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

Reaction

[procollagen]-L-lysine
+
2-oxoglutarate
+
O2
=
[procollagen]-(2S,5R)-5-hydroxy-L-lysine
+
succinate
+
CO2

Synonyms

2-oxoglutarate 5-dioxygenase 2, collagen lysine hydroxylase, Jmjd6, L230, LH, LH1, LH2, LH2 (long), LH2a, LH2b, LH3, 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, 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, procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2, protocollagen lysine hydroxylase, protocollagen lysyl hydroxylase, telopeptide lysyl hydroxylase, TLH

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.4 procollagen-lysine 5-dioxygenase

Engineering

Engineering on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H825S/D827A
-
site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
H80A
-
site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
D97A/D99A
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
L78K
-
site-directed mutagenesis, the mutant cannot be expressed in Escherichia coli
-
D97A/D99A
-
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
-
H825S/D827A
-
site-directed mutagenesis, lysyl hydroxylase inactive mutant, that is still active as collagen glucosyltransferase
-
H80A
-
site-directed mutagenes, the mutant cannot be expressed in Escherichia coli
-
L208I
-
isoform 3, reduces glycosyltransferase activity
C144I
-
isoform 3, reduces glycosyltransferase activity
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
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
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
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
Q543L/Y544F
-
site-directed mutagenesis
N223S
site-directed mutagenesis, the mutant shows 50% reduced lysylhydroxylase activity, while the glycosyltransferase activity is almost abolished
E542A
-
site-directed mutagenesis
C882T
naturally occuring heterozygous polymorphism in gene PLOD3
A434G
naturally occuring polymorphism in gene PLOD3
A1011G
-
naturally occuring heterozygous polymorphism in gene PLOD3
A195G
naturally occuring polymorphism in gene PLOD3
D689A
inactive mutant
E542A/E547A
-
site-directed mutagenesis
E542A/E547A/E574A/E579A
-
site-directed mutagenesis
E542A/E547A/E574A/E579A/E560A
-
site-directed mutagenesis
E542A/H546L/E547A
-
site-directed mutagenesis
E542A/Q543L/Y544F/E547A/E574A
-
site-directed mutagenesis
E547A
-
site-directed mutagenesis
E579A/E560A
-
site-directed mutagenesis
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
K541M
-
site-directed mutagenesis
K541M/E542A
-
site-directed mutagenesis
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
A1011G
naturally occuring heterozygous polymorphism in gene PLOD3
D669A
additional information