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Evolution of prokaryotic subtilases: Genome-wide analysis reveals novel subfamilies with different catalytic residues by Roland J. Siezen; Bernadet Renckens; Jos Boekhorst is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Subtilisin‐like serine proteases (subtilases) are a very diverse family of serine proteases with low sequence homology, often limited to regions surrounding the three catalytic residues. Starting with different Hidden Markov Models (HMM), based on sequence alignments around the catalytic residues of the S8 family (subtilisins) and S53 family (sedolisins), we iteratively searched all ORFs in the complete genomes of 313 eubacteria and archaea. In 164 genomes we identified a total of 567 ORFs with one or more of the conserved regions with a catalytic residue. The large majority of these contained all three regions around the “classical” catalytic residues of the S8 family (Asp‐His‐Ser), while 63 proteins were identified as S53 (sedolisin) family members (Glu‐Asp‐Ser). More than 30 proteins were found to belong to two novel subsets with other evolutionary variations in catalytic residues, and new HMMs were generated to search for them. In one subset the catalytic Asp is replaced by an equivalent Glu (i.e. Glu‐His‐Ser family). The other subset resembles sedolisins, but the conserved catalytic Asp is not located on the same helix as the nucleophile Glu, but rather on a β‐shee

Who reads Evolution of prokaryotic subtilases: Genome-wide analysis reveals novel subfamilies with different catalytic residues?

Author

Roland J. Siezen; Bernadet Renckens; Jos Boekhorst

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)