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Information on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase
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1.14.11.4 procollagen-lysine 5-dioxygenaseIUBMB Comments
Requires Fe2+ and ascorbate.
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Word Map
- 1.14.11.4
-
prolyl
- ehlers-danlos
- hydroxylysine
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jumonji
- procollagens
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fragility
- demethylase
- hydroxylases
-
4-hydroxylase
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kyphoscoliosis
- imperfecta
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osteogenesis
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pyridinoline
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glucosyltransferase
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hydroxylysyl
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col1a1
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galactosyltransferase
- hypotonia
- contractures
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bruck
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hypermobl
- minoxidil
- fkbp10
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hypermobility
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hyperextensibility
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hyperelasticity
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underhydroxylated
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chick-embryo
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laxity
- medicine
- ppib
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crtap
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dihydroxylysinonorleucine
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2-oxoglutarate-dependent
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2-oxoglutarate 5-dioxygenase 2, collagen lysine hydroxylase, Jmjd6, L230, LH, LH1, LH2, LH2 (long), LH2a, LH2b, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate 5-dioxygenase 2
collagen lysine hydroxylase
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L230
LH
LH1
LH2
LH2a
LH2b
LH3
lysine hydroxylase
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lysine, 2-oxoglutarate 5-dioxygenase
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lysine-2-oxoglutarate dioxygenase
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lysyl hydroxylase
lysyl hydroxylase 2
lysyl hydroxylase 3
lysyl-hydroxylase 1
lysylprotocollagen dioxygenase
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oxygenase, protocollagen lysine, di-
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peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase
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peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase
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Plod1
PLOD2
PLOD3
procollagen-lysine, 2-oxoglutarate 5-dioxygenase
protocollagen lysine hydroxylase
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protocollagen lysyl hydroxylase
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additional information
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the enzyme is a member of the 2-oxoglutarate-dependent dioxygenase family
lysyl hydroxylase 3
with lysyl hydroxylase, collagen galactosyltransferase and glucosylransferase activities
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[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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[procollagen]-L-lysine + 2-oxoglutarate + O2 = [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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hydroxylation
redox reaction
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hydroxylation
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hydroxylation
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the enzyme possesses also hydroxylysyl galactosyltransferase and galactosylhydroxylysyl glucosyltransferase activities
hydroxylation
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the multifunctional enzyme associated with collagen biosynthesis possesses lysyl hydroxylase and collagen glycosyltransferase activities
hydroxylation
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the enzyme catalyzes the formation of hydroxylysine by acting on -X-Lys-Gly- triplets in the collagenous domains of proteins of the collagen superfamily and also in -X-Lys-Ala- or -X-Lys-Ser- sequences in the telopeptides located at the ends of the polypeptide chains in some fibril-forming collagens
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SYSTEMATIC NAME
IUBMB Comments
L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Requires Fe2+ and ascorbate.
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CAS REGISTRY NUMBER
COMMENTARY
9059-25-0
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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
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-
-
?
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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-
-
?
L-lysine containing nonapeptides + 2-oxoglutarate + O2
5-hydroxy-L-lysine containing nonapeptides + succinate + CO2
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diverse nonapeptides, synthetic substrates
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-
?
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
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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
(GDK)4 + 2-oxoglutarate + O2
?
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peptide acceptor substrate
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-
?
(GDK)4 + 2-oxoglutarate + O2
?
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peptide acceptor substrate
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-
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
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-
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
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-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
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-
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2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
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uncoupled decarboxylation in absence of peptide substrate
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?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
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2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
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2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
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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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-
-
?
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
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-
-
?
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
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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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-
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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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?
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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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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?
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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?
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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?
KGIKGIKG + 2-oxoglutarate + O2
?
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a synthetic peptide substrate
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?
KGIKGIKG + 2-oxoglutarate + O2
?
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a synthetic peptide substrate
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?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
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?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + 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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-
?
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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-
-
-
?
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
-
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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?
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
-
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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the hydroxylysyl residues are located in Y positions of X-Y-Gly repeats of collagenous sequences
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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-[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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?
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-kilodalton subunit
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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
purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
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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
purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
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-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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-
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
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-
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?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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-
hydroxy-L-lysine
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
-
minimum sequence required: Xaa-Lys-Gly
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-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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in e.g. lysinevasopressin, lysine-rich histone
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-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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helical regions of collagen
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-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
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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
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-
-
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
-
-
-
-
?
[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
-
-
-
?
additional information
?
-
-
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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-
the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
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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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-
the enzyme sequentially hydroxylates and glucosylates collagensubstrates in vitro
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-
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additional information
?
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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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-
-
additional information
?
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-
Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
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-
-
additional information
?
-
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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-
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
?
-
-
LH2 hydroxylates the N telopeptide of the full-length procollagen alpha type I chain when coexpressed with this isoenzyme
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
-
-
-
additional information
?
-
lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
-
-
-
additional information
?
-
-
the enzyme is responsible for the hydroxylation of collagen telopeptides
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
lysyl hydroxylase 3 is a multifunctional enzyme of collagen biosynthesis, with glycosyltransferase activity and lysyl hydroxylase activity
-
-
-
additional information
?
-
-
in absence of substrate JMJD6 catalyses turnover of 2-oxoglutarate to succinate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
isozyme LH2a possesses telopeptide lysyl hydroxylase activity
-
-
-
additional information
?
-
-
isozyme LH2a possesses telopeptide lysyl hydroxylase activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
-
?
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
-
-
-
?
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + 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
-
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
enzyme required during collagen biosynthesis
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
influence the integrity and stability of collagen
-
?
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
-
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
-
-
-
?
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
C-terminally FLAG-tagged rat MBL-A
-
-
?
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
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
-
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
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
-
-
-
-
?
[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
-
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
Ehlers-Danlos syndrome type VIA patients show highly reduced enzyme activity
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
LH3 is responsible for hydroxylysine formation and also for hydroxylysine glycosylations in polypeptides, enzyme mutations cause a severe phenotype, detailed overview
-
-
-
additional information
?
-
lysyl hydroxylase catalyzes the posttranslational formation of hydroxylysines in -X-Lys-Gly- sequences in collagens and other proteins with collagen-like domains
-
-
-
additional information
?
-
-
the enzyme is responsible for the hydroxylation of collagen telopeptides
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
lysyl hydroxylase 3 is a multifunctional enzyme of collagen biosynthesis, with glycosyltransferase activity and lysyl hydroxylase activity
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
-
-
-
additional information
?
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
NaCl
-
reduces the activity of the isozymes LH1, LH2a, LH2b, and LH3 with most of the synthetic nonpeptide substrates tested, in some cases the isozyme is activated or completely inhibited, overview
Fe2+
-
a peptide fold in the iron-binding site, within the 40 amino acid residues at the C-terminus, is responsible for KDEL-receptor-independent localization in the endoplasmic reticulum
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dipyridyl
a non-specific hydroxylase inhibitor; a non-specific hydroxylase inhibitor; a non-specific hydroxylase inhibitor
L-alpha-hydroxyglutarate
-
the enzyme activity is inhibited by L-alpha-hydroxyglutarate but not its enantiomer D-alpha-hydroxyglutarate
NaCl
-
reduces the activity of the isozymes LH1, LH2a, LH2b, and LH3 with most of the synthetic nonpeptide substrates tested, in some cases the isozyme is activated or completely inhibited, overview
additional information
the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. 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. CRTAP, a non-enzymic member of the Leprecan family of proteins which includes Synaptonemal Complex 65 (SC65) and the prolyl 3-hydroxylases (P3H1, P3H2 and P3H3), is an essential third subunit of a complex with prolyl 3-hydroxylase 1 (aka LEPRECAN) and cyclophilin B (CYPB) in the endoplasmic reticulum, forming the so-called collagen prolyl 3-hydroxylation complex
-
minoxidil
-
0.4 mM inhibits LH1 completely, 1 mM inhibits LH2b and LH3 incompletely
minoxidil
specific inhibition of lysyl hydroxylases; specific inhibition of lysyl hydroxylases; specific inhibition of lysyl hydroxylases
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cannabidiol
CBD, a major non-psychotropic cannabis constituent, stimulates lysyl hydroxylase 1 activity in osteoblasts, cannabidiol enhances the biomechanical properties of healing rat mid-femoral fractures
DELTA9-tetrahydrocannabinol
THC, the psychotropic cannabis constituent, stimulates lysyl hydroxylase 2 activity in osteoblasts
FKBP65
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
-
additional information
no stimulating effect of LH1 by DELTA9-tetrahydrocannabinol (THC), but THC potentiates the CBD stimulated work-to-failure at 6 weeks postfracture followed by attenuation of the CBD effect at 8 weeks
-
additional information
no stimulating effect of LH1 by DELTA9-tetrahydrocannabinol (THC), but THC potentiates the CBD stimulated work-to-failure at 6 weeks postfracture followed by attenuation of the CBD effect at 8 weeks
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
comparison of Km of 2-oxoglutarate, ascorbate, Fe2+ and type I, type II and type IV protocollagen as substrate with type I, type II and type IV enzyme
-
additional information
additional information
-
comparison of Km of 2-oxoglutarate, ascorbate, Fe2+ and type I, type II and type IV protocollagen as substrate with type I, type II and type IV enzyme
-
additional information
additional information
-
Km of recombinant isozymes LH1, LH2a, LH2b, and LH3 for diverse synthetic nonpeptide substrates, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity of the recombinant enzyme three-fold higher than the specific activity of native enzyme
additional information
-
specific activity of the recombinant enzyme three-fold higher than the specific activity of native enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene dPlod, or CG6199, encoding the only lysyl hydroxylase of the organism
-
-
brenda
-
349014, 439148, 439149, 439150, 439151, 439152, 439153, 439154, 439156, 439157, 439158, 439159, 439160, 439162, 439169
-
-
brenda
-
-
-
brenda
2 splicing variants of isozyme LH2, termed LH2long and LH2short
SwissProt
brenda
3 isozymes LH1-3, isozyme LH2 exists in 2 splicing variants LH2a and LH2b
-
-
brenda
; isoform LH3, possessing lysyl hydroxylase, collagengalactosyltransferase and glucosyltransferase activities
UniProt
brenda
isozyme LH2, gene PLOD2; gene PLOD2 encoding isozyme LH2
SwissProt
brenda
isozyme lysyl hydroxylase 1, i.e. LH1, Ehlers-Danlos syndrome type VIA patients
-
-
brenda
3 isozymes LH1-3, isozyme LH2 occurs in 2 splicing variant, 2a and 2b, the first without insert
-
-
brenda
ob/ob mice and age-matched C57/BL littermates as non-obese controls, phenotype comparison, overview
UniProt
brenda
ob/ob mice and age-matched C57/BL littermates as non-obese controls, phenotype comparison, overview
SwissProt
brenda
ob/ob mice and age-matched C57/BL littermates as non-obese controls, phenotype comparison, overview
UniProt
brenda
isozyme LH2b; 3 isozymes LH1-3; ospzyme LH2a; 3 isozymes LH1-3
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
p21-deficient (KC) and -replete (K) murine lung adenocarcinoma cells, increased LH2 enzyme activity
brenda
stem marrow cell, no expression of isozymes LH3 and LH2b
brenda
in the hatching larvae, LH1 is expressed in the pectoral fin bud; in the hatching larvae, LH3 is expressed in the pectoral fin bud
brenda
4 lung adenocarcinoma cell lines (KC1–KC4) from lung tumors in KC mice and 2 lung adenocarcinoma cell lines (K1 and K2) from Cdkn1aWT K-rasLA1 mice. Expression levels of the third gene of interest, LH2, are 10-30 times higher in the highly metastatic KC cells and include both LH2 isoforms, full-length (LH2b) and spliced at exon 13 (LH2a)
brenda
-
increased LH2 enzyme activity in lung carcinoma compared to healthy lung
brenda
lysyl hydroxylases are expressed in white-adipose tissue of ob/ob mice, overview; lysyl hydroxylases are expressed in white-adipose tissue of ob/ob mice, wherein LH3 levels are increased compared with C57/BL controls. Expression levels of mRNAs corresponding to LH1 (Plod1) and LH3 (Plod3) are both altered in ob/ob mice, in the same direction as the changes in serum levels of adiponectin and the HMW isoforms; lysyl hydroxylases are expressed in white-adipose tissue of ob/ob mice, wherein LH3 levels are increased compared with C57/BL controls. Expression levels of mRNAs corresponding to LH1 (Plod1) and LH3 (Plod3) are both altered in ob/ob mice, in the same direction as the changes in serum levels of adiponectin and the HMW isoforms
brenda
additional information
-
PLOD2 is mainly expressed within the tunica media of the blood vessels
brenda
-
-
brenda
tissue expression profiles of the three isozymes are different, quantitative expression analysis, in situ localizations, overview; tissue expression profiles of the three isozymes are different, quantitative expression analysis, in situ localizations, overview; tissue expression profiles of the three isozymes are different, quantitative expression analysis, in situ localizations, overview
brenda
head and body; head and body; head and body
brenda
-
different clones, osteoblastic cell line, expression of splicing vaiant 2b of isozyme LH2, but not of splicing variant 2a, expression analysis of the 3 isozymes in MC3T3-E1 cells and comparison of collagen cross-linking activities, overview
brenda
ordinary and dark; ordinary and dark; ordinary and dark, high expression of lysine hydroxylase 1
brenda
additional information
-
developmental expression patterns of dPlod RNA and protein during embryogenesis,overview. dPlod is highly expressed in type-IV collagen-producing cells, particularly the hemocytes and fat body
brenda
additional information
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, cartilage, spleen, liver, and placenta, not in skin, lung, aorta, and dura
brenda
additional information
-
PLOD2 expression determination by immunhistochemic analysis
brenda
additional information
isozymes LH1 and LH2a are expressed in all tissues, isozymes LH2b and LH3 are expressed in almost all tissues, no tissue specificity; the 3 isozymes are expressed in almost all tissues, no tissue specificity; the 3 isozymes are expressed in almost all tissues, no tissue specificity
brenda
additional information
-
isozymes LH1 and LH2a are expressed in all tissues, isozymes LH2b and LH3 are expressed in almost all tissues, no tissue specificity; the 3 isozymes are expressed in almost all tissues, no tissue specificity; the 3 isozymes are expressed in almost all tissues, no tissue specificity
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
LH3 found on the cell surface bypasses the Golgi complex
brenda
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LH3 is the only secreted LH isoform, secretion of LH3 into the cell medium occurs through both the apical and basolateral plasma membranes of epithelial MDCK cells
-
brenda
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LH3 is the only secreted LH isoform, secretion of LH3 into the cell medium occurs through both the apical and basolateral plasma membranes of epithelial MDCK cells
-
-
brenda
LH3 is the only secreted LH isoform, LH3 is secreted by two pathways, one through the Golgi complex leading to EndoH resistant LH3, and the other by-passing the Golgi complex and leading to EndoH sensitive LH3
-
brenda
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enzyme binds to membrane via weak electrostatic interactions
brenda
additional information
-
LH3 secretory pathways leading to both surfaces of the cells and the non-polarized secretion of LH3 in MDCK cells
-
brenda
additional information
-
LH3 secretory pathways leading to both surfaces of the cells and the non-polarized secretion of LH3 in MDCK cells
-
-
brenda
additional information
-
a peptide fold in the iron-binding site, within the 40 amino acid residues at the C-terminus, is responsible for KDEL-receptor-independent localization in the endoplasmic reticulum
-
brenda
additional information
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
-
brenda
additional information
-
lysyl hydroxylase 3 is a multifunctional protein that localizes to the endoplasmic reticulum but is also secreted into the extracellular space and is associated with collagenous proteins on the cell surface
-
brenda
additional information
isozyme LH1 contains a signal peptide comprising residues Met1-Cys20; isozyme LH2a contains a signal peptide comprising residues Met1-Ser19; isozyme LH3 contains a signal peptide comprising residues Met1-Ala21
-
brenda
additional information
isozyme LH1 contains a signal peptide comprising residues Met1-Cys20; isozyme LH2a contains a signal peptide comprising residues Met1-Ser19; isozyme LH3 contains a signal peptide comprising residues Met1-Ala21
-
brenda
additional information
isozyme LH1 contains a signal peptide comprising residues Met1-Cys20; isozyme LH2a contains a signal peptide comprising residues Met1-Ser19; isozyme LH3 contains a signal peptide comprising residues Met1-Ala21
-
brenda
additional information
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isozyme LH1 contains a signal peptide comprising residues Met1-Cys20; isozyme LH2a contains a signal peptide comprising residues Met1-Ser19; isozyme LH3 contains a signal peptide comprising residues Met1-Ala21
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
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
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
-
malfunction
-
disorders of LH3 with a unique phenotype causing severe morbidity as a result of feauters that overlap with collagen disorders; 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; 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
-
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
impairment of LH3 function significantly affects type I collagen fibrillogenesis
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
-
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
-
enzyme LH3 downregulation decreases MMP-9 recruitment to MRC-5 and thus MMP-9/LH3 interaction
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
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; 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; 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
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
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
Mus musculus 714
-
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
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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; 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
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malfunction
-
impairment of LH3 function significantly affects type I collagen fibrillogenesis
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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; essential roles of insulin, AMPK signaling and lysyl and prolyl hydroxylases in the biosynthesis and multimerization of adiponectin, pathway regulation, detailed overview; 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
Mus musculus 714
-
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
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physiological function
-
forms part of the many posttranslational modifications required during collagen biosynthesis
physiological function
the enzyme LH3 has an important role in the organization of the extracellular matrix and the cytoskeleton; the enzyme LH3 has an important role in the organization of the extracellular matrix and the cytoskeleton
physiological function
-
the enzyme is responsible for the hydroxylation of collagen telopeptides
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 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
lysyl hydroxylase (LH) catalyzes the hydroxylation of lysine residues in collagens, and contributes to the formation of more stable collagen cross-links; lysyl hydroxylase (LH) catalyzes the hydroxylation of lysine residues in collagens, and contributes to the formation of more stable collagen cross-links; lysyl hydroxylase (LH) catalyzes the hydroxylation of lysine residues in collagens, and contributes to the formation of more stable collagen cross-links
physiological function
-
dPlod is required for type-IV collagen secretion from hemocytes and fat body
physiological function
lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture, role of LH3 in bone physiology
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
-
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
-
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
-
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
-
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 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 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; the enzyme LH2 catalyzes lysine hydroxylation, which is involved in collagen crosslinking and stabilization. PLOD2 has no role in determining bone quality; the enzyme LH3 catalyzes lysine hydroxylation
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
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
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; 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; 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
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
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
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
-
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
-
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
Mus musculus 714
-
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
-
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; 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
-
lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture, role of LH3 in bone physiology
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
200000
42000
x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343
82380
-
2 * 82380, calculation from amino acid sequence, recombinant enzyme: isoform 3
85000
86000
88000
-
2 * 88000 or 97000 SDS-PAGE, recombinant enzymes: isoform 2, possibly two forms are due to variation in the glycosylation of enzymes
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
structure of the catalytic domain of recombinant His-tagged JMJD6 and active site structure, overview
?
x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343
?
x * 84385, isozyme LH1, sequence calculation; x * 84558, isozyme LH3, sequence calculation; x * 85063, isozyme LH2a, sequence calculation
dimer
-
localization of the region responsible for the dimerization of lysyl hydroxylase 3, to a sequence of amino acids between the glycosyltransferase activity and the lysyl hydroxylase activity domains. This area is covered by amino acids 541-547 and contains no cysteine residues
homodimer
-
2 * 88000 or 97000 SDS-PAGE, recombinant enzymes: isoform 2, possibly two forms are due to variation in the glycosylation of enzymes
homodimer
-
2 * 82380, calculation from amino acid sequence, recombinant enzyme: isoform 3
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
side-chain modification
additional information
-
posttranslational hydroxylation in both the cytoplasm and the nucleoplasm is ubiquitous
glycoprotein
isozyme LH1 contains 4 glycosylation sites; isozyme LH2a contains 7 glycosylation sites; isozyme LH3 contains 4 glycosylation sites
side-chain modification
-
hydroxylation of lysyl residue in -X-Lys-Gly
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged SeMet-derivatised and wild-type JMJD61-343, at both 20°C and 4°C by the sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.75-2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D250A
-
site-directed mutagenesis, the mutant shows unaltered lysyl hydroxylase activity, although reduced collagen glucosyltransferase activity, compared to the wild-type enzyme
D97A/D99A
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
H80A
-
site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
H825S/D827A
-
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
-
D97A/D99A
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
-
H80A
-
site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
-
H825S/D827A
-
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
-
G597V
-
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
K694G
-
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
R594H
-
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
-
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
additional information
D669A
-
site-directed mutagenesis, inactive mutant; site-directed mutagenesis, inactive mutant
-
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
-
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; 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; mutations in the LH3 gene cause connective tissue disorder. Genotype-phenotype analysis of PLOD3 mutations, phenotypes, detailed 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; 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
LH-deficient mutant, deficiency of LH3 glycosyltransferase activity decreases cell growth and increases lethality; overexpression of LH3, increased hydroxylation of lysyl residues and increased galactosylation and glucosylation of hydroxylysyl residues; 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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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
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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
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generation of an N-terminally truncated enzyme mutant comprising residues 33-758
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
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 an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein
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
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
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generation of an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein
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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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by freezing/thawing
labile in tissue extracts
loss of activity during concentration
stabilization by detergents, NaCl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-20°C, enzyme purified by collagen-agarose column-chromatography stable, enzyme from Bio-gel column unstable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ProBond metal chelate affinity resin chromatography and Chelating Sepharose fast flow column chromatography
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recombinant His-tagged full-length JMJD6 and JMJD61-343 from Escherichia coli strain Rosetta by nickel affinity chromatography
recombinant His-tagged isozymes LH1-3 from Sf9 insect cells by nickel affinity chromatography
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recombinant His10-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant V5/His-tagged LH3 protein from HEK-293 cells by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant wild-type and mutant enzymes from Sf9 insect cells by chelating affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
all 3 isozymes LH1-3, LH2 in 2 splicing variants, are expressed in as His-tagged proteins in Spodoptera frugiperda Sf9 cells via baculovirus infection system with the signal peptide at the N-terminus in isozymes LH2a and b and LH3 being exchanged for the signal peptide of isozyme LH1
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cloning of 3 isozymes LH1-3, with 2 splicing variants of isozyme LH2, LH2a and LH2b, stable and functional expression in CHO-K1 cells; cloning of 3 isozymes LH1-3, with 2 splicing variants of isozyme LH2, LH2a and LH2b, stable and functional expression in CHO-K1 cells
DNA and amino acid sequence determination and analysis of mutant DNA from an Ehlers-Danlos syndrome type IVA patient, expression of mutant enzyme W446G in an insect cell system via baculovirus infection
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endogenous LH2 alternate splicing pattern and conservation analysis of LH2 genomic sequence., overview. Construction and expression of a functional LH2 minigene in HEK-293 cells, human neonatal skin fibroblasts, and mouse embryonic fibroblasts. The TIA proteins play a role in the regulation of the alternative splicing of LH2, overview
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expression in Escherichia coli, isoform 3 gene product possesses the collagen glycosyltransferase activity, but not isoform 1 and 2
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expression in insect cells using a baculovirus vector
expression in insect cells using a baculovirus vector; expression in various human tissues
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expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, and functional expression of N-terminally His10-tagged enzyme in Escherichia coli strain BL21(DE3)
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expression of 40 amino acid residues of the C-terminal end of isozyme LH1 fused to human cathepsin D and c-Myc-tagged and 2 mutant variants thereof in COS-7 cells
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expression of a synthetic gene encoding LH3, SEQ ID, in Nicotiana tabacum leaves. Co-expression of the human genes encoding recombinant heterotrimeric collagen type I, rhCOL1, the human prolyl-4-hydroxylase, and the lysyl hydroxylase 3, all responsible for key posttranslational modifications of collagen. Plants coexpressing all five vacuole-targeted proteins generate intact procollagen yields ofabout 2% of the extracted total soluble protein, overview
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expression of active LH2b and of antisense construct in MC3T3-E1 cells, the latter suppresses the endogenous enzyme
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expression of GFP-tagged Jmjd6 in HEK-293 cells, GFP pulldown interaction analysis with U2AF65, overview
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expression of His-tagged full-length JMJD6 and JMJD61-343 in Escherichia coli strain Rosetta
expression of wild-type and mutantenzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method
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gene dPlod or CG6199, maps to cytological position 68B1 on the left arm of the third chromosome, DNA and amino acid sequence determination and analysis, sequence comparisons
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gene encoding isozyme LH1, DNA and amino acid sequence determination and analysis, quantitative expression analysis; gene encoding isozyme LH2a, DNA and amino acid sequence determination and analysis, quantitative expression analysis; gene encoding isozyme LH3, DNA and amino acid sequence determination and analysis, quantitative expression analysis
gene Plod1, quantitative RT-PCR enzyme expression analysis; gene Plod3, quantitative RT-PCR enzyme expression analysis; genes Plod2a and Plod2b, quantitative RT-PCR enzyme expression analysis
gene Plod1, real-time RT-PCR enzyme expression analysis; gene Plod2, real-time RT-PCR enzyme expression analysis; gene Plod3, real-time RT-PCR enzyme expression analysis
gene PLOD2
gene PLOD2, 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. Depletion of SMAD3 reduces gene PLOD2 acetylated H3 and H4, histone methylation marks at the PLOD2 promoter depicted an increase of the active histone mark H3K79me2, a decrease of the repressive H4K20me3 mark, but no role for the generally strong transcription-related modifications: H3K4me3, H3K9me3 and H3K27me3. TGFbeta1 induces a SP1- and SMAD3-dependent recruitment of histone modifying enzymes to the PLOD2 promoter other than the currently known TGFbeta1 downstream co-activators and epigenetic modifications. Quantitative real-time PCR enzyme expression analysis
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gene PLOD2, encoding for splice variants LH2a and LH2b, quantitative expression analysis of LH2b
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gene PLOD2, large-scale transfection with N-terminal His8 and human growth hormone (hGH) tags transfection with polyethylenimine and recombinant expression of wild-type enzyme, N-terminally truncated enzyme mutant, and of inactive mutant D689A in engineered CHO cells and secretion to the cell culture medium
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gene PLOD3, DNA and amino acid sequence determination and analysis, quantitative expression analysis
gene PLOD3, expression in COS-7 and HT-1080 cells, the enzyme is secreted into the culture medium, expression of enzyme mutants in COS-7 cells
gene Plod3, expression of recombinant V5/His-tagged LH3 protein in HEK-293 cells
genomic structure of isozyme LH2, expression analysis of the 2 splicing variants of isozyme LH2
overexpression in HT-1080 cells, expression of fragments in Escherichia coli
quantitative LH gene expression analysis by realtime PCR, genes LH2a and LH2b DNA and amino acid sequence analysis using RT-PCR
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transient transfection of HA-tagged LH1 in 714 mouse embryonic fibroblasts
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cannabidiol stimulates mRNA expression of Plod1 in primary osteoblast cultures; DELTA9-tetrahydrocannabinol stimulates mRNA expression of Plod2 in primary osteoblast cultures
gene expressions of isozymes LH1, LH2b and LOXL2 are significantly upregulated by 1,25(OH)2D3, the active form of vitamin D
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hypoxia-inducible factor 1 activates transcription of the PLOD1 and PLOD2 genes in hypoxic breast cancer cells, knockdown of HIF-1a expression blocks PLOD1 and PLOD2 induction under hypoxic conditions
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in osteoarthritic human synovial fibroblasts, the enzyme expression is induced by TGF-beta via kinase ALK5, not ALK1, and Smad2/3P
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no induction of PLOD3 expression in osteoblasts by DELTA9-tetrahydrocannabinol and cannabidiol
overexpression of the TIA proteins in HEK-293 cells leads to an increase in levels of the LH2(long) spliced product in the minigene
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procollagen lysyl hydroxylase 2 expression is regulated by an alternative downstream transforming growth factor beta-1 activation mechanism. TGF-beta1 induces the enzyme, mechanism of TGFbeta1-enhanced PLOD2 expression, detailed overview
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reduction of TIA protein levels in mous embryonic fibroblasts and HEK-293 cells leads to a corresponding decrease in the LH2(long) spliced product in both the minigene and the endogenous gene
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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PLOD expression is associated with human breast cancer progression, PLOD2 expression is specifically prognostic in breast cancer
medicine
medicine
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deficiency in enzyme activity causes the Ehler-Danlos syndrome type 6
medicine
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deficiency in enzyme activity causes the Ehler-Danlos syndrome type 6
medicine
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LH2b is an interesting target to interfere with osteoarthritis-related persistent fibrosis
medicine
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isozyme LH2 is of interest as candidate mediator of a p21-independent transcriptional program that regulates the metastatic propensity of KC cells. LH2 promotes lung cancer metastatic behavior and predicts poor prognosis in patients
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Majamaa, K.; Turpeenniemi-Hujanen, T.M.; Latipää, P.; Gunzler, V.; Hanauske-Abel, H.M.; Hassinen, I.E.; Kivirikko, K.I.
Differences between collagen hydroxylases and 2-oxoglutarate dehydrogenase in their inhibition by structural analogues of 2-oxoglutarate
Biochem. J.
229
127-133
1985
Gallus gallus
brenda
Kivirikko, K.I.; Myllylä, R.
The hydroxylation of prolyl and lysyl residues
Enzymol. Post- transl. Modif. Proteins (Freedman, R. B. , Hawkins, H. C. , eds. ) Academic Press, New York
1
53-104
1980
Gallus gallus
-
brenda
Kivirikko, K.I.; Myllylä, R.
Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
Methods Enzymol.
82
245-304
1982
Gallus gallus, Homo sapiens
brenda
Puistola, U.
Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types
Biochem. J.
201
215-219
1982
Gallus gallus, Homo sapiens
brenda
Royce, P.M.; Barnes, M.J.
Failure of highly purified lysyl hydroxylase to hydroxylate lysyl residues in the non-helical regions of collagen
Biochem. J.
230
475-480
1985
Gallus gallus
brenda
Puistola, U.; Turpeenniemi-Hujanen, T.M.; Myllylä, R.; Kivirikko, K.I.
Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects
Biochim. Biophys. Acta
611
40-50
1980
Gallus gallus
brenda
Puistola, U.; Turpeenniemi-Hujanen, T.M.; Myllylä, R.; Kivirikko, K.I.
Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism
Biochim. Biophys. Acta
611
51-60
1980
Gallus gallus
brenda
Turpeenniemi-Hujanen, T.M.; Puistola, U.; Kivirikko, K.I.
Isolation of lysyl hydroxylase, an enzyme of collagen synthesis, from chick embryos as a homogeneous protein
Biochem. J.
189
247-253
1980
Gallus gallus
brenda
Miller, R.L.; Varner, H.H.
Purification and enzymatic properties of lysyl hydroxylase from fetal procine skin
Biochemistry
18
5928-5932
1979
Sus scrofa
-
brenda
Murray, J.C.; Cassell, R.H.; Pinnell, S.R.
Inhibition of lysyl hydroxylase by catechol analogs
Biochim. Biophys. Acta
481
63-70
1977
Gallus gallus
brenda
Ryhänen, L.
Lysyl hydroxylase. Further purification and characterization of the enzyme from chick embryos and chick embryo cartilage
Biochim. Biophys. Acta
438
71-89
1976
Gallus gallus
brenda
Kivirikko, K.I.; Shudo, K.; Sakakibara, S.; Prockop, D.J.
Studies on protocollagen lysine hydroxylase. Hydroxylation of synthetic peptides and the stoichiometric decarboxylation of alpha-ketoglutarate
Biochemistry
11
122-129
1972
Gallus gallus
brenda
Popenoe, E.A.; Aronson, R.B.
Partial purification and properties of collagen lysine hydroxylase from chick embryos
Biochim. Biophys. Acta
258
380-386
1972
Gallus gallus
brenda
Kivirikko, K.I.; Prockop, D.J.
Partial purification and characterization of protocollagen lysine hydroxylase from chick embryos
Biochim. Biophys. Acta
258
366-379
1972
Gallus gallus
brenda
Hausmann E.
Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen
Biochim. Biophys. Acta
133
591-593
1967
Gallus gallus
brenda
Kellokumpu, S.; Sormunen, R.; Heikkinen, J.; Myllyla, R.
Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum
J. Biol. Chem.
269
30524-30529
1994
Homo sapiens
brenda
Valtavaara, M.; Papponen, H.; Pirttilae, A.M.; Hiltunen, K.; Helander, H.; Myllylae, R.