Literature summary for 2.4.1.66 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 .

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
structures of full-length human LH3 in complex with cofactors and donor substrates. LH3 has three domains encompassing multiple catalytic sites and forms elongated tail-to-tail dimers showing two distinct catalytic sites at the N- and C-terminal boundaries of each monomer. The glycosyltransferase domain displays distinguishing features compared to other known glycosyltransferases. Known disease-related mutations map in close proximity to the catalytic sites	Homo sapiens

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

structures of full-length human LH3 in complex with cofactors and donor substrates. LH3 has three domains encompassing multiple catalytic sites and forms elongated tail-to-tail dimers showing two distinct catalytic sites at the N- and C-terminal boundaries of each monomer. The glycosyltransferase domain displays distinguishing features compared to other known glycosyltransferases. Known disease-related mutations map in close proximity to the catalytic sites

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	contributes to the overall enzyme stabilization, enzymatic activity peaks at 25 microM Fe2+	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine	Homo sapiens	-	UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60568	-	-
Homo sapiens	O60568	multifunctional, cataylzes reactions of EC 1.14.11.4, EC 2.4.1.50, EC 2.4.1.66	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine	-	Homo sapiens	UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine	-	?
UDP-alpha-D-glucose + [procollagen]-(5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysine	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	UDP + [procollagen]-(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-hydroxy-L-lysine	-	?

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	-	Homo sapiens
LH3/PLOD3	-	Homo sapiens
multifunctional procollagen lysine hydroxylase and glycosyltransferase	-	Homo sapiens
PLOD3	-	Homo sapiens