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PEPD gene

Known as: PEPD, PROLIDASE, IMIDODIPEPTIDASE 
 
National Institutes of Health

Papers overview

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Review
2008
Review
2008
Prolidase [EC.3.4.13.9] is a cytosolic imidodipeptidase, which specifically splits imidodipeptides with C-terminal proline or… Expand
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Highly Cited
2006
Highly Cited
2006
The purpose of this study was to determine serum oxidative/antioxidative status in patients with knee osteoarthritis and its… Expand
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Review
1999
Review
1999
Enzymes catalyzing the hydrolysis of highly toxic organophosphorus compounds (OPs) are classified as organophosphorus acid… Expand
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Highly Cited
1997
Highly Cited
1997
Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C‐terminal proline or… Expand
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Highly Cited
1994
Highly Cited
1994
Amino acid sequence comparison suggests that the structure of Escherichia coli methionine aminopeptidase (EC 3.4.11.18) and the C… Expand
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Highly Cited
1989
Highly Cited
1989
Complementary DNA clones of prolidase (imidodipeptidase, EC 3.4.13.9) were isolated from human liver and placental cDNA libraries… Expand
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Highly Cited
1984
Highly Cited
1984
We describe here an easy method of determining prolidase (EC 3.4.13.9) in plasma after preincubation with Mn2+ for 24 h at 37… Expand
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Highly Cited
1982
Highly Cited
1982
Prolidase assay was reinvestigated by determining proline, using Chinard's method. Although several authors had previously tested… Expand
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Highly Cited
1975
Highly Cited
1975
A 39-month-old girl was found to have a genetic deficiency of prolidase. This enzyme specifically splits dipeptides with proline… Expand
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Highly Cited
1962
Highly Cited
1962
The strong acids that are required for complete hydrolysis of proteins destroy some amino acids, such as tryptophan, asparagine… Expand
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