Literature summary for 1.4.3.2 extracted from

Li, R.; Zhu, S.; Wu, J.; Wang, W.; Lu, Q.; Clemetson, K.J.
L-amino acid oxidase from Naja atra venom activates and binds to human platelets (2008), Acta Biochim. Biophys. Sin., 40, 19-26.

Search for more literature for 1.4.3.2

Application

Application	Comment	Organism
additional information	LAAO dose-dependently induces aggregation of washed human platelets. It induces tyrosine phosphorylation of a number of platelet proteins including Src kinase, spleen tyrosine kinase, and phospholipase C gamma2. Both H2O2 production and binding to platelet membrane proteins may be involved in its action. The enzyme binds to the platelet membrane to enhance the sensitivity of platelets to H2O2. At the same time, H2O2 released by the enzyme activates platelets by an unknown mechanism	Naja atra

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	inhibits platelet aggregation induced by LAAO	Naja atra
EMD 132338	inhibits platelet aggregation induced by LAAO	Naja atra
additional information	LAAO has no activity on platelets in platelet-rich plasma. Catalase inhibits the platelet aggregation and platelet protein phosphorylation induced by LAAO	Naja atra

Organism

Organism	UniProt	Comment	Textmining
Naja atra	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by cation ion exchange chromatography, gel filtration and anion ion exchange chromatography, to homogeneity	Naja atra

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Naja atra	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-leucine + H2O + O2	-	Naja atra	4-methyl-2-oxopentanoic acid + NH3 + H2O2	-	?

Synonyms

Synonyms	Comment	Organism
LAAO	-	Naja atra

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Release 2023.1 (January 2023)