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

Jimin Pei, Nick V. Grishin

Research output: Contribution to journalArticle

24 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1131-1135
Number of pages5
JournalProtein Science
Volume12
Issue number5
DOIs
StatePublished - May 1 2003

Fingerprint

Penicillin Amidase
Acid Ceramidase
Peptide Hydrolases
Lactobacillus helveticus
Nucleophiles
Hydrolases
Enzymes
Substrate Specificity
Catalysis
Structural analysis
Cysteine
Sequence Analysis
Substrates
Proteins
N-terminal nucleophile hydrolase

Keywords

  • Ntn-hydrolase
  • Penicillin V acylase
  • Peptidase classification
  • Peptidase family U34
  • Structure prediction

ASJC Scopus subject areas

  • Biochemistry

Cite this

Peptidase family U34 belongs to the superfamily of N-terminal nucleophile hydrolases. / Pei, Jimin; Grishin, Nick V.

In: Protein Science, Vol. 12, No. 5, 01.05.2003, p. 1131-1135.

Research output: Contribution to journalArticle

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