Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad
S Shin, YS Yun, HM Koo, YS Kim, KY Choi… - Journal of Biological …, 2003 - ASBMB
Amidase signature family enzymes, which are widespread in nature, contain a newly
identified Ser-cisSer-Lys catalytic triad in which the peptide bond between Ser 131 and the
preceding residue Gly 130 is in a cis configuration. In order to characterize the property of
the novel triad, we have determined the structures of five mutant malonamidase E2 enzymes
that contain a Cys-cisSer-Lys, Ser-cisAla-Lys, or Ser-cisSer-Ala triad or a substitution of Gly
130 with alanine. Cysteine cannot replace the role of Ser 155 due to a hyper-reactivity of the …
identified Ser-cisSer-Lys catalytic triad in which the peptide bond between Ser 131 and the
preceding residue Gly 130 is in a cis configuration. In order to characterize the property of
the novel triad, we have determined the structures of five mutant malonamidase E2 enzymes
that contain a Cys-cisSer-Lys, Ser-cisAla-Lys, or Ser-cisSer-Ala triad or a substitution of Gly
130 with alanine. Cysteine cannot replace the role of Ser 155 due to a hyper-reactivity of the …
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