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Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily.

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.

SUBMITTER: Linsky T

PROVIDER: S-EPMC4104755 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily.

Linsky Thomas T Fast Walter W

Biochimica et biophysica acta 20100721 10

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 ...[more]

PMID: 20654741

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