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FOR THE RECORD

Peptidase family U34 belongs to the superfamily of N-terminal nucleophile hydrolases

¹ Howard Hughes Medical Institute,
² Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA

Reprint requests to: Nick V. Grishin, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390, USA; e-mail: grishin{at}chop.swmed.edu; fax: (214) 648-9099.

Peptidase family U34 consists of enzymes with unclear catalytic mechanism, for instance, dipeptidase A from Lactobacillus helveticus. Using extensive sequence similarity searches, we infer that U34 family members are homologous to penicillin V acylases (PVA) and thus potentially adopt the N-terminal nucleophile (Ntn) hydrolase fold. Comparative sequence and structural analysis reveals a cysteine as the catalytic nucleophile as well as other conserved residues important for catalysis. The PVA/U34 family is variable in sequence and exhibits great diversity in substrate specificity, to include enzymes such as choloyglycine hydrolases, acid ceramidases, isopenicillin N acyltransferases, and a subgroup of eukaryotic proteins with unclear function.

Keywords: Peptidase family U34; penicillin V acylase; Ntn-hydrolase; structure prediction; peptidase classification

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