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Literature summary for 2.4.1.50 extracted from

  • Risteli, M.; Ruotsalainen, H.; Bergmann, U.; Venkatraman Girija, U.; Wallis, R.; Myllylae, R.
    Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin (2014), PLoS ONE, 9, e113498.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in MEF cells Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-galactose + procollagen 5-hydroxy-L-lysine Homo sapiens
-
UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information LH3 is the only enzyme capable of glucosylating the galactosylhydroxylysine residues in proteins with a collagenous domain Homo sapiens ?
-
?
UDP-alpha-D-galactose + procollagen 5-hydroxy-L-lysine
-
Homo sapiens UDP + procollagen 5-(D-galactosyloxy)-L-lysine
-
?

Synonyms

Synonyms Comment Organism
LH3
-
Homo sapiens
lysyl hydroxylase 3 a multifunctional protein with lysyl hydroxylase, collagen galactosyltransferase and glucosyltransferase activities Homo sapiens

General Information

General Information Comment Organism
metabolism the enzyme is commonly involved in biosynthesis of collagenous proteins Homo sapiens