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

Content Provider	PubMed Central
Author	Linsky, Thomas Fast, Walter
Copyright Year	2010
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.
Related Links	http://dx.doi.org/10.1016/j.bbapap.2010.07.016
Ending Page	1953
Page Count	11
Starting Page	1943
File Format	PDF
ISSN	15709639
Journal	Biochimica et biophysica acta
Issue Number	10
Volume Number	1804
Language	English
Publisher Date	2010-10-01
Access Restriction	Open
Subject Keyword	Biophysics Analytical Chemistry Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Molecular Biology Biochemistry Biophysics

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