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Example sentences for: asn
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The substrate-binding model showed that Tyr228 in L1 was position-conserved with Asn233 in the other crystallographically characterized metallo-β-lactamases [ 37 42 44 45 46 ] . Spencer and coworkers postulated that Tyr228 is part of an oxyanion hole that interacts with the β-lactam carbonyl on substrate and helps to stabilize the putative tetrahedral intermediate formed during substrate turnover [ 37 ] . To test this hypothesis, Tyr228 was changed to an alanine and to a phenylalanine to afford the Y228A and Y228F mutants, respectively.
The middle histidine of the histidine triad (His96 in human Fhit), which is critical for hydrolysis of ApppA by Fhit [ 14 16 ] , is not necessary for tumor suppression [ 17 18 ] . Nonetheless, wild-type and His96Asn forms of Fhit are saturated by ApppA in the low micromolar range and form stable complexes with non-hydrolyzable ApppA in which two ApppA analogs are bound per Fhit dimer and all phosphates cluster on one surface of the protein [ 16 ] . These observations suggested that Fhit-substrate complexes may be the active, signaling form of Fhit and that the function of the catalytically essential histidine may be to terminate the lifetime of signaling complexes [ 16 ] .
Two-thirds of all sequenced metallo-β-lactamases have an Asn at position 233 [ 41 ] , and this residue was predicted [ 42 ] and shown [ 43 ] to be involved with substrate binding and activation by interacting electrostatically with the substrate β-lactam carbonyl.
Asp or Asn is usually found at X and Y; Asp, Asn, or Ser at Z; a variety of residues at -Y; usually Asp, Asn, or Ser at -X, but this position is more variable; and usually Glu at -Z [ 11].
Mutation of Asn122 to Asp by site-directed mutagenesis destroyed the phosphatase activity, confirming the essential role of this residue of PP1 in catalysis [ 19 ] . PfPP1 was inhibited by NaF, inorganic orthophosphate, and pyrophosphate at respective IC 50 values of 2.5 mM, 10 mM, and 90 μM (data not shown).
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