ABCC8 p.Asp96Ala
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PMID: 10908566
[PubMed]
Garinot-Schneider C et al: "Identification of essential amino acid residues in the Sinorhizobium meliloti glucosyltransferase ExoM."
No.
Sentence
Comment
40
We found that replacement of each of the three positions by alanine (D44A, D96A, and the newly identified D187A) abolished glucosyltransferase activity in vitro and resulted in the loss of the ability to restore succinoglycan production in an in vivo rescue assay.
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ABCC8 p.Asp96Ala 10908566:40:75
status: NEW143 Only the mutation of the conserved Asp, D96A, resulted in complete loss of activity.
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ABCC8 p.Asp96Ala 10908566:143:40
status: NEW162 The substitutions of the conserved aspartic acids, D44A, D96A, and D187A, which were expressed in E. coli but inactive in vitro, were expressed in S. meliloti and were also not able to restore succinoglycan production in vivo.
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ABCC8 p.Asp96Ala 10908566:162:57
status: NEW175 In vitro activity Succinoglycan production (%wt) %wt ExoM 100 100 Site I V42I 100 69 A43D 3 Ͼ3 D44Aa 0 Ͼ3 D44E 7 77 N45A NEb NE D46A 75 NE Site II F94V 69 77 L95A 30 114 D96A 0 7 D96E NE 41 D97A 15 115 D98A 26 139 E99A 100 84 Site III D187A 0 3 D187E 0 4 a The mutations involving conserved amino acid residues are in italics. b NE, not expressed.
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ABCC8 p.Asp96Ala 10908566:175:182
status: NEW