Abstract
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.
Original language | English (US) |
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Pages (from-to) | 1131-1135 |
Number of pages | 5 |
Journal | Protein Science |
Volume | 12 |
Issue number | 5 |
DOIs | |
State | Published - May 1 2003 |
Keywords
- Ntn-hydrolase
- Penicillin V acylase
- Peptidase classification
- Peptidase family U34
- Structure prediction
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology