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- W2014568456 endingPage "1953" @default.
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- W2014568456 abstract "The pentein superfamily is a mechanistically diverse superfamily encompassing both noncatalytic proteins and enzymes that catalyze hydrolase, dihydrolase and amidinotransfer reactions on guanidine substrates. Despite generally low sequence identity, they possess a conserved structural fold and display common mechanistic themes in catalysis. The structurally characterized catalytic penteins possess a conserved core of residues that include a Cys, His and two polar, guanidine-binding residues. All known catalytic penteins use the core Cys to attack the substrate's guanidine moiety to form a covalent thiouronium adduct and all cleave one or more of the guanidine C--N bonds. The mechanistic information compiled to date supports the hypothesis that this superfamily may have evolved divergently from a catalytically promiscuous ancestor." @default.
- W2014568456 created "2016-06-24" @default.
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- W2014568456 creator A5043373111 @default.
- W2014568456 date "2010-10-01" @default.
- W2014568456 modified "2023-10-16" @default.
- W2014568456 title "Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily" @default.
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- W2014568456 doi "https://doi.org/10.1016/j.bbapap.2010.07.016" @default.
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