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Information on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase and Organism(s) Mus musculus and UniProt Accession Q9R0E2
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1.14.11.4 procollagen-lysine 5-dioxygenaseIUBMB Comments
Requires Fe2+ and ascorbate.
Specify your search results
Word Map
- 1.14.11.4
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prolyl
- ehlers-danlos
- hydroxylysine
-
jumonji
- fibrosis
- procollagens
-
fragility
-
domain-containing
- hydroxylases
-
osteogenesis
-
4-hydroxylase
-
kyphoscoliosis
- imperfecta
- demethylase
-
glucosyltransferase
-
pyridinoline
-
hypermobl
-
galactosyltransferase
- contractures
- minoxidil
- hypotonia
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hydroxylysyl
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hypermobility
-
bruck
- fkbp10
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hyperelasticity
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underhydroxylated
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sclera
- scoliosis
-
laxity
-
chick-embryo
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hyperextensibility
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2-oxoglutarate-dependent
-
serpinh1
-
galactosylhydroxylysyl
- ppib
- medicine
-
crtap
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
collagen lysine hydroxylase
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LH1
LH2
LH2b
LH3
lysine hydroxylase
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-
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lysine, 2-oxoglutarate 5-dioxygenase
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lysine-2-oxoglutarate dioxygenase
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lysyl hydroxylase 3
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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protocollagen lysine hydroxylase
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protocollagen lysyl hydroxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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redox reaction
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-
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hydroxylation
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
SYSTEMATIC NAME
IUBMB Comments
L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Requires Fe2+ and ascorbate.
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
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
adiponectin-L-lysine + 2-oxoglutarate + O2
adiponectin-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
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-
-
-
?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
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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
[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
-
-
-
?
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
C-terminally FLAG-tagged rat MBL-A
-
-
?
mannan-binding lectin-A-L-lysine + 2-oxoglutarate + O2
mannan-binding lectin-A-5-hydroxy-L-lysine + succinate + CO2
purified recombinant C-terminally FLAG-tagged MBL-A from Rattus norvegicus
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-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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-
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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isozyme LH2b directs the collagen cross-linking pathways, lysine hydroxylation as post-translational modification critical for collagen cross-linking and glycosylation, isozyme LH2 modulates the cross-linking pattern
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-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
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-
-
-
?
additional information
?
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-
1,25(OH)2D3 directly regulates collagen cross-linking in MC3T3-E1 cells likely by upregulating gene expression of specific lysyl hydroxylase and lysine oxidase enzymes, overview
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-
?
additional information
?
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lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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-
?
additional information
?
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lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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-
?
additional information
?
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FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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-
?
additional information
?
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FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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-
?
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
[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
-
-
-
?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + 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
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
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isozyme LH2b directs the collagen cross-linking pathways, lysine hydroxylation as post-translational modification critical for collagen cross-linking and glycosylation, isozyme LH2 modulates the cross-linking pattern
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
-
-
-
?
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
?
-
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lysyl hydroxylase 3 is the multifunctional collagen-modifying enzyme possessing lysyl hydroxylase, hydroxylysine galactosyltransferase, and galactosylhydroxylysine-glucosyltransferase activities, lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen
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-
?
additional information
?
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FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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-
?
additional information
?
-
-
FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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additional information
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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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ob/ob mice and age-matched C57/BL littermates as non-obese controls, phenotype comparison, overview
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
p21-deficient (KC) and -replete (K) murine lung adenocarcinoma cells, increased LH2 enzyme activity
4 lung adenocarcinoma cell lines (KC1KC4) 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)
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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
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
metabolism
essential roles of insulin, AMPK signaling and lysyl and prolyl hydroxylases in the biosynthesis and multimerization of adiponectin, pathway regulation, detailed overview
physiological function
malfunction
inhibition of prolyl hydroxylation and lysyl hydroxylation/glycosylation affects on adiponectin production, pharmacological LH inhibition causes significant suppression of adiponectin production, more particularly of the higher-order isoforms
malfunction
mice with loss of function of Leprel2 (encoding P3H3) have the same loss of tissue type I collagen lysine-hydroxylation as that observed in the Sc65 knockout mice. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. Sc65KO mouse generation and confirmation of bone loss phenotype, overview
metabolism
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
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
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
malfunction
impairment of LH3 function significantly affects type I collagen fibrillogenesis
malfunction
-
lack of LH3 prevents the formation of hydroxylysine linked Glc-Gal structures in collagen. Secretion of type IV collagen is blocked in embryos that lack LH3 catalyzed Glc-Gal-Hyl residues, and this disrupts formation of the basement membranes that support tissues e.g. blood vessels. Changes in the lysyl hydroxylase activity of LH3 affect the adiponectin level and modifications in mouse, its secretion and oligomer distribtion, phenotype, overview. Recombinant adiponectin produced in LH3-/- knockout fibroblasts cells does not form middle molecular weight and high molecular weight oligomers
malfunction
inhibition of prolyl hydroxylation and lysyl hydroxylation/glycosylation affects on adiponectin production, pharmacological LH inhibition causes significant suppression of adiponectin production, more particularly of the higher-order isoforms
malfunction
inhibition of prolyl hydroxylation and lysyl hydroxylation/glycosylation affects on adiponectin production, pharmacological LH inhibition causes significant suppression of adiponectin production, more particularly of the higher-order isoforms. Transient gene knock-down of LH3 encoding gene Plod3 causes a suppressive effect, especially on the high molecular-weight (HMW) isoforms
malfunction
LH3 knockout studies in mice demonstrate that the loss of LH3 leads to embryonic lethality due to disruption in the formation of basement membranes. The absence of LH3 glycosyltransferase activities are responsible for the lethality. The lack of LH3 leads to loss of all Glc-Gal-Hyl residues in collagens I, IV and VI and prevents the assembly and secretion of type IV and VI collagens. In addition, the mutated LH activity, one out of three activities of LH3, leads to underglycosylation of collagen IV and VI, which is detected as abnormal distribution and aggregation of these collagens in mouse tissues. Oligomerization of recombinant MBL-A is defective in LH3-/- knockout MEF cells
physiological function
lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture, role of LH3 in bone physiology
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
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
LH2 promotes fibrosis and cancer metastasis. Peptidyl prolyl isomerase (PPIase) activity of FKBP65 positively modulates LH2 enzymatic activity and is critical for the formation of hydroxylysine-aldehyde derived intermolecular collagen cross-links. FKBP65 regulates LH2-mediated collagen cross-linking. FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2. Reconstitution with wild-type FKBP65 increases the enzyme activity by 7fold
physiological function
LH3 is essential for catalyzing formation of the glucosylgalactosylhydroxylysines of mannan-binding lectin-A (MBL-A), the first component of the lectin pathway of complement activation. LH3 catalyzes formation of Glc-Gal-Hyl residues in collagens and in collagenous domain of adiponectin. Similar lysine modifications are also present in MBL-A. LH3 also modifies the lysine residues in the collagenous domain of adiponectin, an insulin-sensitizing hormone, and thus affects the oligomerization and secretion of adiponectin
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PLOD1_MOUSE
728
0
83595
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
86000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D669A
additional information
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 an LH3 knockout line, the LH32/2 knockout embryonic fibroblasts totally lack the LH3 protein
additional information
generation of mouse osteoblastic cell line, MC3T3-E1, stably suppressing Plod3 expresion using short hairpin RNA technology, reduced LH3 protein levels in the Sh clones, phenotype, overview
additional information
-
generation of mouse osteoblastic cell line, MC3T3-E1, stably suppressing Plod3 expresion using short hairpin RNA technology, reduced LH3 protein levels in the Sh clones, phenotype, overview
additional information
in syngeneic wild-type Cdkn1a mice, LH2-deficient KC2 tumors are smaller and generate fewer lung metastases than KC2 tumors transfected with scrambled shRNA do
additional information
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant V5/His-tagged LH3 protein from HEK-293 cells by nickel affinity chromatography, dialysis, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Plod1, quantitative RT-PCR enzyme expression analysis
transient transfection of HA-tagged LH1 in 714 mouse embryonic fibroblasts
expression of active LH2b and of antisense construct in MC3T3-E1 cells, the latter suppresses the endogenous enzyme
-
gene Plod3, expression of recombinant V5/His-tagged LH3 protein in HEK-293 cells
gene Plod3, quantitative RT-PCR enzyme expression analysis
genes Plod2a and Plod2b, quantitative RT-PCR enzyme expression analysis
quantitative LH gene expression analysis by realtime PCR, genes LH2a and LH2b DNA and amino acid sequence analysis using RT-PCR
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expressions of isozymes LH1, LH2b and LOXL2 are significantly upregulated by 1,25(OH)2D3, the active form of vitamin D
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pornprasertsuk, S.; Duarte, W.R.; Mochida, Y.; Yamauchi, M.
Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells
J. Bone Miner. Res.
19
1349-1355
2004
Mus musculus
Pornprasertsuk, S.; Duarte, W.R.; Mochida, Y.; Yamauchi, M.
Overexpression of lysyl hydroxylase-2b leads to defective collagen fibrillogenesis and matrix mineralization
J. Bone Miner. Res.
20
81-87
2005
Mus musculus
Ruotsalainen, H.; Sipilae, L.; Vapola, M.; Sormunen, R.; Salo, A.M.; Uitto, L.; Mercer, D.K.; Robins, S.P.; Risteli, M.; Aszodi, A.; Faessler, R.; Myllylae, R.
Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
J. Cell Sci.
119
625-635
2006
Mus musculus
Salo, A.M.; Wang, C.; Sipilae, L.; Sormunen, R.; Vapola, M.; Kervinen, P.; Ruotsalainen, H.; Heikkinen, J.; Myllylae, R.
Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling
J. Cell. Physiol.
207
644-653
2006
Mus musculus
Salo, A.M.; Sipilae, L.; Sormunen, R.; Ruotsalainen, H.; Vainio, S.; Myllylae, R.
The lysyl hydroxylase isoforms are widely expressed during mouse embryogenesis, but obtain tissue- and cell-specific patterns in the adult
Matrix Biol.
25
475-483
2006
Mus musculus
Takaluoma, K.; Hyry, M.; Lantto, J.; Sormunen, R.; Bank, R.A.; Kivirikko, K.I.; Myllyharju, J.; Soininen, R.
Tissue-specific changes in the hydroxylysine content and cross-links of collagens and alterations in fibril morphology in lysyl hydroxylase 1 knock-out mice
J. Biol. Chem.
282
6588-6596
2007
Mus musculus (Q9R0E2)
Nagaoka, H.; Mochida, Y.; Atsawasuwan, P.; Kaku, M.; Kondoh, T.; Yamauchi, M.
1,25(OH)2D3 regulates collagen quality in an osteoblastic cell culture system
Biochem. Biophys. Res. Commun.
377
674-678
2008
Mus musculus
Sricholpech, M.; Perdivara, I.; Nagaoka, H.; Yokoyama, M.; Tomer, K.B.; Yamauchi, M.
Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture
J. Biol. Chem.
286
8846-8856
2011
Mus musculus (Q9R0E1), Mus musculus, Mus musculus CRL-2593 (Q9R0E1)
Ruotsalainen, H.; Risteli, M.; Wang, C.; Wang, Y.; Karppinen, M.; Bergmann, U.; Kvist, A.P.; Pospiech, H.; Herzig, K.H.; Myllylae, R.
The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin
PLoS ONE
7
e50045
2012
Mus musculus, Mus musculus C57BL/6
Chen, Y.; Terajima, M.; Yang, Y.; Sun, L.; Ahn, Y.H.; Pankova, D.; Puperi, D.S.; Watanabe, T.; Kim, M.P.; Blackmon, S.H.; Rodriguez, J.; Liu, H.; Behrens, C.; Wistuba, I.I.; Minelli, R.; Scott, K.L.; Sanchez-Adams, J.; Guilak, F.; Pati, D.; Thilaganathan, N.; Burns, A.R.; Creighton, C.J.; Martinez, E.D.; Zal, T.; Allen, K.; Yamauchi, M.; Kurie, J.M.
Lysyl hydroxylase 2 induces a collagen cross-link switch in tumor stroma
J. Clin. Invest.
125
1147-1162
2015
Homo sapiens (O00469), Homo sapiens, Mus musculus (Q9R0B9), Mus musculus
Zhang, L.; Li, M.M.; Corcoran, M.; Zhang, S.; Cooper, G.J.
Essential roles of insulin, AMPK signaling and lysyl and prolyl hydroxylases in the biosynthesis and multimerization of adiponectin
Mol. Cell. Endocrinol.
399
164-177
2015
Mus musculus (Q9R0B9), Mus musculus (Q9R0E1), Mus musculus (Q9R0E2)
Heard, M.E.; Besio, R.; Weis, M.; Rai, J.; Hudson, D.M.; Dimori, M.; Zimmerman, S.M.; Kamykowski, J.A.; Hogue, W.R.; Swain, F.L.; Burdine, M.S.; Mackintosh, S.G.; Tackett, A.J.; Suva, L.J.; Eyre, D.R.; Morello, R.
Sc65-null mice provide evidence for a novel endoplasmic reticulum complex regulating collagen lysyl hydroxylation
PLoS Genet.
12
e1006002
2016
Mus musculus (Q9R0E2), Mus musculus, Mus musculus 714 (Q9R0E2)
Risteli, M.; Ruotsalainen, H.; Bergmann, U.; Venkatraman Girija, U.; Wallis, R.; Myllylae, R.
Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin
PLoS ONE
9
e113498
2014
Mus musculus (Q9R0E1), Mus musculus, Mus musculus C57BL/6 (Q9R0E1)
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