|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Supersedes EC number: 220.127.116.11
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: prolyl aminopeptidase
Enzyme Commission Synonyms: proline aminopeptidase, Pro-X aminopeptidase, cytosol aminopeptidase V, proline iminopeptidase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 74.62598 [Latendresse13]
Enzyme Commission Summary:
This enzyme catlayzes Release of N-terminal proline from a peptide.
A Mn2+-requiring enzyme present in the cytosol of mammalian and microbial cells. In contrast to the mammalian form, the bacterial form of the enzyme (type example of peptidase family S33) hydrolyses both polyproline and prolyl-2-naphthylamide. The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 18.104.22.168, leucyl aminopeptidase.
Unification Links: KEGG:R00135
Relationship Links: BRENDA:EC:22.214.171.124, ENZYME:EC:126.96.36.199, IUBMB-ExplorEnz:EC:188.8.131.52, UniProt:RELATED-TO:O32449, UniProt:RELATED-TO:P23974, UniProt:RELATED-TO:P28839, UniProt:RELATED-TO:P42786, UniProt:RELATED-TO:P46542, UniProt:RELATED-TO:P46547, UniProt:RELATED-TO:P47266, UniProt:RELATED-TO:P75092, UniProt:RELATED-TO:P94800, UniProt:RELATED-TO:P96084, UniProt:RELATED-TO:Q9JUV1, UniProt:RELATED-TO:Q48570
Nordwig73: Nordwig A, Mayer H (1973). "The cleavage of prolyl peptides by kidney peptidases. Detection of a new peptidase capable of removing N-terminal proline." Hoppe Seylers Z Physiol Chem 354(4);380-3. PMID: 4803482
Turzynski90: Turzynski A, Mentlein R (1990). "Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase." Eur J Biochem 190(3);509-15. PMID: 2373079
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