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
-
1.14.11.4
-
prolyl
-
ehlers-danlos
-
hydroxylysine
-
jumonji
-
fibrosis
-
procollagens
-
fragility
-
domain-containing
-
hydroxylases
-
osteogenesis
-
4-hydroxylase
-
kyphoscoliosis
-
imperfecta
-
demethylase
-
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
- 1.14.11.4
-
prolyl
- ehlers-danlos
- hydroxylysine
-
jumonji
- fibrosis
- procollagens
-
fragility
-
domain-containing
- hydroxylases
-
osteogenesis
-
4-hydroxylase
-
kyphoscoliosis
- imperfecta
- demethylase
-
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 (Substrates Products
Substrates Products on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase
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SUBSTRATE 
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
(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
-
-
-
?
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
-
-
-
?
L-lysine containing nonapeptides + 2-oxoglutarate + O2
5-hydroxy-L-lysine containing nonapeptides + succinate + CO2
-
diverse nonapeptides, synthetic substrates
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
luc7like2(267-278) + 2-oxoglutarate
? + succinate + CO2
substrate is a Luc7like2 protein fragment
-
-
?
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
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
(GDK)4 + 2-oxoglutarate + O2
?
-
peptide acceptor substrate
-
-
?
(GDK)4 + 2-oxoglutarate + O2
?
-
peptide acceptor substrate
-
-
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
-
-
-
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
uncoupled decarboxylation in absence of peptide substrate
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
-
-
-
?
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
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-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
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
influence the integrity and stability of collagen
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
influence the integrity and stability of collagen
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
influence the integrity and stability of collagen
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
-
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
influence the integrity and stability of collagen
-
?
KGIKGIKG + 2-oxoglutarate + O2
?
-
a synthetic peptide substrate
-
-
?
KGIKGIKG + 2-oxoglutarate + O2
?
-
a synthetic peptide substrate
-
-
?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[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-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
collagen type IV
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
PLOD2 specifically hydroxylates lysines in the telopeptide of procollagens, whereas PLOD1 is responsible for lysine hydroxylation in the alpha-helical or central domain
-
-
?
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
the hydroxylysyl residues are located in Y positions of X-Y-Gly repeats of collagenous sequences
-
-
?
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
-
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
-
-
?
L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
-
U2AF65 is the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kilodalton subunit
-
-
?
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
-
-
?
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
-
-
?
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
-
-
?
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
minimum sequence required: Xaa-Lys-Gly
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
in e.g. lysinevasopressin, lysine-rich histone
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
helical regions of collagen
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
synthetic peptides
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
synthetic peptides
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
protocollagen
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
protocollagen
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
protocollagen
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
minimum sequence required: Xaa-Lys-Gly
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
synthetic peptides
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
synthetic peptides
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
synthetic peptides
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
protocollagen
hydroxy-L-lysine
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
collagen and other proteins with collagenous domains
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 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 5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
?
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
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
hydroxylation of lysine residues in collagenous sequences
-
-
?
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
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
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
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
hydroxylation of lysine residues collagen causes cross-linking with pyrolidine
-
-
?
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
r
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
r
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
r
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
r
[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
-
-
-
-
?
[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
-
-
-
?
[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
-
-
-
?
[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
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
-
-
?
[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
-
-
-
?
[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
-
-
-
?
[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
Mus musculus 714
-
-
-
?
[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
-
-
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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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the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
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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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the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
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the enzyme is also able to glycosylate hydroxylysyl residues and is functionally similar to the isozyme LH3 of vertebrates
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Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
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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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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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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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LH2 hydroxylates the N telopeptide of the full-length procollagen alpha type I chain when coexpressed with this isoenzyme
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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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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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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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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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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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the enzyme is responsible for the hydroxylation of collagen telopeptides
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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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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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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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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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lysyl hydroxylase 3 is a multifunctional enzyme of collagen biosynthesis, with glycosyltransferase activity and lysyl hydroxylase activity
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in absence of substrate JMJD6 catalyses turnover of 2-oxoglutarate to succinate
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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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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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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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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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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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FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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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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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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isozyme LH2a possesses telopeptide lysyl hydroxylase activity
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isozyme LH2a possesses telopeptide lysyl hydroxylase activity
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