Literature summary for 1.5.3.16 extracted from

Leonetti, A.; Cervoni, L.; Polticelli, F.; Kanamori, Y.; Yurtsever, Z.N.; Agostinelli, E.; Mariottini, P.; Stano, P.; Cervelli, M.
Spectroscopic and calorimetric characterization of spermine oxidase and its association forms (2017), Biochem. J., 474, 4253-4268 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NWM0	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
55	-	melting temperature, presence of dithiothreitol	Homo sapiens
56	-	meling temperature	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
FAD	unfolding of the FAD-binding domain occurs at 57.6°C (melting temperature) in the absence of dithiothreitol and at 49.4°C in presence of dithiothreitol	Homo sapiens

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Release 2023.1 (January 2023)