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Proline iminopeptidase

Known as: proline-imino-peptidase, cytosol aminopeptidase V, proline aminopeptidase 
National Institutes of Health

Papers overview

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2008
2008
X-prolyl aminopeptidases catalyze the removal of a penultimate prolyl residue from the N termini of peptides. Mammalian X-prolyl… 
Highly Cited
2007
Highly Cited
2007
Expression of bacterial genes is often regulated by complex mechanisms, some of which involve host cues. Analysis of the… 
Review
2000
Review
2000
  • M. Holmquist
  • Current protein & peptide science
  • 2000
  • Corpus ID: 12138269
The alpha/beta-hydrolase fold family of enzymes is rapidly becoming one of the largest group of structurally related enzymes with… 
Highly Cited
1998
Highly Cited
1998
The proline iminopeptidase from Xanthomonas campestris pv. citri is a serine peptidase that catalyses the removal of N‐terminal… 
Highly Cited
1994
Highly Cited
1994
The gene for proline iminopeptidase from Lactobacillus delbrueckii subsp. lactis DSM 7290 coding for an enzyme that hydrolyses… 
Highly Cited
1994
Highly Cited
1994
The proline iminopeptidase (PepIP) of Lactobacillus delbrueckii subsp. bulgaricus is a major peptidase located in the cell… 
Review
1993
Review
1993
  • S. Hillier
  • American journal of obstetrics and gynecology
  • 1993
  • Corpus ID: 28589731
Highly Cited
1984
Highly Cited
1984
  • F. Exterkate
  • Applied and environmental microbiology
  • 1984
  • Corpus ID: 31737547
Peptidase activity determinations involving native cells of Streptococcus cremoris and completely disrupted cell preparations, as… 
1983
1983
Proline iminopeptidase [EC 3.4.11.5] was purified about 1,700-fold from cell free extract of Bacillus megaterium by a series of…