ABCC8 p.Ser405Asn

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PMID: 21543331 [PubMed] Triboulet S et al: "Inactivation kinetics of a new target of beta-lactam antibiotics."
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61 Derivatives of pET2818 containing the same portion of the ldtfm gene with mutations leading to G430S, S405N, or both amino acid substitutions were constructed as described in the supplemental "Experimental Procedures".
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ABCC8 p.Ser405Asn 21543331:61:102
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152 Identification of Amino Acid Substitutions in Ldtfm-Sequencing the ldtfm gene of mutant S11 revealed two point mutations that led to amino acid substitutions S405N and G430S, both located in the catalytic domain of the LD-transpeptidase (supplemental Fig. S3).
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ABCC8 p.Ser405Asn 21543331:152:158
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153 Sequencing of ldtfm from the intermediary mutants showed that the two mutations appeared sequentially at the eighth (S405N) and 11th (G430S) selection steps.
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ABCC8 p.Ser405Asn 21543331:153:117
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154 Substitution S405N is located at the entrance of the catalytic cavity in the loop connecting sheets beta13 to beta14.
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ABCC8 p.Ser405Asn 21543331:154:13
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157 Kinetics of Inactivation of LD-Transpeptidases from Mutants Resistant to Imipenem-In order to analyze the impact of substitutions G430S and S405N on the catalytic constants, we constructed and purified derivatives of Ldtfm harboring these two substitutions alone or in combination.
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ABCC8 p.Ser405Asn 21543331:157:140
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174 The second substitution, S405N alone, caused moderate decreases in kinact (from 4.5 to 1.6 min-1 ) and k1 (from 0.065 to 0.030 ␮M -1 min-1 ).
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ABCC8 p.Ser405Asn 21543331:174:25
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176 Impact of amino acid substitutions S405N and G430S on the kinetics of Ldtfm inactivation by imipenem.
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ABCC8 p.Ser405Asn 21543331:176:35
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223 A decrease in the efficiency of enzyme acylation was expected to result in increased resistance to imipenem, and this possibility was explored by selecting mutant S11 and analyzing the impact of substitutions S405N and G430S on the kinetics of Ldtfm inactivation (Fig. 7).
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ABCC8 p.Ser405Asn 21543331:223:209
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