1.14.11.4: procollagen-lysine 5-dioxygenase
This is an abbreviated version!
For detailed information about procollagen-lysine 5-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.4
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1.14.11.4
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prolyl
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ehlers-danlos
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hydroxylysine
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jumonji
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fibrosis
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procollagens
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fragility
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domain-containing
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hydroxylases
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osteogenesis
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4-hydroxylase
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kyphoscoliosis
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imperfecta
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demethylase
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glucosyltransferase
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pyridinoline
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hypermobl
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galactosyltransferase
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contractures
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minoxidil
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hypotonia
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hydroxylysyl
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hypermobility
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bruck
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fkbp10
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hyperelasticity
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underhydroxylated
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sclera
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scoliosis
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laxity
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chick-embryo
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hyperextensibility
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2-oxoglutarate-dependent
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serpinh1
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galactosylhydroxylysyl
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ppib
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medicine
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crtap
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diagnostics
- 1.14.11.4
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prolyl
- ehlers-danlos
- hydroxylysine
-
jumonji
- fibrosis
- procollagens
-
fragility
-
domain-containing
- hydroxylases
-
osteogenesis
-
4-hydroxylase
-
kyphoscoliosis
- imperfecta
- demethylase
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glucosyltransferase
-
pyridinoline
-
hypermobl
-
galactosyltransferase
- contractures
- minoxidil
- hypotonia
-
hydroxylysyl
-
hypermobility
-
bruck
- fkbp10
-
hyperelasticity
-
underhydroxylated
-
sclera
- scoliosis
-
laxity
-
chick-embryo
-
hyperextensibility
-
2-oxoglutarate-dependent
-
serpinh1
-
galactosylhydroxylysyl
- ppib
- medicine
-
crtap
- diagnostics
Reaction
Synonyms
2-oxoglutarate 5-dioxygenase 2, collagen lysine hydroxylase, Jmjd6, L230, LH, LH1, LH2, LH2 (long), LH2a, LH2b, LH3, LH3/PLOD3, lysine hydroxylase, lysine, 2-oxoglutarate 5-dioxygenase, lysine-2-oxoglutarate dioxygenase, lysyl 5S-hydroxylase, lysyl hydroxylase, lysyl hydroxylase 1, lysyl hydroxylase 2, lysyl hydroxylase 2 (long), lysyl hydroxylase 2a, lysyl hydroxylase 2b, lysyl hydroxylase 3, Lysyl hydroxylase-2b, lysyl-hydroxylase 1, lysylhydroxylase 2, lysylprotocollagen dioxygenase, More, multifunctional collagen lysyl hydroxylase, oxygenase, protocollagen lysine, di-, peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase, peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase, PLOD, Plod1, PLOD2, Plod2a, Plod2b, PLOD2iso1, PLOD2iso2, PLOD3, procollagen lysyl hydroxylase 2, procollagen-lysine, procollagen-lysine 2-oxoglutarate 5-dioxygenase, procollagen-lysine 2-oxoglutarate 5-dioxygenase 2, procollagen-lysine, 2-oxoglutarate 5-dioxygenase, procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2, procollagen-lysine,2-oxoglutarate 5-dioxygenase, protocollagen lysine hydroxylase, protocollagen lysyl hydroxylase, telopeptide lysyl hydroxylase, TLH
ECTree
1.14.11.4 procollagen-lysine 5-dioxygenaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + 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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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
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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influence the integrity and stability of collagen
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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enzyme required during collagen biosynthesis
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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enzyme required during collagen biosynthesis
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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influence the integrity and stability of collagen
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
influence the integrity and stability of collagen
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
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?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
influence the integrity and stability of collagen
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?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
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-
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?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
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-
-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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collagen type IV
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-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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-
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?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
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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
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-
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?
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
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
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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collagen and other proteins with collagenous domains
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-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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-
-
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?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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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hydroxylation of lysine residues in collagenous sequences
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-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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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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
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
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-
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?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Mus musculus 714
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-
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?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
additional information
?
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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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-
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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Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
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?
additional information
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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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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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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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LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
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additional information
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LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
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additional information
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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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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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the enzyme is responsible for the hydroxylation of collagen telopeptides
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?
additional information
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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
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?
additional information
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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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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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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
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?
additional information
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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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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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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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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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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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