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Information on EC 1.14.11.4 - procollagen-lysine 5-dioxygenase and Organism(s) Homo sapiens and UniProt Accession Q6NYC1

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IUBMB Comments
Requires Fe2+ and ascorbate.
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q6NYC1
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-oxoglutarate 5-dioxygenase 2, collagen lysine hydroxylase, Jmjd6, L230, LH, LH1, LH2, LH2 (long), LH2a, LH2b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-oxoglutarate 5-dioxygenase 2
collagen lysine hydroxylase
-
-
-
-
LH2 (long)
247
-
lysine hydroxylase
-
-
-
-
lysine, 2-oxoglutarate 5-dioxygenase
-
-
-
-
lysine-2-oxoglutarate dioxygenase
-
-
-
-
lysyl 5S-hydroxylase
247
-
lysyl hydroxylase
lysyl hydroxylase 2
lysyl hydroxylase 2 (long)
247
-
lysyl hydroxylase 2b
247
-
lysyl hydroxylase 3
lysylhydroxylase 2
276941
-
lysylprotocollagen dioxygenase
-
-
-
-
oxygenase, protocollagen lysine, di-
-
-
-
-
peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase
-
-
-
-
peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase
-
-
-
-
PLOD2
PLOD3
procollagen lysyl hydroxylase 2
276941
-
procollagen-lysine
276941
-
procollagen-lysine, 2-oxoglutarate 5-dioxygenase
276941
-
procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2
276941
-
protocollagen lysine hydroxylase
-
-
-
-
protocollagen lysyl hydroxylase
-
-
-
-
telopeptide lysyl hydroxylase
276941
-
TLH
276941
-
additional information
247
the enzyme is a member of the 2-oxoglutarate-dependent dioxygenase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
hydroxylation
redox reaction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
-
-
-
-
?
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
-
-
?
collagen + 2-oxoglutarate + O2
5-hydroxylysyl-collagen + succinate + CO2
show the reaction diagram
KGIKGIKG + 2-oxoglutarate + O2
?
show the reaction diagram
a synthetic peptide substrate
-
-
?
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
-
-
?
peptide (IKG)3 + 2-oxoglutarate + O2
?
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 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
-
-
-
-
?
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
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
[procollagen]-L-lysine + 2-oxoglutarate + O2
[procollagen]-(2S,5R)-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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
competitive substrate inhibition
L-alpha-hydroxyglutarate
-
the enzyme activity is inhibited by L-alpha-hydroxyglutarate but not its enantiomer D-alpha-hydroxyglutarate
minoxidil
-
0.4 mM inhibits LH1 completely, 1 mM inhibits LH2b and LH3 incompletely
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
required for activity
ascorbic acid
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
0.011 - 0.25
2-oxoglutarate
0.5 - 0.6
Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly
0.3 - 0.35
ascorbate
0.169
peptide (IKG)3
-
pH 7.4, 37C, recombinant wild-type enzyme
0.4 - 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
0.183
2-oxoglutarate
-
pH 7.4, 37C, recombinant wild-type enzyme
0.2
peptide (IKG)3
-
pH 7.4, 37C, recombinant wild-type enzyme
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.6
2-oxoglutarate
-
pH 7.4, 37C, recombinant wild-type enzyme
1.18
peptide (IKG)3
-
pH 7.4, 37C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression only of LH2long
Manually annotated by BRENDA team
-
PLOD2 is mainly expressed within the tunica media of the blood vessels
Manually annotated by BRENDA team
expression of LH2long and LH2short
Manually annotated by BRENDA team
expression only of LH2long
Manually annotated by BRENDA team
expression of LH2long and LH2short
Manually annotated by BRENDA team
expression of LH2long and LH2short
Manually annotated by BRENDA team
-
increased LH2 enzyme activity in lung carcinoma compared to healthy lung
Manually annotated by BRENDA team
expression of LH2long and LH2short
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the 2-oxoglutarate/Fe2+-dependent oxygenase family
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
JMJD6_HUMAN
403
0
46462
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343
80000
-
value about, Western blot
82380
-
2 * 82380, calculation from amino acid sequence, recombinant enzyme: isoform 3
85000
SDS-PAGE
88000
-
2 * 88000 or 97000 SDS-PAGE, recombinant enzymes: isoform 2, possibly two forms are due to variation in the glycosylation of enzymes
150000
-
gel filtration
180000
-
gel filtration, isoforms 1-3
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, recombinant His-tagged catalytic domain of JMJD6, residues 1-343
dimer
-
localization of the region responsible for the dimerization of lysyl hydroxylase 3, to a sequence of amino acids between the glycosyltransferase activity and the lysyl hydroxylase activity domains. This area is covered by amino acids 541-547 and contains no cysteine residues
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
-
hydroxylation of lysyl residue in -X-Lys-Gly
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 20C and 4C by the sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.75-2.0 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
D689A
-
inactive mutant
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by freezing/thawing
-
labile in tissue extracts
-
loss of activity during concentration
-
stabilization by detergents, NaCl
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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 wild-type and mutant enzymes from Sf9 insect cells by chelating affinity chromatography
-
three recombinant isoenzymes
-
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
-
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
-
expressed in H5 insect cells
-
expression in insect cells using a baculovirus vector
-
expression in insect cells using a baculovirus vector; expression in various human tissues
-
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 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 PLOD2
-
gene PLOD2, binding of the TGFbeta1 pathway related transcription factors SMAD3 and SP1-mediated TGFbeta1 enhanced PLOD2 expression and might be correlated to an increase of acetylated histone H3 and H4 at the PLOD2 promoter. Depletion of SMAD3 reduces gene PLOD2 acetylated H3 and H4, histone methylation marks at the PLOD2 promoter depicted an increase of the active histone mark H3K79me2, a decrease of the repressive H4K20me3 mark, but no role for the generally strong transcription-related modifications: H3K4me3, H3K9me3 and H3K27me3. TGFbeta1 induces a SP1- and SMAD3-dependent recruitment of histone modifying enzymes to the PLOD2 promoter other than the currently known TGFbeta1 downstream co-activators and epigenetic modifications. Quantitative real-time PCR enzyme 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 PLOD2, large-scale transfection with N-terminal His8 and human growth hormone (hGH) tags transfection with polyethylenimine and recombinant expression of wild-type enzyme, N-terminally truncated enzyme mutant, and of inactive mutant D689A in engineered CHO cells and secretion to the cell culture medium
-
gene PLOD3
-
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
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
procollagen lysyl hydroxylase 2 expression is regulated by an alternative downstream transforming growth factor beta-1 activation mechanism. TGF-beta1 induces the enzyme, mechanism of TGFbeta1-enhanced PLOD2 expression, detailed overview
-
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kivirikko, K.I.; Myllyl, R.
Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes
Methods Enzymol.
82
245-304
1982
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Puistola, U.
Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types
Biochem. J.
201
215-219
1982
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Kellokumpu, S.; Sormunen, R.; Heikkinen, J.; Myllyla, R.
Lysyl hydroxylase, a collagen processing enzyme, exemplifies a novel class of luminally-oriented peripheral membrane proteins in the endoplasmic reticulum
J. Biol. Chem.
269
30524-30529
1994
Homo sapiens
Manually annotated by BRENDA team
Valtavaara, M.; Papponen, H.; Pirttilae, A.M.; Hiltunen, K.; Helander, H.; Myllylae, R.
Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle
J. Biol. Chem.
272
6831-6834
1997
Homo sapiens, Homo sapiens (O00469)
Manually annotated by BRENDA team
Passoja, K.; Rautavuoma, K.; Ala-Kokko, L.; Kosonen, T.; Kivirikko, K.I.
Cloning and characterization of a third human lysyl hydroxylase isoform
Proc. Natl. Acad. Sci. USA
95
10482-10486
1998
Homo sapiens, Homo sapiens (O60568)
Manually annotated by BRENDA team
Rautavuoma, K.; Takaluoma, K.; Passoja, K.; Pirskanen, A.; Kvist, A.P.; Kivirikko, K.I.; Myllyharju, J.
Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3: The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity
J. Biol. Chem.
277
23084-23091
2002
Homo sapiens
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
Suokas, M.; Lampela, O.; Juffer, A.H.; Myllyla, R.; Kellokumpu, S.
Retrieval-independent localization of lysyl hydroxylase in the endoplasmic reticulum via a peptide fold in its iron-binding domain
Biochem. J.
370
913-920
2003
Homo sapiens
Manually annotated by BRENDA team
van der Slot, A.J.; Zuurmond, A.M.; Bardoel, A.F.; Wijmenga, C.; Pruijs, H.E.; Sillence, D.O.; Brinckmann, J.; Abraham, D.J.; Black, C.M.; Verzijl, N.; DeGroot, J.; Hanemaaijer, R.; TeKoppele, J.M.; Huizinga, T.W.; Bank, R.A.
Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis
J. Biol. Chem.
278
40967-40972
2003
Homo sapiens, Homo sapiens (O00469)
Manually annotated by BRENDA team
Risteli, M.; Niemitalo, O.; Lankinen, H.; Juffer, A.H.; Myllyla, R.
Characterization of collagenous peptides bound to lysyl hydroxylase isoforms
J. Biol. Chem.
279
37535-37543
2004
Caenorhabditis elegans, Homo sapiens
Manually annotated by BRENDA team
Walker, L.C.; Overstreet, M.A.; Siddiqui, A.; De Paepe, A.; Ceylaner, G.; Malfait, F.; Symoens, S.; Atsawasuwan, P.; Yamauchi, M.; Ceylaner, S.; Bank, R.A.; Yeowell, H.N.
A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient
J. Invest. Dermatol.
124
914-918
2005
Homo sapiens
Manually annotated by BRENDA team
Walker, L.C.; Overstreet, M.A.; Yeowell, H.N.
Tissue-specific expression and regulation of the alternatively-spliced forms of lysyl hydroxylase 2 (LH2) in human kidney cells and skin fibroblasts
Matrix Biol.
23
515-523
2005
Homo sapiens, Homo sapiens (O00469)
Manually annotated by BRENDA team
Wu, J.; Reinhardt, D.P.; Batmunkh, C.; Lindenmaier, W.; Far, R.K.; Notbohm, H.; Hunzelmann, N.; Brinckmann, J.
Functional diversity of lysyl hydroxylase 2 in collagen synthesis of human dermal fibroblasts
Exp. Cell Res.
312
3485-3494
2006
Homo sapiens
Manually annotated by BRENDA team
Zuurmond, A.M.; van der Slot-Verhoeven, A.J.; van Dura, E.A.; De Groot, J.; Bank, R.A.
Minoxidil exerts different inhibitory effects on gene expression of lysyl hydroxylase 1, 2, and 3: implications for collagen cross-linking and treatment of fibrosis
Matrix Biol.
24
261-270
2005
Homo sapiens
Manually annotated by BRENDA team
Takaluoma, K.; Lantto, J.; Myllyharju, J.
Lysyl hydroxylase 2 is a specific telopeptide hydroxylase, while all three isoenzymes hydroxylate collagenous sequences
Matrix Biol.
26
396-403
2007
Homo sapiens
Manually annotated by BRENDA team
Salo, A.M.; Cox, H.; Farndon, P.; Moss, C.; Grindulis, H.; Risteli, M.; Robins, S.P.; Myllylae, R.
A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene
Am. J. Hum. Genet.
83
495-503
2008
Homo sapiens, Homo sapiens (O60568)
Manually annotated by BRENDA team
Stein, H.; Wilensky, M.; Tsafrir, Y.; Rosenthal, M.; Amir, R.; Avraham, T.; Ofir, K.; Dgany, O.; Yayon, A.; Shoseyov, O.
Production of bioactive, post-translationally modified, heterotrimeric, human recombinant type-I collagen in transgenic tobacco
Biomacromolecules
10
2640-2645
2009
Homo sapiens
Manually annotated by BRENDA team
Risteli, M.; Ruotsalainen, H.; Salo, A.M.; Sormunen, R.; Sipilae, L.; Baker, N.L.; Lamande, S.R.; Vimpari-Kauppinen, L.; Myllylae, R.
Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix
J. Biol. Chem.
284
28204-28211
2009
Homo sapiens, Homo sapiens (O60568)
Manually annotated by BRENDA team
Hyry, M.; Lantto, J.; Myllyharju, J.
Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2
J. Biol. Chem.
284
30917-30924
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, C.; Kovanen, V.; Raudasoja, P.; Eskelinen, S.; Pospiech, H.; Myllylae, R.
The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability
J. Cell. Mol. Med.
13
508-521
2009
Homo sapiens (O60568)
Manually annotated by BRENDA team
Yeowell, H.N.; Walker, L.C.; Mauger, D.M.; Seth, P.; Garcia-Blanco, M.A.
TIA nuclear proteins regulate the alternate splicing of lysyl hydroxylase 2
J. Invest. Dermatol.
129
1402-1411
2009
Homo sapiens
Manually annotated by BRENDA team
Webby, C.J.; Wolf, A.; Gromak, N.; Dreger, M.; Kramer, H.; Kessler, B.; Nielsen, M.L.; Schmitz, C.; Butler, D.S.; Yates, J.R.; Delahunty, C.M.; Hahn, P.; Lengeling, A.; Mann, M.; Proudfoot, N.J.; Schofield, C.J.; Boettger, A.
Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
Science
325
90-93
2009
Homo sapiens
Manually annotated by BRENDA team
Mantri, M.; Krojer, T.; Bagg, E.A.; Webby, C.J.; Butler, D.S.; Kochan, G.; Kavanagh, K.L.; Oppermann, U.; McDonough, M.A.; Schofield, C.J.
Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6
J. Mol. Biol.
401
211-222
2010
Homo sapiens (Q6NYC1)
Manually annotated by BRENDA team
Wang, C.; Ristiluoma, M.M.; Salo, A.M.; Eskelinen, S.; Myllylae, R.
Lysyl hydroxylase 3 is secreted from cells by two pathways
J. Cell. Physiol.
227
668-675
2012
Canis lupus familiaris, Canis lupus familiaris Madin-Darby, Homo sapiens (O60568)
Manually annotated by BRENDA team
Remst, D.F.; Blaney Davidson, E.N.; Vitters, E.L.; Bank, R.A.; van den Berg, W.B.; van der Kraan, P.M.
TGF-beta induces lysyl hydroxylase 2b in human synovial osteoarthritic fibroblasts through ALK5 signaling
Cell Tissue Res.
355
163-171
2013
Homo sapiens
Manually annotated by BRENDA team
Heikkinen, J.; Risteli, M.; Lampela, O.; Alavesa, P.; Karppinen, M.; Juffer, A.; Myllylae, R.
Dimerization of human lysyl hydroxylase 3 (LH3) is mediated by the amino acids 541-547
Matrix Biol.
30
27-33
2011
Homo sapiens
Manually annotated by BRENDA team
Mantri, M.; Webby, C.; Loik, N.; Hamed, R.; Nielsen, M.; McDonough, M.; McCullagh, J.; Boettger, A.; Schofield, C.; Wolf, A.
Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6
MedChemComm
3
80-85
2012
Homo sapiens
-
Manually annotated by BRENDA team
Gilkes, D.M.; Bajpai, S.; Wong, C.C.; Chaturvedi, P.; Hubbi, M.E.; Wirtz, D.; Semenza, G.L.
Procollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis
Mol. Cancer Res.
11
456-466
2013
Homo sapiens
Manually annotated by BRENDA team
Guo, H.F.; Cho, E.J.; Devkota, A.K.; Chen, Y.; Russell, W.; Phillips, G.N.; Yamauchi, M.; Dalby, K.N.; Kurie, J.M.
A scalable lysyl hydroxylase 2 expression system and luciferase-based enzymatic activity assay
Arch. Biochem. Biophys.
618
45-51
2017
Homo sapiens, Homo sapiens (O00469)
Manually annotated by BRENDA team
Dayer, C.; Stamenkovic, I.
Recruitment of matrix metalloproteinase-9 (MMP-9) to the fibroblast cell surface by lysyl hydroxylase 3 (LH3) triggers transforming growth factor-beta (TGF-beta) activation and fibroblast differentiation
J. Biol. Chem.
290
13763-13778
2015
Homo sapiens (O60568)
Manually annotated by BRENDA team
Gjaltema, R.A.; de Rond, S.; Rots, M.G.; Bank, R.A.
Procollagen lysyl hydroxylase 2 expression is regulated by an alternative downstream transforming growth factor beta-1 activation mechanism
J. Biol. Chem.
290
28465-28476
2015
Homo sapiens (O00469)
Manually annotated by BRENDA team
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, Homo sapiens (O00469), Mus musculus, Mus musculus (Q9R0B9)
Manually annotated by BRENDA team
Neyazi, B.; Tanrikulu, L.; Wilkens, L.; Hartmann, C.; Stein, K.P.; Dumitru, C.A.; Sandalcioglu, I.E.
Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 expression in brain arteriovenous malformations and its association with brain arteriovenous malformation size
World Neurosurg.
102
79-84
2017
Homo sapiens, Homo sapiens (O00469)
Manually annotated by BRENDA team
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