Information on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.4
-
RECOMMENDED NAME
GeneOntology No.
procollagen-lysine 5-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
hydroxylation
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Lysine degradation
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
zebrafish
TrEMBL
Manually annotated by BRENDA team
gene dPlod, or CG6199, encoding the only lysyl hydroxylase of the organism
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
Mus musculus CRL-2593
gene Plod3
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
in osteoarthritic human synovial fibroblasts, the enzyme expression is induced by TGF-beta via kinase ALK5, not ALK1, and Smad2/3P
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(GDK)4 + 2-oxoglutarate + O2
?
show the reaction diagram
(IKG)3 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
(Ile-5-hydroxylyseine-Gly)3 + succinate + CO2
show the reaction diagram
(Ile-Lys-Gly)3 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
(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
show the reaction diagram
-
-
-
?
2-oxoglutarate + O2 + ascorbate
succinate + CO2 + dehydroascorbate + H2O
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
show the reaction diagram
KGIKGIKG + 2-oxoglutarate + O2
?
show the reaction diagram
L-lysine containing nonapeptides + 2-oxoglutarate + O2
5-hydroxy-L-lysine containing nonapeptides + succinate + CO2
show the reaction diagram
-
diverse nonapeptides, synthetic substrates
-
-
?
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
show the reaction diagram
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
show the reaction diagram
L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
show the reaction diagram
luc7like2(267-278) + 2-oxoglutarate
? + succinate + CO2
show the reaction diagram
substrate is a Luc7like2 protein fragment
-
-
?
peptidyl-L-lysine + 2-oxoglutarate + O2
peptidyl-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
type I procollagen + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
type IV procollagen + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
U2AF65 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
L-lysine-[collagen] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[collagen] + succinate + CO2
show the reaction diagram
L-lysine-[procollagen] + 2-oxoglutarate + O2
(2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
show the reaction diagram
L-lysine-[U2AF65] + 2-oxoglutarate + O2
5-hydroxy-L-lysine-[U2AF65] + succinate + CO2
show the reaction diagram
-
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
-
-
?
procollagen L-lysine + 2-oxoglutarate + O2
procollagen 5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Ni2+
can substitute for Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Adrenochrome
-
slight
catechol
-
-
dehydroascorbate
-
-
DL-Serine 2-[(2,3,4-trihydroxyphenyl)methyl]hydrazide
-
most potent
dopamine
-
-
ephedrine
-
slight
epinephrine
-
-
homogentisic acid
-
-
Hydroxylysine-rich peptides
-
-
iodoacetamide
-
-
malaoxon
-
mechanism of inhibition
malathion
-
mechanism of inhibition
minoxidil
-
0.4 mM inhibits LH1 completely, 1 mM inhibits LH2b and LH3 incompletely
N-ethylmaleimide
-
-
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
nitroblue tetrazolium
-
-
norepinephrine
-
-
p-chloromercuribenzoate
-
-
p-mercuribenzoate
-
-
phenylalanine
-
slight
Phenylephedrine
-
slight
-
Pyridine 2,4-dicarboxylate
-
-
Pyridine 2,5-dicarboxylate
-
-
pyridine 2-carboxylate
-
-
pyrogallol
-
most potent
succinate
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-
tyrosine
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slight
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine
-
can replace ascorbate
2-mercaptoethanol
-
can replace ascorbate
ascorbic acid
bovine serum albumin
catalase
dithiothreitol
L-cysteine
-
can replace ascorbate
lysolecithin
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activation
Triton X-100
-
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 5
(IKG)3
0.31 - 0.8
(Ile-Lys-Gly)3
0.43
(L-Ile-L-Lys-Gly)3
-
lysyl hydroxylase 3
0.2
(Pro-Pro-Gly)4-Ala-Arg-Gly-Met-Lys-Gly-His-Arg-Gly-(Pro-Pro-Gly)4
-
-
0.025 - 0.25
2-oxoglutarate
0.4 - 0.6
Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly
0.2
Ala-Arg-Gly-Met-Lys-Gly-His-Arg-Gly-(Pro-Pro-Gly)4
-
-
0.05 - 0.35
ascorbate
0.04 - 0.05
O2
-
-
0.1 - 0.5
Protocollagen
0.08 - 0.23
type I procollagen
0.04 - 0.3
type IV procollagen
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6 - 4.2
lysine
Gallus gallus
-
in synthetic peptides
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
catechol
-
-
0.047
malaoxon
-
-
0.059
malathion
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
8 - 8.4
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
isozyme LH1, sequence calculation
6.1
isozyme LH3, sequence calculation
6.2
isozyme LH2a, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression only of LH2long
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
stem marrow cell, no expression of isozymes LH3 and LH2b
Manually annotated by BRENDA team
expression only of LH2long
Manually annotated by BRENDA team
expression of LH2long and LH2short
Manually annotated by BRENDA team
in the hatching larvae, LH1 is expressed in the pectoral fin bud; in the hatching larvae, LH3 is expressed in the pectoral fin bud
Manually annotated by BRENDA team
high expression of lysine hydroxylase 3
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
LH3 found on the cell surface bypasses the Golgi complex
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
value about, Western blot
85000
SDS-PAGE
89000
-
LH2, SDS-PAGE
97000
-
SDS-PAGE, V5-tagged LH2b
150000
-
gel filtration
180000
-
gel filtration, isoforms 1-3
200000
220000
-
gel filtration, peak 1
550000
-
gel filtration, peak 2
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
structure of the catalytic domain of recombinant His-tagged JMJD6 and active site structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
side-chain modification
additional information
-
posttranslational hydroxylation in both the cytoplasm and the nucleoplasm is ubiquitous
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme formes aggregates in low ionic strength buffer
-
inactivation by freezing/thawing
labile in tissue extracts
loss of activity during concentration
stabilization by detergents, NaCl
stabilization by glycine
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C
-20°C, enzyme purified by collagen-agarose column-chromatography stable, enzyme from Bio-gel column unstable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA-agarose
ProBond metal chelate affinity resin chromatography and Chelating Sepharose fast flow column chromatography
-
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
-
recombinant His10-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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
-
three recombinant isoenzymes
-
two alternative procedures
-
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
-
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
-
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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expressed in H5 insect cells
-
expression in Escherichia coli, isoform 3 gene product possesses the collagen glycosyltransferase activity, but not isoform 1 and 2
-
expression in insect cells using a baculovirus vector
expression in insect cells using a baculovirus vector; expression in various human tissues
-
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)
-
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
-
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
-
expression of active LH2b and of antisense construct in MC3T3-E1 cells, the latter suppresses the endogenous enzyme
-
expression of GFP-tagged Jmjd6 in HEK-293 cells, GFP pulldown interaction analysis with U2AF65, overview
-
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
-
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
-
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 PLOD2, DNA and amino acid sequence determination and analysis
gene PLOD2, encoding for splice variants LH2a and LH2b, quantitative expression analysis of LH2b
-
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
genes PLOD1 and PLOD2, real-time quantitative reverse transcription PCR
-
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
-
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
-
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
-
in osteoarthritic human synovial fibroblasts, the enzyme expression is induced by TGF-beta via kinase ALK5, not ALK1, and Smad2/3P
-
LH activity of LH3 is not reduced by mutations of this DXD motif
overexpression of the TIA proteins in HEK-293 cells leads to an increase in levels of the LH2(long) spliced product in the minigene
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
-
C144I
-
isoform 3, reduces glycosyltransferase activity
L208I
-
isoform 3, reduces glycosyltransferase activity
A1011G
naturally occuring heterozygous polymorphism in gene PLOD3
A195G
naturally occuring polymorphism in gene PLOD3
A434G
naturally occuring polymorphism in gene PLOD3
C882T
naturally occuring heterozygous polymorphism in gene PLOD3
E542A
-
site-directed mutagenesis
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
N223S
site-directed mutagenesis, the mutant shows 50% reduced lysylhydroxylase activity, while the glycosyltransferase activity is almost abolished
Q543L/Y544F
-
site-directed mutagenesis
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
PLOD expression is associated with human breast cancer progression, PLOD2 expression is specifically prognostic in breast cancer
medicine