Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Park, H.; Shim, J.S.; Kim, B.S.; Jung, H.J.; Huh, T.L.; Kwon, H.J.
    Purpurin inhibits adipocyte-derived leucine aminopeptidase and angiogenesis in a zebrafish model (2014), Biochem. Biophys. Res. Commun., 450, 561-567 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.1 additional information knockdown of A-LAP expression by siRNA Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.1 purpurin is isolated from the natural product library and inhibits adipocyte-derived leucine aminopeptidase and angiogenesis in a zebrafish model. Purpurin inhibits A-LAP activity in a non-competitive manner showing a strong selectivity toward A-LAP versus another member of M1 family of zinc metallopeptidase, aminopeptidase N (APN). Purpurin can be developed as an anti-angiogenic agent. Purpurin also causes a partial inhibition of extension of the intersegmental vessels (ISVs) from the dorsal aorta Danio rerio
3.4.11.1 purpurin is isolated from the natural product library and inhibits the proliferation of HUVECs in a dose-dependent manner with an IC50 value of 0.03 mM. The proliferation of other types of cells such as HeLa (cervical carcinoma) and C8161 (melanoma) is not significantly inhibited by purpurin at the same concentration range used for HUVEC. Purpurin selectively inhibits the proliferation of endothelial cells over the other types of mammalian cells. Purpurin does not significantly affect the viability of HUVEC up to 0.02 mM treatment. A marginal decrease in the HUVEC viability is observed between 0.04-0.06 mM, and the significant cytotoxicity is observed at over 0.08 mM treatment with purpurin. The treatment of purpurin does not significantly affect the expression level of A-LAP in HUVEC Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.1 Zn2+ a zinc metallopeptidase Homo sapiens
3.4.11.1 Zn2+ a zinc metallopeptidase Danio rerio

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.1 Danio rerio
-
-
-
3.4.11.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.1 adipocyte
-
Homo sapiens
-
3.4.11.1 adipocyte
-
Danio rerio
-
3.4.11.1 embryo
-
Danio rerio
-
3.4.11.1 HUVEC cell human umbilical vein endothelial cell Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.1 L-Leu 7-amido-4-methylcoumarin + H2O
-
Homo sapiens L-Leu + 7-amino-4-methylcoumarin
-
?
3.4.11.1 L-Leu 7-amido-4-methylcoumarin + H2O
-
Danio rerio L-Leu + 7-amino-4-methylcoumarin
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.1 A-LAP
-
Homo sapiens
3.4.11.1 A-LAP
-
Danio rerio
3.4.11.1 adipocyte-derived leucine aminopeptidase
-
Homo sapiens
3.4.11.1 adipocyte-derived leucine aminopeptidase
-
Danio rerio
3.4.11.1 leucine aminopeptidase
-
Homo sapiens
3.4.11.1 leucine aminopeptidase
-
Danio rerio

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.1 37
-
assay at Homo sapiens
3.4.11.1 37
-
assay at Danio rerio

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.1 7.4
-
assay at Homo sapiens
3.4.11.1 7.4
-
assay at Danio rerio

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.11.1 additional information
-
additional information inhibition kinetics Homo sapiens
3.4.11.1 additional information
-
additional information inhibition kinetics Danio rerio

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.4.11.1 0.02
-
pH 7.4, 37°C Danio rerio purpurin

General Information

EC Number General Information Comment Organism
3.4.11.1 evolution the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases Homo sapiens
3.4.11.1 evolution the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases Danio rerio
3.4.11.1 malfunction knockdown of A-LAP expression by siRNA inhibits HUVEC angiogenesis Homo sapiens
3.4.11.1 physiological function adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis Homo sapiens
3.4.11.1 physiological function adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis Danio rerio