Literature summary for 1.4.3.21 extracted from

Liang, G.; Choi-Sledeski, Y.M.; Poli, G.; Chen, X.; Shum, P.; Minnich, A.; Wang, Q.; Tsay, J.; Sides, K.; Cairns, J.; Stoklosa, G.; Nieduzak, T.; Zhao, Z.; Wang, J.; Vaz, R.J.
A conformationally constrained inhibitor with an enhanced potency for beta-tryptase and stability against semicarbazide-sensitive amine oxidase (SSAO) (2010), Bioorg. Med. Chem. Lett., 20, 6721-6724.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in CHO cells	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Semicarbazide	-	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	active site bound, coordinated by three conserved histidine residues	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methyl 1-(2-methoxyethyl)-3-(trifluoroacetyl)-1H-indole-4-carboxylate + H2O + O2	-	Homo sapiens	?	-	?
additional information	the catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A. This channel is gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO. While specific interactions with residues lining the surface of the accessing channel are important for substrate specificity, the flexibility of substrates also plays an important role, molecular dynamics and induced docking studies, detailed overview	Homo sapiens	?	-	?
additional information	no activity with dimethylamide substituted indole 3-((4-[5-(aminomethyl)-2-fluorophenyl]piperidin-1-yl)carbonyl)-1-(2-methoxyethyl)-N,N-dimethyl-1H-indole-4-carboxamide	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
dimer	human SSAO is a dimeric membrane protein with a short N-terminal cytoplasmic tail, a membrane-spanning domain, and an extracellular catalytic domain. The catalytic center is deeply buried within the enzyme and is accessible only through a narrow channel with a diameter of about 4.5 A, gated by the side chain of L469 which, along with the copper-TPQ coordination, controls the catalytic activity of SSAO, conformational changes, detailed overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
semicarbazide-sensitive amine oxidase	-	Homo sapiens
SSAO	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
trihydroxyphenylalanine quinone	-	Homo sapiens

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Release 2023.1 (January 2023)