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Literature summary for 3.4.21.B28 extracted from

  • Jambunathan, K.; Watson, D.S.; Endsley, A.N.; Kodukula, K.; Galande, A.K.
    Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha (2012), FEBS Lett., 586, 2507-2512.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B28

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by Z-Pro-prolinal Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane a type II integral membrane serine protease Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens a post-proline cleaving serine peptidase ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q12844
-
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelial carcinoma cell
-
 Homo sapiens
-
additional information the enzyme is not expressed in normal adult tissues, but is highly expressed on stromal fibroblasts in virtually all epithelial carcinomas and on tumor cells of some sarcomas Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha2-antiplasmin + H2O
-
 Homo sapiens ?
-
 ?
GASGPAGPA + H2O
-
 Homo sapiens GASGP + AGPA
-
 ?
Gelatin + H2O
-
 Homo sapiens ?
-
 ?
GEPGPPGPA + H2O
-
 Homo sapiens GEP + GPPGP + L-Ala
-
 ?
GFSPFQRED + H2O low activity Homo sapiens ?
-
 ?
GTAGPNQEQE + H2O
-
 Homo sapiens GTAGP + NQEQE
-
 ?
GTSGPNQEQE + H2O
-
 Homo sapiens GTSGP + NQEQE
-
 ?
additional information a post-proline cleaving serine peptidase Homo sapiens ?
-
 ?
additional information the enzyme exhibits post-proline cleaving dipeptidyl peptidase and endopeptidase activity toward gelatin and alpha2-antiplasmin. Substrate specificity analysis using a internally quenched fluorogenic probes library for screening, overview. The sequence Pro-Tyr-Asp is strongly cleaved by the enzyme, sequence specificity, detailed overview Homo sapiens ?
-
 ?
RPKPQQFFGLM + H2O the substance P-derived sequence is cleaved although it does not contain Gly-Pro Homo sapiens RPKP + L-Gln-L-Gln + FFGLM
-
 ?

Synonyms

Synonyms Comment Organism
FAP
-
 Homo sapiens
fibroblast activation protein alpha
-
 Homo sapiens
seprase
-
 Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme exhibits similar substrate specificity and properties compared to prolyl oligopeptidase, EC 3.4.21.26, the latter is specifically inhibited by Z-Pro-prolinal, while the fibroblast activation protein alpha is not. In contrast to prolyl oligopeptidase, fibroblast activation protein alpha is not expressed in normal adult tissues. Substrate specificity preferences among these sequences include Pro-Phe-Thr, which is strongly cleaved by prolyl oligopeptidase, and Pro-Tyr-Asp, which is strongly cleaved by fibroblast activation protein alpha. Pro-Phe/Tyr-Asp/Glu sequences are extensively cleaved by both prolyl oligopeptidase and fibroblast activation protein alpha, but neither enzyme exhibit substantial cleavage of Pro-Asp/Glu-Phe-Tyr Homo sapiens