Literature summary for 1.4.3.21 extracted from

Hysmith, R.M.; Boor, P.J.
Purification of benzylamine oxidase from cultured porcine aortic smooth muscle cells (1988), Biochem. Cell Biol., 66, 821-829.

Search for more literature for 1.4.3.21

Inhibitors

Inhibitors	Comment	Organism	Structure
Cuprizone	-	Sus scrofa
diethyldithiocarbamate	no inhibition	Sus scrofa
p-chloromercuriphenylsulfonate	0.1 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells	Sus scrofa
Phenelzine	0.001 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells	Sus scrofa
Semicarbazide	0.01 mM, complete inhibition of enzyme from cultured aortic smooth muscle cells	Sus scrofa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0051	-	benzylamine	enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH	Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
130000	-	x * 130000, SDS-PAGE	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
2.08	-	enzyme from cultured aortic smooth muscle cells	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
benzylamine + H2O + O2	-	Sus scrofa	benzaldehyde + NH3 + H2O2	-	?
RCH2NH2 + H2O + O2	-	Sus scrofa	RCHO + NH3 + H2O2	-	?

Subunits

Subunits	Comment	Organism
?	x * 130000, SDS-PAGE	Sus scrofa

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Release 2023.1 (January 2023)