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(GDK)4 + 2-oxoglutarate + O2
?
(IKG)3 + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
?
(Pro-Pro-Gly)4-Ala-Arg-Gly-Met-Lys-Gly-His-Arg-Gly-(Pro-Pro-Gly)4 + 2-oxoglutarate + O2
(Pro-Pro-Gly)4-Ala-Arg-Gly-Met-5-hydroxylysine-Gly-His-Arg-Gly-(Pro-Pro-Gly)4 + succinate + CO2
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Substrates: -
Products: -
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2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly + 2-oxoglutarate + O2
Ala-Arg-Gly-Ile-5-hydroxylysine-Gly-Ile-Arg-Gly-Phe-Ser-Gly + succinate + CO2
Ala-Arg-Gly-Met-Lys-Gly-His-Arg-Gly-(Pro-Pro-Gly)4 + 2-oxoglutarate + O2
Ala-Arg-Gly-Met-5-hydroxylysine-Gly-His-Arg-Gly-(Pro-Pro-Gly)4 + succinate + CO2
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Substrates: -
Products: -
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
KGIKGIKG + 2-oxoglutarate + O2
?
L-lysine containing nonapeptides + 2-oxoglutarate + O2
5-hydroxy-L-lysine containing nonapeptides + succinate + CO2
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Substrates: diverse nonapeptides, synthetic substrates
Products: -
?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
luc7like2(267-278) + 2-oxoglutarate
? + succinate + CO2
Substrates: substrate is a Luc7like2 protein fragment
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
peptide (IKG)3 + 2-oxoglutarate + O2
?
Substrates: -
Products: -
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
type I procollagen + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
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type IV procollagen + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
?
U2AF65 + 2-oxoglutarate + O2
?
-
Substrates: -
Products: -
?
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
additional information
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(GDK)4 + 2-oxoglutarate + O2
?
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Substrates: peptide acceptor substrate
Products: -
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(GDK)4 + 2-oxoglutarate + O2
?
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Substrates: peptide acceptor substrate
Products: -
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
-
Substrates: -
Products: -
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
Substrates: -
Products: -
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
Substrates: -
Products: -
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
Substrates: uncoupled decarboxylation in absence of peptide substrate
Products: -
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
Substrates: -
Products: -
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
Substrates: -
Products: -
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
Substrates: -
Products: -
?
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
?
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
?
Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly + 2-oxoglutarate + O2
Ala-Arg-Gly-Ile-5-hydroxylysine-Gly-Ile-Arg-Gly-Phe-Ser-Gly + succinate + CO2
-
Substrates: -
Products: -
?
Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly + 2-oxoglutarate + O2
Ala-Arg-Gly-Ile-5-hydroxylysine-Gly-Ile-Arg-Gly-Phe-Ser-Gly + succinate + CO2
Substrates: -
Products: -
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: -
Products: -
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
Substrates: -
Products: -
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
Substrates: influence the integrity and stability of collagen
Products: -
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
Substrates: -
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: enzyme required during collagen biosynthesis
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: influence the integrity and stability of collagen
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: influence the integrity and stability of collagen
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: -
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: influence the integrity and stability of collagen
Products: -
?
KGIKGIKG + 2-oxoglutarate + O2
?
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Substrates: a synthetic peptide substrate
Products: -
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KGIKGIKG + 2-oxoglutarate + O2
?
-
Substrates: a synthetic peptide substrate
Products: -
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KGIKGIKG + 2-oxoglutarate + O2
?
Substrates: a synthetic peptide substrate
Products: -
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L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
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Substrates: -
Products: -
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L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
-
Substrates: -
Products: -
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: collagen type IV
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
Substrates: -
Products: -
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: PLOD2 specifically hydroxylates lysines in the telopeptide of procollagens, whereas PLOD1 is responsible for lysine hydroxylation in the alpha-helical or central domain
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: the hydroxylysyl residues are located in Y positions of X-Y-Gly repeats of collagenous sequences
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
Substrates: -
Products: -
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L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
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Substrates: U2AF65 is the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kDa subunit, which undergoes posttranslational lysyl-5-hydroxylation catalyzed by the Fe2+ and 2-oxoglutarate-dependent dioxygenase Jumonji domain-6 protein Jmjd6, a nuclear protein that has an important role in vertebrate development and is a human homologue of the HIF asparaginyl-hydroxylase
Products: -
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L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
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Substrates: U2AF65 is the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kilodalton subunit
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: C-terminally FLAG-tagged rat MBL-A
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: C-terminally FLAG-tagged rat MBL-A
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: minimum sequence required: Xaa-Lys-Gly
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: in e.g. lysinevasopressin, lysine-rich histone
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: helical regions of collagen
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: synthetic peptides
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: protocollagen
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: protocollagen
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: minimum sequence required: Xaa-Lys-Gly
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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Substrates: synthetic peptides
Products: -
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peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
Substrates: synthetic peptides
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
Substrates: synthetic peptides
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: protocollagen
Products: hydroxy-L-lysine
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: collagen and other proteins with collagenous domains
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: enzyme is important in fibrosis because its hydroxylation activity of lysine residues in telopeptides leads to increased cross-linking of accumulated collagen with pyrolidine in fibrotic tissues, enzyme expression in increased in systemic sclerosis
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: hydroxylation of lysine residues in collagenous sequences
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: -
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: isozyme LH2b directs the collagen cross-linking pathways, lysine hydroxylation as post-translational modification critical for collagen cross-linking and glycosylation, isozyme LH2 modulates the cross-linking pattern
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: hydroxylation of lysine residues collagen causes cross-linking with pyrolidine
Products: -
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[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
r
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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Substrates: -
Products: -
r
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
r
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
r
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: 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
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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additional information
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Substrates: bifunctional lysyl hydroxylase and glycosyltransferase enzyme, mimivirus L230 is capable of hydroxylating lysine and glycosylating the resulting hydroxylysine residues in a native mimivirus collagen acceptor substrate. In contrast to other animals, the mimivirus L230 enzyme transfers glucose instead of galactose to hydroxylysine in collagen
Products: -
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additional information
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Substrates: the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
Products: -
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additional information
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Substrates: bifunctional lysyl hydroxylase and glycosyltransferase enzyme, mimivirus L230 is capable of hydroxylating lysine and glycosylating the resulting hydroxylysine residues in a native mimivirus collagen acceptor substrate. In contrast to other animals, the mimivirus L230 enzyme transfers glucose instead of galactose to hydroxylysine in collagen
Products: -
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additional information
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Substrates: the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
Products: -
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additional information
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Substrates: the enzyme is also able to glycosylate hydroxylysyl residues and is functionally similar to the isozyme LH3 of vertebrates
Products: -
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additional information
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Substrates: Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
Products: -
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additional information
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Substrates: the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
Products: -
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additional information
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Substrates: the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
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additional information
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Substrates: isozymes show no strict substrate specificity concerning the synthetic peptide substrates, but preferences for sequences, analysis of the different isozymes' binding affinities for the peptides whose net charges are very important, partly the peptides bind to the active site, overview
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additional information
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Substrates: LH2 hydroxylates the N telopeptide of the full-length procollagen alpha type I chain when coexpressed with this isoenzyme
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additional information
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Substrates: Jmjd6 changes alternative RNA splicing of some, but not all, of the endogenous and reporter genes, supporting a specific role for Jmjd6 in the regulation of RNA splicing, overview
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additional information
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Substrates: LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
Products: -
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additional information
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Substrates: LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
Products: -
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additional information
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Substrates: lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
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additional information
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Substrates: lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
Products: -
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additional information
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Substrates: the enzyme is responsible for the hydroxylation of collagen telopeptides
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additional information
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Substrates: LH3 differs from the other lysyl hydroxylase isoforms in that it possesses, in addition to lysyl hydroxylase activity, hydroxylysyl galactosyltransferase and galactosylhydroxylysyl glucosyltransferase activities, thus LH3 is able to catalyze the formation of glucosylgalactosylhydroxylysine residues
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additional information
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Substrates: LH3 differs from the other lysyl hydroxylase isoforms in that it possesses, in addition to lysyl hydroxylase activity, hydroxylysyl galactosyltransferase and galactosylhydroxylysyl glucosyltransferase activities, thus LH3 is able to catalyze the formation of glucosylgalactosylhydroxylysine residues
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additional information
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Substrates: JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNAsplicing-related proteins. It catalyses C5 hydroxylation rather than Nepsilon demethylation
Products: -
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additional information
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Substrates: JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 2-oxoglutarate, in absence of substrate or in presence of substrates like U2AF65, resulting in production of (5S)<-hydroxylysine residues. JMJD6 in human cells is hydroxylated
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additional information
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Substrates: lysyl hydroxylase 3 is a multifunctional enzyme of collagen biosynthesis, with glycosyltransferase activity and lysyl hydroxylase activity
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additional information
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Substrates: in absence of substrate JMJD6 catalyses turnover of 2-oxoglutarate to succinate
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additional information
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Substrates: an enzyme activity assay for detection of succinate is evaluated: the succinate-Glo assay, employing a luciferase-based luminescence system, is superior from the standpoint of stability and signal-to-noise ratio. Luciferase activity is detected over a wide range of concentrations of LH2, and the luminescence signal was proportional to the concentration of LH2. Method development and evaluation, overview
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additional information
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Substrates: an enzyme activity assay for detection of succinate is evaluated: the succinate-Glo assay, employing a luciferase-based luminescence system, is superior from the standpoint of stability and signal-to-noise ratio. Luciferase activity is detected over a wide range of concentrations of LH2, and the luminescence signal was proportional to the concentration of LH2. Method development and evaluation, overview
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additional information
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Substrates: 1,25(OH)2D3 directly regulates collagen cross-linking in MC3T3-E1 cells likely by upregulating gene expression of specific lysyl hydroxylase and lysine oxidase enzymes, overview
Products: -
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additional information
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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additional information
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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additional information
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Substrates: FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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additional information
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Substrates: FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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additional information
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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additional information
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Substrates: isozyme LH2a possesses telopeptide lysyl hydroxylase activity
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additional information
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Substrates: isozyme LH2a possesses telopeptide lysyl hydroxylase activity
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adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
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Substrates: U2AF65 is the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kDa subunit, which undergoes posttranslational lysyl-5-hydroxylation catalyzed by the Fe2+ and 2-oxoglutarate-dependent dioxygenase Jumonji domain-6 protein Jmjd6, a nuclear protein that has an important role in vertebrate development and is a human homologue of the HIF asparaginyl-hydroxylase
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
additional information
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adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
Substrates: -
Products: -
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: influence the integrity and stability of collagen
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: enzyme required during collagen biosynthesis
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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Substrates: influence the integrity and stability of collagen
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: influence the integrity and stability of collagen
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: enzyme required during collagen biosynthesis
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collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
Substrates: influence the integrity and stability of collagen
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L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: collagen type IV
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
Substrates: -
Products: -
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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Substrates: PLOD2 specifically hydroxylates lysines in the telopeptide of procollagens, whereas PLOD1 is responsible for lysine hydroxylation in the alpha-helical or central domain
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L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
Substrates: -
Products: -
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: C-terminally FLAG-tagged rat MBL-A
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mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
Substrates: C-terminally FLAG-tagged rat MBL-A
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: collagen and other proteins with collagenous domains
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: enzyme is important in fibrosis because its hydroxylation activity of lysine residues in telopeptides leads to increased cross-linking of accumulated collagen with pyrolidine in fibrotic tissues, enzyme expression in increased in systemic sclerosis
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: hydroxylation of lysine residues in collagenous sequences
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: some hydroxylated L-lysine residues are precursors for the cross-link formation essential for the tensile strength of collagen, the 2 splicing variants exhibit different specificity for hydroxylation of either telopeptide or helical collagen domain lysine residues, so that their relative expression level determines the type of cross-links formed and affecting collagen strength
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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Substrates: isozyme LH2b directs the collagen cross-linking pathways, lysine hydroxylation as post-translational modification critical for collagen cross-linking and glycosylation, isozyme LH2 modulates the cross-linking pattern
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procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
Substrates: hydroxylation of lysine residues collagen causes cross-linking with pyrolidine
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Substrates: -
Products: -
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additional information
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Substrates: bifunctional lysyl hydroxylase and glycosyltransferase enzyme, mimivirus L230 is capable of hydroxylating lysine and glycosylating the resulting hydroxylysine residues in a native mimivirus collagen acceptor substrate. In contrast to other animals, the mimivirus L230 enzyme transfers glucose instead of galactose to hydroxylysine in collagen
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additional information
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Substrates: bifunctional lysyl hydroxylase and glycosyltransferase enzyme, mimivirus L230 is capable of hydroxylating lysine and glycosylating the resulting hydroxylysine residues in a native mimivirus collagen acceptor substrate. In contrast to other animals, the mimivirus L230 enzyme transfers glucose instead of galactose to hydroxylysine in collagen
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additional information
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Substrates: Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
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additional information
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Substrates: the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
Products: -
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additional information
?
-
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Substrates: the long splicing variant of isozyme LH2 is the major ubiquitously-expressed form that is spliced into the short form, which is expressed together with the long form only in some tissues, e.g. kidney, spleen, liver, and placenta, alternative splicing can be regulated by both cell density and cycloheximide, regulation of LH2long transcript and of expression of both splicing variants in kidney via cycloheximide that suppress a factor taht inhibits exclusion of exon 13A thereby promoting expression of LH2short, and vice versa also via cycloheximide in fibroblasts, overview, perturbation of LH2 regulation can influence the stability of the extracellular matrix and contribute to connective tissue disorders
Products: -
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additional information
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Substrates: Jmjd6 changes alternative RNA splicing of some, but not all, of the endogenous and reporter genes, supporting a specific role for Jmjd6 in the regulation of RNA splicing, overview
Products: -
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additional information
?
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Substrates: LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
Products: -
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additional information
?
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Substrates: LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
Products: -
?
additional information
?
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Substrates: lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
Products: -
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additional information
?
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Substrates: lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the hydroxylation of collagen telopeptides
Products: -
?
additional information
?
-
Substrates: JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNAsplicing-related proteins. It catalyses C5 hydroxylation rather than Nepsilon demethylation
Products: -
?
additional information
?
-
-
Substrates: JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 2-oxoglutarate, in absence of substrate or in presence of substrates like U2AF65, resulting in production of (5S)<-hydroxylysine residues. JMJD6 in human cells is hydroxylated
Products: -
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additional information
?
-
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Substrates: lysyl hydroxylase 3 is a multifunctional enzyme of collagen biosynthesis, with glycosyltransferase activity and lysyl hydroxylase activity
Products: -
?
additional information
?
-
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Substrates: 1,25(OH)2D3 directly regulates collagen cross-linking in MC3T3-E1 cells likely by upregulating gene expression of specific lysyl hydroxylase and lysine oxidase enzymes, overview
Products: -
?
additional information
?
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
Products: -
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additional information
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
Products: -
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additional information
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Substrates: FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
Products: -
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additional information
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Substrates: FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
Products: -
?
additional information
?
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Substrates: lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
Products: -
?
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additional information
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heterocomplex formation between mouse and human LH3, between human LH1 and LH3 and between human LH2 and LH3, low amount of complexes formed in vivo
drug target
normalizing the cross-link pattern by selectively inhibiting LH2 (and thus hydroxy-alpha-aminoadipic acid-delta-semialdehyde cross-linking) alters the balance of collagen degradation. It is expected that this results in reversible fibrosis. Since the up-regulation of LH2 is seen in all organs, a drug that specifically inhibits LH2 activity can be used in a wide range of fibrotic disorders. Since LH2 catalyzes only a single reaction downstream in the fibrogenic cascade (namely the formation of unwanted cross-links in collagen of the fibrotic lesions), little (if any) side-effects are expected, as the deposited collagen in the wound area is expected to be normally modified, and thus have the properties (e.g. with respect to tensile strength) required for a normal function of the repaired tissue
drug target
PLOD2 is a gene of clinical relevance with implications in glioblastoma invasion and treatment strategies. PLOD2 expression is positively correlated with tumor grade and inversely associated with glioblastoma patient prognosis
drug target
the expression level of the procollagen-lysine, 2-oxoglutarate 5-dioxygenase (PLOD) might become a novel biomarker for prognosis and is a potential target for individual treatment decisions in lower-grade glioma (LGG)
evolution
-
LH3 belongs to the lysyl hydroxylase family of enzymes that has important roles in the biosynthesis of collagen
evolution
-
whereas in animals from sponges to humans the transfer of galactose to hydroxylysine in collagen is conserved, the mimivirus L230 enzyme transfers glucose to hydroxylysine, thereby defining another type of collagen glycosylation in nature. Utilization of glucose instead of the galactose found throughout animals as well as a bifunctional enzyme rather than two separate enzymes may represent a parallel evolutionary track in collagen biology
evolution
the enzyme belongs to the 2-oxoglutarate/Fe2+-dependent oxygenase family
evolution
-
whereas in animals from sponges to humans the transfer of galactose to hydroxylysine in collagen is conserved, the mimivirus L230 enzyme transfers glucose to hydroxylysine, thereby defining another type of collagen glycosylation in nature. Utilization of glucose instead of the galactose found throughout animals as well as a bifunctional enzyme rather than two separate enzymes may represent a parallel evolutionary track in collagen biology
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malfunction
-
although differential expression of LH2 (long) is associated with fibrotic conditions, there is no direct evidence that the increased Pyr cross-links in the overaccumulated collagen contribute definitively to fibrosis
malfunction
mutations in the LH3 gene cause connective tissue disorder
malfunction
reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix
malfunction
reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix. Mutations in the human LH3 gene cause a severe connective tissue disorder with features that overlap with a number of collagen disorders
malfunction
disorders of LH3 with a unique phenotype causing severe morbidity as a result of feauters that overlap with collagen disorders
malfunction
impairment of LH3 function significantly affects type I collagen fibrillogenesis
malfunction
-
lack of LH3 prevents the formation of hydroxylysine linked Glc-Gal structures in collagen. Secretion of type IV collagen is blocked in embryos that lack LH3 catalyzed Glc-Gal-Hyl residues, and this disrupts formation of the basement membranes that support tissues e.g. blood vessels. Changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion, phenotype, overview. Recombinant adiponectin produced in LH3-/- knockout fibroblasts cells does not form middle molecular weight and high molecular weight oligomers
malfunction
-
PLOD2 knockdown prevents fibrillar collagen formation in breast tumors, decreased PLOD2 expression in breast cancer cells inhibits metastasis, also lung metastasis is significantly impaired by PLOD2 knockdown
malfunction
enzyme LH3 downregulation decreases MMP-9 recruitment to MRC-5 and thus MMP-9/LH3 interaction
malfunction
inhibition of prolyl hydroxylation and lysyl hydroxylation/glycosylation affects on adiponectin production, pharmacological LH inhibition causes significant suppression of adiponectin production, more particularly of the higher-order isoforms
malfunction
inhibition of prolyl hydroxylation and lysyl hydroxylation/glycosylation affects on adiponectin production, pharmacological LH inhibition causes significant suppression of adiponectin production, more particularly of the higher-order isoforms. Transient gene knock-down of LH3 encoding gene Plod3 causes a suppressive effect, especially on the high molecular-weight (HMW) isoforms
malfunction
LH3 knockout studies in mice demonstrate that the loss of LH3 leads to embryonic lethality due to disruption in the formation of basement membranes. The absence of LH3 glycosyltransferase activities are responsible for the lethality. The lack of LH3 leads to loss of all Glc-Gal-Hyl residues in collagens I, IV and VI and prevents the assembly and secretion of type IV and VI collagens. In addition, the mutated LH activity, one out of three activities of LH3, leads to underglycosylation of collagen IV and VI, which is detected as abnormal distribution and aggregation of these collagens in mouse tissues. Oligomerization of recombinant MBL-A is defective in LH3-/- knockout MEF cells
malfunction
mice with loss of function of Leprel2 (encoding P3H3) have the same loss of tissue type I collagen lysine-hydroxylation as that observed in the Sc65 knockout mice. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. Sc65KO mouse generation and confirmation of bone loss phenotype, overview
malfunction
patients with Bruck syndrome, a recessively inherited disorder with inactivating mutations in the gene encoding LH2 (PLOD2/LH2), have traits of osteogenesis imperfecta with congenital contractures of the large joints. Conversely, skin fibroblasts from patients with systemic sclerosis, a fibrotic disease involving skin and other organs, have elevated LH2 expression and increased production of HLCCs
malfunction
knockdown of PLOD2 in glioma cell lines leads to decreases in migration and invasion under normoxia and hypoxia
malfunction
-
lack of LH3 prevents the formation of hydroxylysine linked Glc-Gal structures in collagen. Secretion of type IV collagen is blocked in embryos that lack LH3 catalyzed Glc-Gal-Hyl residues, and this disrupts formation of the basement membranes that support tissues e.g. blood vessels. Changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion, phenotype, overview. Recombinant adiponectin produced in LH3-/- knockout fibroblasts cells does not form middle molecular weight and high molecular weight oligomers
-
malfunction
-
LH3 knockout studies in mice demonstrate that the loss of LH3 leads to embryonic lethality due to disruption in the formation of basement membranes. The absence of LH3 glycosyltransferase activities are responsible for the lethality. The lack of LH3 leads to loss of all Glc-Gal-Hyl residues in collagens I, IV and VI and prevents the assembly and secretion of type IV and VI collagens. In addition, the mutated LH activity, one out of three activities of LH3, leads to underglycosylation of collagen IV and VI, which is detected as abnormal distribution and aggregation of these collagens in mouse tissues. Oligomerization of recombinant MBL-A is defective in LH3-/- knockout MEF cells
-
malfunction
-
impairment of LH3 function significantly affects type I collagen fibrillogenesis
-
malfunction
-
mice with loss of function of Leprel2 (encoding P3H3) have the same loss of tissue type I collagen lysine-hydroxylation as that observed in the Sc65 knockout mice. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. Sc65KO mouse generation and confirmation of bone loss phenotype, overview
-
metabolism
-
in osteoarthritic human synovial fibroblasts, the enzyme expression is induced by TGF-beta via kinase ALK5, not ALK1, and Smad2/3P
metabolism
essential roles of insulin, AMPK signaling and lysyl and prolyl hydroxylases in the biosynthesis and multimerization of adiponectin, pathway regulation, detailed overview
metabolism
the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3 affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. The prolyl-hydroxylase complex in the endoplasmic reticulum controls lysyl-hydroxylase activity during collagen synthesis. SC65/LH1/P3H3 are interlinked within a protein complex in the endoplasmic reticulum
metabolism
-
the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3 affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. The prolyl-hydroxylase complex in the endoplasmic reticulum controls lysyl-hydroxylase activity during collagen synthesis. SC65/LH1/P3H3 are interlinked within a protein complex in the endoplasmic reticulum
-
physiological function
-
the enzyme is responsible for the hydroxylation of collagen telopeptides
physiological function
the enzyme LH3 has an important role in the organization of the extracellular matrix and the cytoskeleton
physiological function
forms part of the many posttranslational modifications required during collagen biosynthesis
physiological function
-
dPlod is required for type-IV collagen secretion from hemocytes and fat body
physiological function
-
in hypoxic breast cancer cells, hypoxia-inducible factor 1 activates transcription of the PLOD1 and PLOD2 genes encoding procollagen lysyl hydroxylases that are required for the biogenesis of collagen, which is a major constituent of the extracellular matrix. High PLOD2 expression in breast cancer biopsies is associated with increased risk of mortality. PLOD2 is critical for fibrillar collagen formation by breast cancer cells, increases tumor stiffness, and is required for metastasis to lymph nodes and lungs
physiological function
lysyl hydroxylase (LH) catalyzes the hydroxylation of lysine residues in collagens, and contributes to the formation of more stable collagen cross-links
physiological function
-
lysyl hydroxylase 3 (LH3) is a post-translational modification enzyme with lysyl hydroxylase, collagen galactosyltransferase EC 2.4.1.50, and glucosyltransferase, EC 2.4.1.66, activities, LH3 is able to catalyze the three consecutive reactions required for the formation of unique hydroxylysine-linked carbohydrates, galactosylhydroxylysine and glucosylgalactosyl hydroxylysine, found in collagens and a few other proteins. The active sites for the different activities of the mutifunctional enzyme are localized separately in the C- and the N-terminal parts of the molecule. While the lysyl hydroxylase active site mediates retention of LH3 in the endoplasmic reticulum, the glucosyltransferase active site is required for the secretion of LH3 into the extracellular space
physiological function
lysyl hydroxylase 3 (LH3) is a post-translational modification enzyme with lysyl hydroxylase, collagen galactosyltransferase EC 2.4.1.50, and glucosyltransferase, EC 2.4.1.66, activities, LH3 is able to catalyze the three consecutive reactions required for the formation of unique hydroxylysine-linked carbohydrates, galactosylhydroxylysine and glucosylgalactosyl hydroxylysine, found in collagens and a few other proteins. The active sites for the different activities of the mutifunctional enzyme are localized separately in the C- and the N-terminal parts of the molecule. While the lysyl hydroxylase active site mediates retention of LH3 in the endoplasmic reticulum, the glucosyltransferase active site is required for the secretion of LH3 into the extracellular space
physiological function
lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture, role of LH3 in bone physiology
physiological function
-
lysyl hydroxylases are enzymes that catalyze the hydroxylation of lysine into hydroxylysine and, therefore, fulfill a crucial role in collagen modification and cross-linking. Lysyl hydroxylase 2b increases pyridinoline cross-links, making collagen less susceptible to enzymatic degradation
physiological function
-
regulation of the posttranslational lysine modifications in the collagenous domain is the key event in determining the function of adiponectin, changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion
physiological function
-
the lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicin. JMJD6 in human cells is self-hydroxylated at Lys111JMJD6 and Lys167JMJD6 to give lysyl 5S-hydroxylase. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing
physiological function
hydroxylysine aldehyde-derived collagen cross-links (HLCCs) accumulate in fibrotic tissues and certain types of cancer and are thought to drive the progression of these diseases. HLCC formation is initiated by lysyl hydroxylase 2 (LH2), an Fe(II) and 2-oxoglutarate-dependent oxygenase that hydroxylates telopeptidyl lysine residues on collagen
physiological function
in the endoplasmic reticulum, specific proline and lysine residues of newly translated procollagen chains are modified by prolyl- and lysyl-hydroxylases, respectively. These enzymes share a highly conserved catalytic 2-oxoglutarate, ascorbate- and Fe(II)-dependent dioxygenase domain
physiological function
intracellular procollagen-lysine, 2-oxoglutarate 5-dioxygenase enzymes induce hydroxylation of Lys residues on collagen prior to formation of triple helical pro-collagen molecules. Following secretion of pro-collagen molecules into the extracellular space, the telopeptidyl Hyl residues undergo LOX-induced oxidative deamination into Hylald, which then forms Hylald-derived aldimine cross-links that spontaneously rearrange into stable ketoamines; these further mature into stable Hylald-derived collagen cross-links (HLCCs). Epithelial tumor metastasis is preceded by an accumulation of collagen cross-links that heighten stromal stiffness and stimulate the invasive properties of tumor cells. Epithelial tumorigenesis is accompanied by changes in the biochemical type of collagen crosslinks. Ectopic LH2 expression increases cell migration and invasion in Boyden chambers and enhances tumor growth and metastatic capacity in syngeneic wild-type Cdkn1a mice
physiological function
intracellular procollagen-lysine, 2-oxoglutarate 5-dioxygenase enzymes induce hydroxylation of Lys residues on collagen prior to formation of triple helical pro-collagen molecules. Following secretion of pro-collagen molecules into the extracellular space, the telopeptidyl Hyl residues undergo LOX-induced oxidative deamination into Hylald, which then forms Hylald-derived aldimine cross-links that spontaneously rearrange into stable ketoamines; these further mature into stable Hylald-derived collagen cross-links (HLCCs). Epithelial tumor metastasis is preceded by an accumulation of collagen cross-links that heighten stromal stiffness and stimulate the invasive properties of tumor cells. Epithelial tumorigenesis is accompanied by changes in the biochemical type of collagen crosslinks. relative to normal lung tissues, tumor stroma contains higher levels of hydroxylysine aldehyde-derived collagen cross-links (HLCCs) and lower levels of lysine aldehyde-derived cross-links (LCCs), which are the predominant types of collagen cross-links in skeletal tissues and soft tissues, respectively. Lysyl hydroxylase 2 (LH2) hydroxylates telopeptidyl lysine residues on collagen, and shifts the tumor stroma toward a high-HLCC, low-LCC state, increasing tumor stiffness, and enhancing tumor cell invasion and metastasis. LH2 enhances the metastatic properties of tumor cells and functions as a regulatory switch that controls the relative abundance of biochemically distinct types of collagen cross-links in the tumor stroma
physiological function
LH2 promotes fibrosis and cancer metastasis. Peptidyl prolyl isomerase (PPIase) activity of FKBP65 positively modulates LH2 enzymatic activity and is critical for the formation of hydroxylysine-aldehyde derived intermolecular collagen cross-links. FKBP65 regulates LH2-mediated collagen cross-linking. FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2. Reconstitution with wild-type FKBP65 increases the enzyme activity by 7fold
physiological function
LH3 is essential for catalyzing formation of the glucosylgalactosylhydroxylysines of mannan-binding lectin-A (MBL-A), the first component of the lectin pathway of complement activation. LH3 catalyzes formation of Glc-Gal-Hyl residues in collagens and in collagenous domain of adiponectin. Similar lysine modifications are also present in MBL-A. LH3 also modifies the lysine residues in the collagenous domain of adiponectin, an insulin-sensitizing hormone, and thus affects the oligomerization and secretion of adiponectin
physiological function
procollagen-lysine,2-oxoglutarate 5-dioxygenase 2, PLOD2, is involved in the posttranscriptional modification of collagen molecules and considered as a key mediator of collagen cross-linking and thus an important factor for the stability of the extracellular matrix. PLOD2 is known to be associated with several connective tissue diseases, such as Ehlers-Danlos syndrome type VI A, systemic sclerosis, and Bruck syndrome. Isozyme PLOD2 is involved in the pathology of brain arteriovenous malformations (bAVM), severe conditions that can cause severe neurologic deficits and mortality. High levels of PLOD2 expression correlate with bAVM size. Although PLOD2 is not directly associated with bAVM hemorrhage, high PLOD2-expressing bAVM have a lower frequency of hemorrhage compared with low or medium PLOD2-expressing bAVM (25% vs. 63% and 75%, respectively)
physiological function
recruitment of matrix metalloproteinase-9 (MMP-9) to the fibroblast cell surface by lysyl hydroxylase 3 triggers transforming growth factor-beta (TGF-beta) activation and fibroblast differentiation. LH3 provides the docking mechanism for MMP-9 cell surface association via the MMP-9 FN domain. Recruitment of MMP-9 to fibroblast cell surface does not depend merely on LH3 expression at the cell membrane. LH3 provides a mechanism for deployment of MMP-9 catalytic activity at the fibroblast cell surface that promotes TGF-beta activation and the corresponding enhancement of alpha-SMA expression. MMP-9-induced TGF-beta activation promotes alpha-SMA expression in fibroblasts is consistent with a function that supports tumor progression. LH3 expressed in a variety of tumor cell types fails to recruit MMP-9 to their cell surface
physiological function
the enzyme catalyzes lysine hydroxylation, which is involved in collagen crosslinking and stabilization. Critical mechanical role of collagen crosslinking enzymes, e.g. in bone healing. Lysyl hydroxylase 1 (PLOD1) is one of the few collagen crosslinking enzymes associated with bone quality
physiological function
the enzyme hydroxylates lysine residues in collagen telopeptides and is essential for collagen pyridinoline cross-link formation. PLOD2 expression and subsequent pyridinoline cross-links are increased in fibrotic pathologies by transforming growth factorbeta-1 (TGFbeta1). Binding of the TGFbeta1 pathway related transcription factors SMAD3 and SP1-mediated TGFbeta1 enhanced PLOD2 expression and might be correlated to an increase of acetylated histone H3 and H4 at the PLOD2 promoter
physiological function
the enzyme LH2 catalyzes lysine hydroxylation, which is involved in collagen crosslinking and stabilization. PLOD2 has no role in determining bone quality
physiological function
the enzyme LH3 catalyzes lysine hydroxylation
physiological function
the family of lysyl hydroxylases is responsible for catalyzing the hydroxylation of protein-bound lysyl residues to yield hydroxylysyl residues, which can then undergo subsequent glycosylation. Lysyl and prolyl hydroxylases are both required for physiological adiponectin production and in particular are essential for the formation/secretion of the HMW isoforms
physiological function
lysyl hydroxylase 2 is responsible for the formation of telopeptidyl hydroxylysine, leading to the formation of hydroxy-alpha-aminoadipic acid-delta-semialdehyde cross-links by lysyl oxidases. The enzyme is universally up-regulated in fibrosis
physiological function
PLOD2 promotes tissue invasion of human glioma cells
physiological function
procollagen-lysine,2-oxoglutarate 5-dioxygenase (PLOD) family is involved in processes, such as tumor formation and cancer metastasis. A high expression of the PLOD family relates to poor prognosis and high infiltration of immune cells within the tumor microenvironment (TME)
physiological function
-
regulation of the posttranslational lysine modifications in the collagenous domain is the key event in determining the function of adiponectin, changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion
-
physiological function
-
LH3 is essential for catalyzing formation of the glucosylgalactosylhydroxylysines of mannan-binding lectin-A (MBL-A), the first component of the lectin pathway of complement activation. LH3 catalyzes formation of Glc-Gal-Hyl residues in collagens and in collagenous domain of adiponectin. Similar lysine modifications are also present in MBL-A. LH3 also modifies the lysine residues in the collagenous domain of adiponectin, an insulin-sensitizing hormone, and thus affects the oligomerization and secretion of adiponectin
-
physiological function
-
lysyl hydroxylase 3 (LH3) is a post-translational modification enzyme with lysyl hydroxylase, collagen galactosyltransferase EC 2.4.1.50, and glucosyltransferase, EC 2.4.1.66, activities, LH3 is able to catalyze the three consecutive reactions required for the formation of unique hydroxylysine-linked carbohydrates, galactosylhydroxylysine and glucosylgalactosyl hydroxylysine, found in collagens and a few other proteins. The active sites for the different activities of the mutifunctional enzyme are localized separately in the C- and the N-terminal parts of the molecule. While the lysyl hydroxylase active site mediates retention of LH3 in the endoplasmic reticulum, the glucosyltransferase active site is required for the secretion of LH3 into the extracellular space
-
physiological function
-
lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture, role of LH3 in bone physiology
-
physiological function
-
in the endoplasmic reticulum, specific proline and lysine residues of newly translated procollagen chains are modified by prolyl- and lysyl-hydroxylases, respectively. These enzymes share a highly conserved catalytic 2-oxoglutarate, ascorbate- and Fe(II)-dependent dioxygenase domain
-
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D250A
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site-directed mutagenesis, the mutant shows unaltered lysyl hydroxylase activity, although reduced collagen glucosyltransferase activity, compared to the wild-type enzyme
D97A/D99A
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site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
H80A
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site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
H825S/D827A
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site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
L78K
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
D250A
-
site-directed mutagenesis, the mutant shows unaltered lysyl hydroxylase activity, although reduced collagen glucosyltransferase activity, compared to the wild-type enzyme
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D97A/D99A
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
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H80A
-
site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
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H825S/D827A
-
site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
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L78K
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
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C144I
-
isoform 3, reduces glycosyltransferase activity
L208I
-
isoform 3, reduces glycosyltransferase activity
A1011G
naturally occuring heterozygous polymorphism in gene PLOD3
A195G
naturally occuring polymorphism in gene PLOD3
A434G
naturally occuring polymorphism in gene PLOD3
C882T
naturally occuring heterozygous polymorphism in gene PLOD3
E542A
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site-directed mutagenesis
E542A/E547A
-
site-directed mutagenesis
E542A/E547A/E574A/E579A
-
site-directed mutagenesis
E542A/E547A/E574A/E579A/E560A
-
site-directed mutagenesis
E542A/H546L/E547A
-
site-directed mutagenesis
E542A/Q543L/Y544F/E547A/E574A
-
site-directed mutagenesis
E547A
-
site-directed mutagenesis
E579A/E560A
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site-directed mutagenesis
G597V
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naturally occuring recessive point mutation, leads to abnormal folding and oligomerization of the mutant enzyme, which shows over 95% reduced activity compared to the wild-type enzyme
K541M
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site-directed mutagenesis
K541M/E542A
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site-directed mutagenesis
K694G
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site-directed mutagenesis, point mutation is introduced in the LH1 part of the expression construct comprising 40 amino acid residues of the C-terminal end of isozyme LH1, responsible for endoplasmic reticulum localization, fused to human cathepsin D and c-Myc-tagged, the exchange of the charged residue and deletion of 8 amino acids of the last 40 residues at the enzymes' C-terminal end has no effect on retention efficiency of the reporter protein, but deletion of the next 8 amino acid residues, leaving 24 residues, increases the secretion level of enzyme from the cell
N223S
site-directed mutagenesis, the mutant shows 50% reduced lysylhydroxylase activity, while the glycosyltransferase activity is almost abolished
Q543L/Y544F
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site-directed mutagenesis
R594H
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naturally occuring recessive point mutation, leads to abnormal folding and oligomerization of the mutant enzyme, which shows over 95% reduced activity compared to the wild-type enzyme
R693Q
-
site-directed mutagenesis, point mutation is introduced in the LH1 part of the expression construct comprising 40 amino acid residues of the C-terminal end of isozyme LH1, responsible for endoplasmic reticulum localization, fused to human cathepsin D and c-Myc-tagged, the exchange of the charged residue and deletion of 8 amino acis of the last 40 residues at the enzymes' C-terminal end has no effect on retention efficiency of the reporter protein, but deletion of the next 8 amino acid residues, leaving 24 residues, increases the secretion level of enzyme from the cell
T604I
-
naturally occuring recessive point mutation, leads 70-92% reduced activity, dependent on the 2-oxoglutarate concentration, compared top the wild-type due to a 10fold increase in the Km for 2-oxoglutarate, the mutant shows unaltered folding and oligomerization. The Km values of the T604I mutant for the peptide substrate, Fe2+, and ascorbate are identical to those of the wild-type
W446G
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naturally occurring mutation T1360G in a highly conserved region of exon 13 of isozyme LH1 in skin fibroblasts is predicted to lead to the W446G exchange in heterozygous Ehlers-Danlos syndrome type IVA, leads to loss of enzyme activity and causes the pathogenic effect probably due to incorect folding of isozyme LH1, structure-function analysis
D669A
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site-directed mutagenesis, inactive mutant
D669A
site-directed mutagenesis, inactive mutant
D669A
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site-directed mutagenesis, inactive mutant
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additional information
identification of a PLOD2 mutant bearing 2 missense mutations in exon 17 in patients with Buck syndrome caused by a pyrolidine deficiency in bone due to decreased enzyme activity
additional information
-
identification of a PLOD2 mutant bearing 2 missense mutations in exon 17 in patients with Buck syndrome caused by a pyrolidine deficiency in bone due to decreased enzyme activity
additional information
targeted disruption of isoform LH3 by siRNA causes a marked reduction of both glycosyltransferase activities. Overexpression of LH3 increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. Treatment of cells in culture medium with a LH3 N-terminal fragment affects the cell behavior, rapidly leading to arrest of growth in a reversible manner
additional information
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glucosyltransferase, GGT, deficiency in heterozygous LH3 knock-out mouse embryonic fibroblasts affects the extracellular matrix deposition and the arrangement of the cytoskeleton, phenotype, overview. LH3 knock-out embryos and embryonic fibroblasts indicate that the loss of hydroxylysine glycosylation prevents the assembly and secretion of type IV and VI collagens, LH mutant mice show ultrastructural alterations in their skin and muscle
additional information
glucosyltransferase, GGT, deficiency in heterozygous LH3 knock-out mouse embryonic fibroblasts affects the extracellular matrix deposition and the arrangement of the cytoskeleton, phenotype, overview. LH3 knock-out embryos and embryonic fibroblasts indicate that the loss of hydroxylysine glycosylation prevents the assembly and secretion of type IV and VI collagens, LH mutant mice show ultrastructural alterations in their skin and muscle
additional information
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glucosyltransferase, GGT, deficiency, e.g. in the Finnish epidermolysis bullosa simplex family, due to a transcriptional defect in one LH3 allele affects the extracellular matrix deposition and the arrangement of the cytoskeleton in skin fibroblasts, phenotype, overview
additional information
glucosyltransferase, GGT, deficiency, e.g. in the Finnish epidermolysis bullosa simplex family, due to a transcriptional defect in one LH3 allele affects the extracellular matrix deposition and the arrangement of the cytoskeleton in skin fibroblasts, phenotype, overview
additional information
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mutations in the LH3 gene cause connective tissue disorder. Genotype-phenotype analysis of PLOD3 mutations, phenotypes, detailed overview
additional information
mutations in the LH3 gene cause connective tissue disorder. Genotype-phenotype analysis of PLOD3 mutations, phenotypes, detailed overview
additional information
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siRNA knockdowns of TIA-1 and TIAL1 both singly and in combination in HEK293 cells decrease the ratio of LH2 (long) to LH2 (short) splicing variants
additional information
-
A668G, higher apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and reduced glucosyltransferase activity, EC 2.4.1.66, about 50% decreased lysyl hydroxylase activity
additional information
A668G, higher apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and reduced glucosyltransferase activity, EC 2.4.1.66, about 50% decreased lysyl hydroxylase activity
additional information
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delT2071, lower apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and reduced glucosyltransferase activity, EC 2.4.1.66, complete loss of lysyl hydroxylase activity
additional information
delT2071, lower apparent molecular mass, reduced collagen galctosyltransferase, EC 2.4.1.50, and reduced glucosyltransferase activity, EC 2.4.1.66, complete loss of lysyl hydroxylase activity
additional information
LH-deficient mutant, deficiency of LH3 glycosyltransferase activity decreases cell growth and increases lethality
additional information
overexpression of LH3, increased hydroxylation of lysyl residues and increased galactosylation and glucosylation of hydroxylysyl residues
additional information
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monomerization inactivates the LH activity of LH3, distribution of monomers, dimers, and multimers in mutant enzyme structures, overview. Glycosyltransferase activity of the mutant enzymes, overview
additional information
generation of an N-terminally truncated enzyme mutant comprising residues 33-758
additional information
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generation of an N-terminally truncated enzyme mutant comprising residues 33-758
additional information
overexpression of isozyme LH2 in osteoblasts induces a switch in the predominant type of collagen cross-link from LCC to HLCC, which qualitatively affects fibrillogenesis and matrix organization
additional information
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overexpression of isozyme LH2 in osteoblasts induces a switch in the predominant type of collagen cross-link from LCC to HLCC, which qualitatively affects fibrillogenesis and matrix organization
additional information
mice with targeted inactivation of the Plod1 gene for lysyl hydroyxylase 1 are flaccid and have gait abnormalities. About 15% of them die because of aortic rupture, and smooth muscle cells in non-ruptured Plod1-/- aortas show degenerative changes. Collagen fibrils in the Plod1-/- aorta and skin have an abnormal morphology. The lysyl hydrolase activity level in the Plod1-/- skin and aorta samples is 35-45% of that in the wild type. The hydroxylysine content is decreased in all the Plod1-/- tissues, ranging from 22% of that in the wild type in the skin to 75% and 86% in the femur and lung, respectively
additional information
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generation of an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein
additional information
generation of mouse osteoblastic cell line, MC3T3-E1, stably suppressing Plod3 expresion using short hairpin RNA technology, reduced LH3 protein levels in the Sh clones, phenotype, overview
additional information
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generation of mouse osteoblastic cell line, MC3T3-E1, stably suppressing Plod3 expresion using short hairpin RNA technology, reduced LH3 protein levels in the Sh clones, phenotype, overview
additional information
in syngeneic wild-type Cdkn1a mice, LH2-deficient KC2 tumors are smaller and generate fewer lung metastases than KC2 tumors transfected with scrambled shRNA do
additional information
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in syngeneic wild-type Cdkn1a mice, LH2-deficient KC2 tumors are smaller and generate fewer lung metastases than KC2 tumors transfected with scrambled shRNA do
additional information
Plod3 knockout by specific siRNA in differentiated 3T3-L1 adipocytes
additional information
Plod3 knockout by specific siRNA in differentiated 3T3-L1 adipocytes
additional information
Plod3 knockout by specific siRNA in differentiated 3T3-L1 adipocytes
additional information
-
generation of an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein
-
additional information
-
generation of mouse osteoblastic cell line, MC3T3-E1, stably suppressing Plod3 expresion using short hairpin RNA technology, reduced LH3 protein levels in the Sh clones, phenotype, overview
-
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