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Information on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase and Organism(s) Rattus norvegicus and UniProt Accession Q63321

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IUBMB Comments
Requires Fe2+ and ascorbate.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q63321
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
jmjd6, plod2, lysyl hydroxylase, plod1, plod3, lysyl hydroxylase 2, lysyl hydroxylase 3, lysyl hydroxylase 1, procollagen-lysine 2-oxoglutarate 5-dioxygenase 2, procollagen-lysine 2-oxoglutarate 5-dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
collagen lysine hydroxylase
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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
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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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procollagen-lysine 2-oxoglutarate 5-dioxygenase
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protocollagen lysine hydroxylase
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protocollagen lysyl hydroxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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redox reaction
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hydroxylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Requires Fe2+ and ascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
9059-25-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
show the reaction diagram
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
[procollagen] L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
-
-
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r
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
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-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
show the reaction diagram
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
hydroxylation of lysine residues collagen causes cross-linking with pyrolidine
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-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
malaoxon
mechanism of inhibition
malathion
mechanism of inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.106
2-oxoglutarate
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0.122
ascorbate
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0.1
Procollagen L-lysine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047
malaoxon
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0.059
malathion
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
stem marrow cell, no expression of isozymes LH3 and LH2b
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes lysine hydroxylation, which is involved in collagen crosslinking and stabilization. Critical mechanical role of collagen crosslinking enzymes, e.g. in bone healing. Lysyl hydroxylase 1 (PLOD1) is one of the few collagen crosslinking enzymes associated with bone quality
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PLOD1_RAT
728
0
83612
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
x * 85000, SDS-PAGE and Western blotting
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 85000, SDS-PAGE and Western blotting
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
hydroxylation of lysyl residue in -X-Lys-Gly
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in insect cells using a baculovirus vector
gene Plod1, real-time RT-PCR enzyme expression analysis
cloning of 3 isozymes LH1-3, with 2 splicing variants of isozyme LH2, LH2a and LH2b, stable and functional expression in CHO-K1 cells
gene Plod2, real-time RT-PCR enzyme expression analysis
gene Plod3, real-time RT-PCR enzyme expression analysis
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
no induction of PLOD3 expression in osteoblasts by DELTA9-tetrahydrocannabinol and cannabidiol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
deficiency in enzyme activity causes the Ehler-Danlos syndrome type 6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Samimi, A.; Last, J.A.
Mechanism of inhibition of lysyl hydroxylase activity by the organophosphates malathion and malaoxon
Toxicol. Appl. Pharmacol.
176
181-186
2001
Rattus norvegicus (Q63321)
Manually annotated by BRENDA team
Armstrong, L.C.; Last, J.A.
Rat lysyl hydroxylase: molecular cloning, mRNA distribution and expression in a baculovirus system
Biochim. Biophys. Acta
1264
93-102
1995
Gallus gallus, Homo sapiens, Rattus norvegicus (Q63321)
Manually annotated by BRENDA team
Mercer, D.K.; Nicol, P.F.; Kimbembe, C.; Robins, S.P.
Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms
Biochem. Biophys. Res. Commun.
307
803-809
2003
Rattus norvegicus, Rattus norvegicus (Q811A3)
Manually annotated by BRENDA team
Kogan, N.M.; Melamed, E.; Wasserman, E.; Raphael, B.; Breuer, A.; Stok, K.S.; Sondergaard, R.; Escudero, A.V.; Baraghithy, S.; Attar-Namdar, M.; Friedlander-Barenboim, S.; Mathavan, N.; Isaksson, H.; Mechoulam, R.; Mueller, R.; Bajayo, A.; Gabet, Y.; Bab, I.
Cannabidiol, a major non-psychotropic cannabis constituent enhances fracture healing and stimulates lysyl hydroxylase activity in osteoblasts
J. Bone Miner. Res.
30
1905-1913
2015
Rattus norvegicus (Q5U367), Rattus norvegicus (Q63321), Rattus norvegicus (Q811A3)
Manually annotated by BRENDA team