fe2-S2] cluster similar to that of the wild-type enzyme 645604 2.8.1.6 C53A no enzyme activity 645602, 645607 2.8.1.6 C53S no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster 645606 2.8.1.6 C57A inactive, but still exhibits UV-visible spectrum of a [Fe2-S2] cluster similar to that of the wild-type enzyme 645604 2.8.1.6 C57A no enzyme activity 645602, 645607 2.8.1.6 C57S no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster 645606 2.8.1.6 C60A inactive, but still exhibits UV-visible spectrum of a [Fe2-S2] cluster similar to that of the wild-type enzyme 645604 2.8.1.6 C60A no enzyme activity 645602, 645607 2.8.1.6 C60S no enzyme activity, spectrum shows no peak indicative of the presence of an [Fe-S] cluster 645606 2.8.1.6 C97A no enzyme activity 645602, 645607 2.8.1.6 C97A reduced cysteine desulfurase activity 645609 2.8.1.6 D155A mutation in the conserved YNHNLD sequence 702042 2.8.1.6 D155A mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 D155A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical 672076 2.8.1.6 D155E mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 D155N mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 D155S mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 H152A about 10% of turnover rate of wild-type. Ratio of 5’-deoxyadenosine to biotin is about twice as high as in wild-type 672076 2.8.1.6 H152A mutation in the conserved YNHNLD sequence 702042 2.8.1.6 additional information Fe/S cluster assembly of biotin synthase strongly depends on Isu1 and Isu2 proteins. Proteins Isa1 and Isa2 are crucial for in vivo function of biotin synthase but not for de novo synthesis of its Fe/S clusters -, 673421 2.8.1.6 additional information integration of BIO2 enzyme gene into chromosome under strong promoter. Biotin yield of system reaches 100fold above wild-type. Biotin production is not stable if the selection pressure is removed 671522 2.8.1.6 N151A mutation in the conserved YNHNLD sequence 702042 2.8.1.6 N151A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical 672076 2.8.1.6 N153A mutation in the conserved YNHNLD sequence 702042 2.8.1.6 N153A mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 N153A no enzymic activity, mutant is unable to cleave S-adenosyl-l-methionine and to produce the deoxyadenosyl radical 672076 2.8.1.6 N153D mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 N153Q mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 N153S inactive for biotin production, enzyme can bind AdoMet and DTB and can convert DTB to 9-mercaptodethiobiotin, the majority of 9- mercaptodethiobiotin is released into the buffer and not bound to the enzyme, suggesting that dissociation of 9- mercaptodethiobiotin is faster than the second half reaction for biotin formation 691001 2.8.1.6 N153S mutation in the highly conserved sequence motif, YNHNLD, in which Asn153 und Asp155 form hydrogen bonds with the ribose hydroxyl groups of AdoMet 702281 2.8.1.6 P24A/R44Q linked SNPs, residues A24 and Q44 constitute the virulent allele pair, P24 and R44 the avirulent allele pair 761716 2.8.1.6 R260A contains 1.8 iron atoms per monomer, slightly less active than wild-type 672097 2.8.1.6 R260C contains 2.0 iron atoms per monomer, slightly more active than wild-type 672097 2.8.1.6 R260H contains 1.3 iron atoms per monomer, slightly less active than wild-type 672097 2.8.1.6 R260M contains 1.1 iron atoms per monomer, about 30% of wild-type activity 672097