1.14.11.4: procollagen-lysine 5-dioxygenase
This is an abbreviated version!
For detailed information about procollagen-lysine 5-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.4
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1.14.11.4
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prolyl
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ehlers-danlos
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hydroxylysine
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jumonji
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fibrosis
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procollagens
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fragility
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domain-containing
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hydroxylases
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osteogenesis
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4-hydroxylase
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kyphoscoliosis
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imperfecta
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demethylase
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glucosyltransferase
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pyridinoline
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hypermobl
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galactosyltransferase
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contractures
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minoxidil
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hypotonia
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hydroxylysyl
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hypermobility
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bruck
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fkbp10
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hyperelasticity
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underhydroxylated
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sclera
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scoliosis
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laxity
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chick-embryo
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hyperextensibility
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2-oxoglutarate-dependent
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serpinh1
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galactosylhydroxylysyl
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ppib
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medicine
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crtap
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diagnostics
- 1.14.11.4
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prolyl
- ehlers-danlos
- hydroxylysine
-
jumonji
- fibrosis
- procollagens
-
fragility
-
domain-containing
- hydroxylases
-
osteogenesis
-
4-hydroxylase
-
kyphoscoliosis
- imperfecta
- demethylase
-
glucosyltransferase
-
pyridinoline
-
hypermobl
-
galactosyltransferase
- contractures
- minoxidil
- hypotonia
-
hydroxylysyl
-
hypermobility
-
bruck
- fkbp10
-
hyperelasticity
-
underhydroxylated
-
sclera
- scoliosis
-
laxity
-
chick-embryo
-
hyperextensibility
-
2-oxoglutarate-dependent
-
serpinh1
-
galactosylhydroxylysyl
- ppib
- medicine
-
crtap
- diagnostics
Reaction
Synonyms
2-oxoglutarate 5-dioxygenase 2, collagen lysine hydroxylase, Jmjd6, L230, LH, LH1, LH2, LH2 (long), LH2a, LH2b, LH3, LH3/PLOD3, lysine hydroxylase, lysine, 2-oxoglutarate 5-dioxygenase, lysine-2-oxoglutarate dioxygenase, lysyl 5S-hydroxylase, lysyl hydroxylase, lysyl hydroxylase 1, lysyl hydroxylase 2, lysyl hydroxylase 2 (long), lysyl hydroxylase 2a, lysyl hydroxylase 2b, lysyl hydroxylase 3, Lysyl hydroxylase-2b, lysyl-hydroxylase 1, lysylhydroxylase 2, lysylprotocollagen dioxygenase, More, multifunctional collagen lysyl hydroxylase, oxygenase, protocollagen lysine, di-, peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase, peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase, PLOD, Plod1, PLOD2, Plod2a, Plod2b, PLOD2iso1, PLOD2iso2, PLOD3, procollagen lysyl hydroxylase 2, procollagen-lysine, procollagen-lysine 2-oxoglutarate 5-dioxygenase, procollagen-lysine 2-oxoglutarate 5-dioxygenase 2, procollagen-lysine, 2-oxoglutarate 5-dioxygenase, procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2, procollagen-lysine,2-oxoglutarate 5-dioxygenase, protocollagen lysine hydroxylase, protocollagen lysyl hydroxylase, telopeptide lysyl hydroxylase, TLH
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1.14.11.4 procollagen-lysine 5-dioxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D250A
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site-directed mutagenesis, the mutant shows unaltered lysyl hydroxylase activity, although reduced collagen glucosyltransferase activity, compared to the wild-type enzyme
D97A/D99A
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site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
H80A
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site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
H825S/D827A
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site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
L78K
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site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
D250A
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site-directed mutagenesis, the mutant shows unaltered lysyl hydroxylase activity, although reduced collagen glucosyltransferase activity, compared to the wild-type enzyme
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D97A/D99A
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site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
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H80A
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site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
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H825S/D827A
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site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
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L78K
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site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
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G597V
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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
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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
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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
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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
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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
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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
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
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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
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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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
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
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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
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
additional information
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mutations in the LH3 gene cause connective tissue disorder. Genotype-phenotype analysis of PLOD3 mutations, phenotypes, detailed overview
additional information
mutations in the LH3 gene cause connective tissue disorder. Genotype-phenotype analysis of PLOD3 mutations, phenotypes, detailed overview
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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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
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
additional information
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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
additional information
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
additional information
LH-deficient mutant, deficiency of LH3 glycosyltransferase activity decreases cell growth and increases lethality
additional information
overexpression of LH3, increased hydroxylation of lysyl residues and increased galactosylation and glucosylation of hydroxylysyl residues
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
generation of an N-terminally truncated enzyme mutant comprising residues 33-758
additional information
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generation of an N-terminally truncated enzyme mutant comprising residues 33-758
additional information
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
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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
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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
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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
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
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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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