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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.26 Z-prolyl-prolinal
-
Homo sapiens
3.4.21.B28 additional information no inhibition by Z-Pro-prolinal Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.26 soluble
-
Homo sapiens
-
-
3.4.21.B28 membrane a type II integral membrane serine protease Homo sapiens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.26 80000
-
x * 80000 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.B28 additional information Homo sapiens a post-proline cleaving serine peptidase ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.26 Homo sapiens
-
-
-
3.4.21.B28 Homo sapiens Q12844
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.B28 epithelial carcinoma cell
-
Homo sapiens
-
3.4.21.B28 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.26 GEPGPPGPA + H2O
-
Homo sapiens GEP + GPPGP + L-Ala
-
?
3.4.21.26 GFSPFRQED + H2O
-
Homo sapiens GFSP + FRQED
-
?
3.4.21.26 GTAGPNQEQE + H2O
-
Homo sapiens GTAGP + NQEQE
-
?
3.4.21.26 GTSGPNQEQE + H2O
-
Homo sapiens GTSGP + NQEQE
-
?
3.4.21.26 additional information does not cleave GASGPAGPA Homo sapiens ?
-
?
3.4.21.26 RPKPQQFFGLM + H2O
-
Homo sapiens L-Arg-L-Pro + L-Lys-L-Pro + QQFFGLM
-
?
3.4.21.26 Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
-
Homo sapiens Z-Gly-L-Pro + 7-amino-4-methylcoumarin
-
?
3.4.21.B28 alpha2-antiplasmin + H2O
-
Homo sapiens ?
-
?
3.4.21.B28 GASGPAGPA + H2O
-
Homo sapiens GASGP + AGPA
-
?
3.4.21.B28 Gelatin + H2O
-
Homo sapiens ?
-
?
3.4.21.B28 GEPGPPGPA + H2O
-
Homo sapiens GEP + GPPGP + L-Ala
-
?
3.4.21.B28 GFSPFQRED + H2O low activity Homo sapiens ?
-
?
3.4.21.B28 GTAGPNQEQE + H2O
-
Homo sapiens GTAGP + NQEQE
-
?
3.4.21.B28 GTSGPNQEQE + H2O
-
Homo sapiens GTSGP + NQEQE
-
?
3.4.21.B28 additional information a post-proline cleaving serine peptidase Homo sapiens ?
-
?
3.4.21.B28 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 ?
-
?
3.4.21.B28 RPKPQQFFGLM + H2O the substance P-derived sequence is cleaved although it does not contain Gly-Pro Homo sapiens RPKP + L-Gln-L-Gln + FFGLM
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.26 ? x * 80000 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.21.26 POP
-
Homo sapiens
3.4.21.B28 FAP
-
Homo sapiens
3.4.21.B28 fibroblast activation protein alpha
-
Homo sapiens
3.4.21.B28 seprase
-
Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.21.B28 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