Literature summary for 1.14.11.4 extracted from

Scietti, L.; Chiapparino, A.; De Giorgi, F.; Fumagalli, M.; Khoriauli, L.; Nergadze, S.; Basu, S.; Olieric, V.; Cucca, L.; Banushi, B.; Profumo, A.; Giulotto, E.; Gissen, P.; Forneris, F.
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3 (2018), Nat. Commun., 9, 3163 .

Search for more literature for 1.14.11.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression from HeLa cell lines and from transient HEK293 cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method, crystal structures of full-length human LH3 in complex with cofactors and donor substrates provide a molecular understanding of the biochemical knowledge underlying the multiple functions of this enzyme	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
[procollagen]-L-lysine + 2-oxoglutarate + O2	Homo sapiens	-	[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60568	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[procollagen]-L-lysine + 2-oxoglutarate + O2	-	Homo sapiens	[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2	-	?
[procollagen]-L-lysine + 2-oxoglutarate + O2	human lysyl hydroxylase 3 (LH3/PLOD3) is a multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. Two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Collagen glucosyltransferase (EC 2.4.1.66) and procollagen galactosyltransferase (EC 2.4.1.50) activities localize at the N-terminus of the enzyme, whereas the lysyl hydroxylase activity (EC 1.14.11.4) is segregated at the LH3 C-terminus	Homo sapiens	[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	two distinct catalytic sites at the N- and C-terminal boundaries of each monomer are separated by an accessory domain. Dimerization is essential for lysyl hydroxylase activity, whereas disruption of physiological dimers does not significantly perturb the N-terminal glycosyltransferase activities of LH3	Homo sapiens

Synonyms

Synonyms	Comment	Organism
LH3/PLOD3	-	Homo sapiens
lysyl hydroxylase 3	-	Homo sapiens
multifunctional collagen lysyl hydroxylase	-	Homo sapiens

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Release 2023.1 (January 2023)