ABCD1 p.Ala61Val
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PMID: 19521995
[PubMed]
Ohki T et al: "Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a beta-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolase."
No.
Sentence
Comment
47
Plasmid pS1M77 was found to encode the enzyme (Hyb-24 A61V/A253T/F264C/D370Y) (designated as Hyb-S1M77) with the highest Ald-hydrolytic activity among the 350 clones in the first-cycle pS1M mutant library [Fig. 2(b)].17 The plasmids pS1M164, pS1M197, pS1M258, and pS1M259 were found to produce enzymes having the second to fifth highest activity.
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ABCD1 p.Ala61Val 19521995:47:54
status: NEW54 Nucleotide sequencing of the 1.4 kb EcoRI/HindIII-fragment encoding the nylB/nylB0 region in pS4M94 revealed that the mutant enzyme (Hyb-S4M94) had six amino acid alterations (A61V, A124V, R187S, F264C, G291R, and G338A) in addition to the D370Y mutation.
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ABCD1 p.Ala61Val 19521995:54:176
status: NEW76 X-ray crystallographic analysis To analyze the structural basis for the increased activities, we determined the substrate-bound and unbound crystal structures of Hyb-24Y and Hyb-S4M94 by X-ray crystallographic analysis at resolutions of 1.501.58 A˚ (Supporting Information Table S3) and compared the structures with that of Hyb-24DN, which had been solved previously.9 In the three-dimensional structure model of Hyb-S4M94, three of the substitutions (R187S/F264C/D370Y) are located in the catalytic cleft, whereas three others (A61V/G291R/G338A) are located on the surface, and the remaining one (A124V) is located on the inside of the protein molecule [Fig. 4(a)].
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ABCD1 p.Ala61Val 19521995:76:535
status: NEW109 Among the seven alterations differing between Hyb-24 and Hyb-S4M94, three (R187S/F264C/D370Y) were able to effectively increase the Ald-hydrolytic activity and are shown in blue, whereas the remaining four (A61V, A124V, G291R, and G338A) are shown in purple.
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ABCD1 p.Ala61Val 19521995:109:207
status: NEW
PMID: 16949580
[PubMed]
Ohki T et al: "Mutational analysis of 6-aminohexanoate-dimer hydrolase: relationship between nylon oligomer hydrolytic and esterolytic activities."
No.
Sentence
Comment
86
HPLC analysis revealed that the specific activity for Ald-hydrolysis was increased approximately ten-fold in two clones, pR1M9 (containing a single G181D substitution) and pS1M77 (containing A61V, A253T, F264C and D370Y substitutions) (Fig. 3).
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ABCD1 p.Ala61Val 16949580:86:191
status: NEW84 HPLC analysis revealed that the specific activity for Ald-hydrolysis was increased approximately ten-fold in two clones, pR1M9 (containing a single G181D substitution) and pS1M77 (containing A61V, A253T, F264C and D370Y substitutions) (Fig. 3).
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ABCD1 p.Ala61Val 16949580:84:191
status: NEW