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Information on EC 1.4.3.13 - protein-lysine 6-oxidase and Organism(s) Homo sapiens and UniProt Accession Q9Y4K0

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EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.13 protein-lysine 6-oxidase
IUBMB Comments
Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices . These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate .
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Homo sapiens
UNIPROT: Q9Y4K0
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Synonyms
lysyl oxidase, loxl2, loxl1, loxl4, loxl3, lox-pp, lysyl oxidases, lysyl oxidase-like 1, lysyl oxidase-like 2, lysyl oxidase-like, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lysyl oxidase-like 2
-
LOR2
-
-
LOX-like 2
-
-
LOXL-2
-
-
LOXL3-sv1
-
LOXL3 encodes two variants, LOXL3 and LOXL3-sv1, both of which function as amine oxidases with distinct tissue and substrate specificities from one another
lysyl oxidase
lysyl oxidase 1
-
lysyl oxidase homolog 2
-
-
lysyl oxidase like 4
-
-
lysyl oxidase-like 2
-
-
lysyl oxidase-like 4
-
-
lysyl oxidase-like protein
-
-
oxidase-like protein 1
-
-
protein-6-oxidase
-
-
protein-L-lysine:oxygen 6-oxidoreductase
-
-
protein-lysine 6-oxidase
-
-
RAS excision protein
-
-
-
-
WS9-14
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-L-lysine:oxygen 6-oxidoreductase (deaminating)
Also acts on protein 5-hydroxylysine. This enzyme catalyses the final known enzymic step required for collagen and elastin cross-linking in the biosynthesis of normal mature extracellular matrices [4]. These reactions play an important role for the development, elasticity and extensibility of connective tissue. The enzyme is also active on free amines, such as cadaverine or benzylamine [4,5]. Some isoforms can also use [protein]-N(6)-acetyl-L-lysine as substrate deacetamidating the substrate [6].
CAS REGISTRY NUMBER
COMMENTARY hide
99676-44-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
-
-
-
?
tropoelastin + H2O + O2
?
show the reaction diagram
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
1,5-diaminopentane + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
1,5-diaminopentane + O2 + H2O
? + NH3 + H2O2
show the reaction diagram
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
show the reaction diagram
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
collagen + O2 + H2O
?
show the reaction diagram
-
collagen type I, II, III, IV, VI, VIII and X
-
-
?
collagen III + O2 + H2O
allysyl-collagen III + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
dichlorodihydrofluorescein diacetate + O2 + H2O
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
show the reaction diagram
elastin + O2 + H2O
?
show the reaction diagram
-
-
-
-
?
histone H1 + O2 + H2O
?
show the reaction diagram
histone H2 + O2 + H2O
?
show the reaction diagram
-
recombinant mature LOX and C-terminally deleted enzyme
-
-
?
n-alkylamine + O2 + H2O
aldehyde + NH3 + H2O2
show the reaction diagram
-
synthetic substrates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
show the reaction diagram
-
-
-
?
tropoelastin + ?
?
show the reaction diagram
-
LOXL1 catalyzes the polymerization of tropoelastin
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
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
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
show the reaction diagram
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
collagen III + O2 + H2O
allysyl-collagen III + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
show the reaction diagram
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
show the reaction diagram
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lysyl-tyrosyl quinone
Lys-653 and Tyr-689 are the precursor residues for the lysyl-tyrosyl quinone cofactor of the enzyme
lysyl-tyrosyl quinone
lysyl-tyrosyl-quinone
lysyltyrosyl quinone
quinone
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain conserved lysyl and tyrosyl residues that may contribute to quinone cofactor formation
additional information
-
enzyme contains a cross-linked quinone, cross-linking via lysyl- and tyrosyl residues
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
copper loading activates hLOXL2 and supports lysyl tyrosylquinone formation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2-chloropyridin-4-yl)methanamine
-
-
1-(2-chloropyridin-4-yl)methanamine
-
-
1-(2-fluoropyridin-4-yl)methanamine
-
-
1-(2-methoxypyridin-4-yl)methanamine
-
-
1-(2-phenoxypyridin-4-yl)methanamine
-
-
1-(3-fluoropyridin-4-yl)methanamine
-
-
1-(4-fluorophenyl)methanamine
-
-
1-(4-methoxyphenyl)methanamine
-
-
1-(4-nitrophenyl)methanamine
-
-
1-(pyridin-4-yl)methanamine
-
-
1-(quinolin-4-yl)methanamine
-
-
1-([2,3'-bipyridin]-4-yl)methanamine
-
-
1-phenylmethanamine
-
-
1-[2-(1H-imidazol-1-yl)pyridin-4-yl]methanamine
-
-
1-[2-(trifluoromethyl)pyridin-4-yl]methanamine
-
-
1-[3-(hydrazinylmethyl)phenyl]methanamine
-
-
1-[4-(1,3-thiazol-2-yl)phenyl]methanamine
-
-
1-[4-(hydrazinylmethyl)phenyl]methanamine
-
-
1-[5-(trifluoromethyl)[2,3'-bipyridin]-4-yl]methanamine
-
-
2-(pyridin-4-yl)ethan-1-amine
-
-
2-Aminopropionitrile
i.e. BAPN, is an irreversible inhibitor of LOX, involved in regulating the metastatic colonization potential of the human breast cancer cell line MDAMB-231
2-phenylcyclopropan-1-amine
-
-
2-phenylethan-1-amine
-
-
3-aminopropanenitrile
4-(aminomethyl)aniline
-
-
4-(aminomethyl)benzonitrile
-
-
beta-aminopropionitrile
homocysteine
0.03 mM, up to 50% inhibition
methyl 3-(aminomethyl)benzoate
-
-
methyl 4-(aminomethyl)benzoate
-
-
phenylhydrazine
-
-
TNFalpha
-
TNFalpha decreases LOX mRNA levels in endothelial cells in a dose- and time-dependent manner (2fold at 1 ng/ml and maximum at 2.5 ng/ml) and decreases endothelial LOX enzymatic activity
-
additional information
-
LOXL4 suppresses the expression of laminins and alpha3 integrin and the activity of matrix metalloproteinase-2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-aza-deoxycytidine
-
activates LOXL2 gene expression
areca nut extract
-
up-regulates LOX expression
-
hypoxia inducible factor-1
-
hypoxia-induced LOX expression is partially mediated by hypoxia inducible factor-1
suramin
-
0.15 mM, upregulates LOX expression
transforming growth factor-beta1
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.373
1,5-Diaminopentane
pH 8.2, temperature not specified in the publication
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7290
1,5-Diaminopentane
pH 8.2, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000126
(2-chloropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000126
1-(2-chloropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000385
1-(2-fluoropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00118
1-(2-methoxypyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000309
1-(2-phenoxypyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000431
1-(3-fluoropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.026
1-(4-fluorophenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.035
1-(4-methoxyphenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000719
1-(4-nitrophenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00122
1-(pyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00604
1-(quinolin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000321
1-([2,3'-bipyridin]-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.0647
1-phenylmethanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000203
1-[2-(1H-imidazol-1-yl)pyridin-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000999
1-[2-(trifluoromethyl)pyridin-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00497
1-[3-(hydrazinylmethyl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000902
1-[4-(1,3-thiazol-2-yl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00111
1-[4-(hydrazinylmethyl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.031
1-[5-(trifluoromethyl)[2,3'-bipyridin]-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00821
2-(pyridin-4-yl)ethan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.1
2-phenylcyclopropan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.0601
2-phenylethan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000066
3-aminopropanenitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.047
4-(aminomethyl)aniline
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00067
4-(aminomethyl)benzonitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000066
beta-aminopropionitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00354
methyl 3-(aminomethyl)benzoate
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00362
methyl 4-(aminomethyl)benzoate
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.054
-
recombinant His-tagged LOXL1, substrate benzylamine
0.097
-
recombinant His-tagged LOX, substrate benzylamine
0.15
-
recombinant His-tagged LOXL2, substrate benzylamine
0.2
-
about, retina
0.31
-
purified recombinant enzyme, pH not specified in the publication, 37°C
0.4
-
about, lens
1.1
-
about, iris/ciliary body
1.2
-
about, vitreous ocular tissue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
pH 7.5: about 55% of maximal activity, pH 8.5: about 85% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mature form of LOXL1 and polymerized LOXL1protein forms
Manually annotated by BRENDA team
-
polymerized LOXL1protein forms
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
mature form of LOXL1 and polymerized LOXL1protein forms
Manually annotated by BRENDA team
-
determination of LOX activity and expression in donor ocular tissues
Manually annotated by BRENDA team
-
in MCF-10A normal breast epithelial cells stably expressing lysyl oxidase LOX has no effect on cell proliferation. Coexpression of lysyl oxidase and placental lactogen leads to a 121% increase in cell proliferation
Manually annotated by BRENDA team
-
polymerized LOXL1protein forms
Manually annotated by BRENDA team
-
LOX mRNA is upregulated in OSCC cells
Manually annotated by BRENDA team
-
LOXL2, LOX, LOXL
Manually annotated by BRENDA team
-
determination of LOX activity and expression in donor ocular tissues
Manually annotated by BRENDA team
-
LOXL2, LOX, LOXL
Manually annotated by BRENDA team
-
determination of LOX activity and expression in donor ocular tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
passage of unprocessed proenzyme
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
co-overexpression of specific protein 1 (SP1) and LOXL2 significantly correlates with poor prognosis in patients with pancreatic cancer
physiological function
drug target
the enzyme is a promising therapeutic target for the progression of cancer and fibrosis
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOXL2_HUMAN
774
0
86725
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
-
polymerized LOXL1 precursor protein, SDS-PAGE
18000
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
28000
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
29000
30000
-
mature enzyme, SDS-PAGE
32000
34000
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
36000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
42000
-
mature enzyme, SDS-PAGE
46000
49500
x * 49500, calculated from amino acid sequence
50000
51000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
80000
-
polymerized enzyme, SDS-PAGE
83600
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
85000
-
predicted molecular mass
93000
-
SDS-PAGE
97000
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-glycans at Asn-455 and Asn-644 are essential for proper folding and secretion of the enzyme. The N-glycan at Asn-644 enhances the solubility and stability of the enzyme catalytic domain
glycoprotein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at 18°C, crystal structure of the enzyme at 2.4 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N455Q
the mutant protein is not secreted into the medium since the mutation prevents N-glycosylation, so the proteins fail to fold properly and undergo rapid degradation
N644Q
the mutant protein is not secreted into the medium since the mutation prevents N-glycosylation, so the proteins fail to fold properly and undergo rapid degradation
G153D
G758T
-
the mutation is associated with the occurence of exfoliation syndrome
G794A
-
the mutation is associated with the occurence of exfoliation syndrome
R141L
R158Q
-
naturally occuring mutation, G to A polymorphism at nucleotide 473, causes oral submucous fibrosis and is associated to chewing of areca nuts, genotyping, overview
additional information
-
LOXL1 gene variants play no significant role in the pathogenesis of primary open-angle glaucoma
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
the enzyme maintains its secondary structure till 90°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
denatured by urea during purification and refolded by stepwise dialysis in the presence of N-lauroylsarcosinate and Cu2+
-
enzyme is resistant to high urea concentrations
-
sucrose, sorbitol, and mannitol are less effective in stabilization and preservation of the enzyme compared to trehalose
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilized purified recombinant LOX, loss of 73% activity without stabilizing agent, loss of 4% activity in presence of 10 mM trehalose
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
lysyl oxidase is a highly insoluble enzyme requiring high concentrations of urea to solubilize. Development and optimization of a method to obtain lysyl oxidase in high yields directly from an Escherichia coli culture without the need for refolding of inclusion bodies using nutrient rich media, overview
-
Ni-NTA column chromatography
-
recombinant His-tagged mature enzyme and C-terminally deleted enzyme by nickel affinity chromatography
-
recombinant, N-terminally His6-tagged proteolytically processed forms of LOX, LOXL1, and LOXL2 from Escherichia coli inclusion bodies by nickel chelating affinity chromatography, to over 95% purity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Drosophila melanogaster Schneider-2 cells
cloning from cDNA library, DNA and amino acid sequence determination and analysis, expression of C-terminally His6-tagged LOX in Escherichia coli
-
expressed in CHO-K1 cells
expressed in Escherichia coli
-
expressed in immature dendritic cells derived from peripheral blod mononuclear cells
-
expression in Escherichia coli
expression of mature enzyme and C-terminally deleted enzyme as N-terminally His6-tagged enzymes
-
expression of proteolytically processed forms of LOX, LOXL1, and LOXL2 in Escherichia coli as N-terminally His6-tagged proteins
-
LOX genotyping of Asian non-areca nut chewers and arec nut chewers of different ages, overview
-
LOXL3 cDNA is expressed in human HT-1080 fibrosarcoma cells
RT-PCR enzyme expression analysis in esophageal squamous cell carcinoma cells, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in MIA Paca-2 cells, silencing of apecific protein 1 (SP1) induces a reduction of LOXL2 expression
the enzyme is highly up-regulated in metastatic breast cancer cells and tissues
ability of torasemide to correct both lysyl oxidase overexpression and enhanced collagen cross-linking
-
LOX and LOXL2 are induced 13 and 7.5fold, respectively, by hypoxia-inducible transcription factor-1alpha and hypoxia-inducible transcription factor-2beta
-
LOX is induced by hypoxia, loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of LOX mRNA, and loss of Pdcd4 also augments hypoxia induction of LOX
the enzyme is upregulated in polycystic ovarian tissue by LOX promoter binding of transcription factors, e.g. NF-kappaB and activator protein-1, induced in advanced glycation end product, AEG, signaling, overview
-
tumor suppressor Pdcd4 inhibits LOX expression, loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of LOX mRNA
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
convertion of recombinant, N-terminally His6-tagged proteolytically processed forms of LOX, LOXL1, and LOXL2 from Escherichia coli inclusion bodies to active enzymes by denaturation with 8 M urea prior to stepwise dialysis in presence of 2% N-laurylsarcosinate and 0.2 mM CuCl2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
co-overexpression of SP1 and LOXL2 significantly correlates with poor prognosis in patients with pancreatic cancer
diagnostics
-
LOX can serve as a predictive marker of lymph node metastasis and prognosis in esophageal squamous cell carcinoma. Overall survival rates of the patients with esophageal squamous cell carcinoma with high LOX expression are significantly lower than those of the patients with esophageal squamous cell carcinoma with low LOX expression
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mki, J.M.; Kivirikko, K.I.
Cloning and characterization of a fourth human lysyl oxidase isoenzyme
Biochem. J.
355
381-387
2001
Homo sapiens (P58215), Homo sapiens
Manually annotated by BRENDA team
Smith-Mungo, L.I.; Kagan, H.M.
Lysyl oxidase: properties, regulation and multiple functions in biology
Matrix Biol.
16
387-398
1998
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Ovis aries, Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Molnar, J.; Fong, K.S.K.; He, Q.P.; Hayashi, K.; Kim, Y.; Fong, S.F.T.; Fogelgren, B.; Molnarne Szauter, K.; Mink, M.; Csiszar, K.
Structural and functional diversity of lysyl oxidase and the LOX-like proteins
Biochim. Biophys. Acta
1647
220-224
2003
Homo sapiens, Mus musculus, Drosophila melanogaster (Q9N9Y8), Drosophila melanogaster (Q9V9X5)
Manually annotated by BRENDA team
Giampuzzi, M.; Oleggini, R.; Di Donato, A.
Demonstration of in vitro interaction between tumor suppressor lysyl oxidase and histones H1 and H2: definition of the regions involved
Biochim. Biophys. Acta
1647
245-251
2003
Homo sapiens
Manually annotated by BRENDA team
Kagan, H.M.; Li, W.
Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell
J. Cell. Biochem.
88
660-672
2003
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Jung, S.T.; Kim, M.S.; Seo, J.Y.; Kim, H.C.; Kim, Y.
Purification of enzymatically active human lysyl oxidase and lysyl oxidase-like protein from Escherichia coli inclusion bodies
Protein Expr. Purif.
31
240-246
2003
Homo sapiens
Manually annotated by BRENDA team
Bouez, C.; Reynaud, C.; Noblesse, E.; Thepot, A.; Gleyzal, C.; Kanitakis, J.; Perrier, E.; Damour, O.; Sommer, P.
The lysyl oxidase LOX is absent in basal and squamous cell carcinomas and its knockdown induces an invading phenotype in a skin equivalent model
Clin. Cancer Res.
12
1463-1469
2006
Homo sapiens
Manually annotated by BRENDA team
Cenizo, V.; Andre, V.; Reymermier, C.; Sommer, P.; Damour, O.; Perrier, E.
LOXL as a target to increase the elastin content in adult skin: a dill extract induces the LOXL gene expression
Exp. Dermatol.
15
574-581
2006
Homo sapiens
Manually annotated by BRENDA team
Lee, J.E.; Kim, Y.
A tissue-specific variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase with substrate specificity
J. Biol. Chem.
281
37282-37290
2006
Homo sapiens
Manually annotated by BRENDA team
Polgar, N.; Fogelgren, B.; Shipley, J.M.; Csiszar, K.
Lysyl oxidase interacts with hormone placental lactogen and synergistically promotes breast epithelial cell proliferation and migration
J. Biol. Chem.
282
3262-3272
2006
Homo sapiens
Manually annotated by BRENDA team
Hayashi, H.; Gotoh, N.; Ueda, Y.; Nakanishi, H.; Yoshimura, N.
Lysyl oxidase-like 1 polymorphisms and exfoliation syndrome in the Japanese population
Am. J. Ophthalmol.
145
582-585
2008
Homo sapiens
Manually annotated by BRENDA team
Rodriguez, C.; Alcudia, J.F.; Martinez-Gonzalez, J.; Raposo, B.; Navarro, M.A.; Badimon, L.
Lysyl oxidase (LOX) down-regulation by TNFalpha: a new mechanism underlying TNFalpha-induced endothelial dysfunction
Atherosclerosis
196
558-564
2008
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kim, D.J.; Lee, D.C.; Yang, S.J.; Lee, J.J.; Bae, E.M.; Kim, D.M.; Min, S.H.; Kim, S.J.; Kang, D.C.; Sang, B.C.; Myung, P.K.; Park, K.C.; Yeom, Y.I.
Lysyl oxidase like 4, a novel target gene of TGF-beta1 signaling, can negatively regulate TGF-beta1-induced cell motility in PLC/PRF/5 hepatoma cells
Biochem. Biophys. Res. Commun.
373
521-527
2008
Homo sapiens
Manually annotated by BRENDA team
Buchinger, B.; Spitzer, S.; Karlic, H.; Klaushofer, K.; Varga, F.
Lysyl oxidase (LOX) mRNA expression and genes of the differentiated osteoblastic phenotype are upregulated in human osteosarcoma cells by suramin
Cancer Lett.
265
45-54
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wu, G.; Guo, Z.; Chang, X.; Kim, M.S.; Nagpal, J.K.; Liu, J.; Maki, J.M.; Kivirikko, K.I.; Ethier, S.P.; Trink, B.; Sidransky, D.
LOXL1 and LOXL4 are epigenetically silenced and can inhibit ras/extracellular signal-regulated kinase signaling pathway in human bladder cancer
Cancer Res.
67
4123-4129
2007
Homo sapiens
Manually annotated by BRENDA team
Peinado, H.; Moreno-Bueno, G.; Hardisson, D.; Perez-Gomez, E.; Santos, V.; Mendiola, M.; de Diego, J.I.; Nistal, M.; Quintanilla, M.; Portillo, F.; Cano, A.
Lysyl oxidase-like 2 as a new poor prognosis marker of squamous cell carcinomas
Cancer Res.
68
4541-4550
2008
Homo sapiens
Manually annotated by BRENDA team
Kuhlenbaeumer, G.; Friedrichs, F.; Kis, B.; Berlit, P.; Maintz, D.; Nassenstein, I.; Nabavi, D.; Dittrich, R.; Stoll, M.; Ringelstein, B.
Association between single nucleotide polymorphisms in the lysyl oxidase-like 1 gene and spontaneous cervical artery dissection
Cerebrovasc. Dis.
24
343-348
2007
Homo sapiens
Manually annotated by BRENDA team
Shieh, T.M.; Lin, S.C.; Liu, C.J.; Chang, S.S.; Ku, T.H.; Chang, K.W.
Association of expression aberrances and genetic polymorphisms of lysyl oxidase with areca-associated oral tumorigenesis
Clin. Cancer Res.
13
4378-4385
2007
Homo sapiens
Manually annotated by BRENDA team
Fong, S.F.; Dietzsch, E.; Fong, K.S.; Hollosi, P.; Asuncion, L.; He, Q.; Parker, M.I.; Csiszar, K.
Lysyl oxidase-like 2 expression is increased in colon and esophageal tumors and associated with less differentiated colon tumors
Genes Chromosomes Cancer
46
644-655
2007
Homo sapiens
Manually annotated by BRENDA team
Akagawa, H.; Narita, A.; Yamada, H.; Tajima, A.; Krischek, B.; Kasuya, H.; Hori, T.; Kubota, M.; Saeki, N.; Hata, A.; Mizutani, T.; Inoue, I.
Systematic screening of lysyl oxidase-like (LOXL) family genes demonstrates that LOXL2 is a susceptibility gene to intracranial aneurysms
Hum. Genet.
121
377-387
2007
Homo sapiens
Manually annotated by BRENDA team
Hewitt, A.W.; Sharma, S.; Burdon, K.P.; Wang, J.J.; Baird, P.N.; Dimasi, D.P.; Mackey, D.A.; Mitchell, P.; Craig, J.E.
Ancestral LOXL1 variants are associated with pseudoexfoliation in Caucasian Australians but with markedly lower penetrance than in Nordic people
Hum. Mol. Genet.
17
710-716
2008
Homo sapiens
Manually annotated by BRENDA team
Weise, J.B.; Csiszar, K.; Gottschlich, S.; Hoffmann, M.; Schmidt, A.; Weingartz, U.; Adamzik, I.; Heiser, A.; Kabelitz, D.; Ambrosch, P.; Goeroegh, T.
Vaccination strategy to target lysyl oxidase-like 4 in dendritic cell based immunotherapy for head and neck cancer
Int. J. Oncol.
32
317-322
2008
Homo sapiens
Manually annotated by BRENDA team
Pasutto, F.; Krumbiegel, M.; Mardin, C.Y.; Paoli, D.; Laemmer, R.; Weber, B.H.; Kruse, F.E.; Schloetzer-Schrehardt, U.; Reis, A.
Association of LOXL1 common sequence variants in German and Italian patients with pseudoexfoliation syndrome and pseudoexfoliation glaucoma
Invest. Ophthalmol. Vis. Sci.
49
1459-1463
2008
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Schmidt, S.; Qin, X.; Gibson, J.; Hutchins, K.; Santiago-Turla, C.; Wiggs, J.L.; Budenz, D.L.; Akafo, S.; Challa, P.; Herndon, L.W.; Hauser, M.A.; Allingham, R.R.
Lack of association between LOXL1 variants and primary open-angle glaucoma in three different populations
Invest. Ophthalmol. Vis. Sci.
49
3465-3468
2008
Homo sapiens
Manually annotated by BRENDA team
Payne, S.L.; Hendrix, M.J.; Kirschmann, D.A.
Paradoxical roles for lysyl oxidases in cancer - a prospect
J. Cell. Biochem.
101
1338-1354
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Postovit, L.M.; Abbott, D.E.; Payne, S.L.; Wheaton, W.W.; Margaryan, N.V.; Sullivan, R.; Jansen, M.K.; Csiszar, K.; Hendrix, M.J.; Kirschmann, D.A.
Hypoxia/reoxygenation: a dynamic regulator of lysyl oxidase-facilitated breast cancer migration
J. Cell. Biochem.
103
1369-1378
2008
Homo sapiens
Manually annotated by BRENDA team
Goeroegh, T.; Weise, J.B.; Holtmeier, C.; Rudolph, P.; Hedderich, J.; Gottschlich, S.; Hoffmann, M.; Ambrosch, P.; Csiszar, K.
Selective upregulation and amplification of the lysyl oxidase like-4 (LOXL4) gene in head and neck squamous cell carcinoma
J. Pathol.
212
74-82
2007
Homo sapiens
Manually annotated by BRENDA team
Oleggini, R.; Gastaldo, N.; Di Donato, A.
Regulation of elastin promoter by lysyl oxidase and growth factors: cross control of lysyl oxidase on TGF-beta1 effects
Matrix Biol.
26
494-505
2007
Homo sapiens
Manually annotated by BRENDA team
Sivakumar, P.; Gupta, S.; Sarkar, S.; Sen, S.
Upregulation of lysyl oxidase and MMPs during cardiac remodeling in human dilated cardiomyopathy
Mol. Cell. Biochem.
307
159-167
2008
Homo sapiens
Manually annotated by BRENDA team
Mori, K.; Imai, K.; Matsuda, A.; Ikeda, Y.; Naruse, S.; Hitora-Takeshita, H.; Nakano, M.; Taniguchi, T.; Omi, N.; Tashiro, K.; Kinoshita, S.
LOXL1 genetic polymorphisms are associated with exfoliation glaucoma in the Japanese population
Mol. Vis.
14
1037-1040
2008
Homo sapiens
Manually annotated by BRENDA team
Mabuchi, F.; Sakurada, Y.; Kashiwagi, K.; Yamagata, Z.; Iijima, H.; Tsukahara, S.
Lysyl oxidase-like 1 gene polymorphisms in Japanese patients with primary open angle glaucoma and exfoliation syndrome
Mol. Vis.
14
1303-1308
2008
Homo sapiens
Manually annotated by BRENDA team
Fuse, N.; Miyazawa, A.; Nakazawa, T.; Mengkegale, M.; Otomo, T.; Nishida, K.
Evaluation of LOXL1 polymorphisms in eyes with exfoliation glaucoma in Japanese
Mol. Vis.
14
1338-1343
2008
Homo sapiens
Manually annotated by BRENDA team
Challa, P.; Schmidt, S.; Liu, Y.; Qin, X.; Vann, R.R.; Gonzalez, P.; Allingham, R.R.; Hauser, M.A.
Analysis of LOXL1 polymorphisms in a United States population with pseudoexfoliation glaucoma
Mol. Vis.
14
146-149
2008
Homo sapiens
Manually annotated by BRENDA team
Aragon-Martin, J.A.; Ritch, R.; Liebmann, J.; OBrien, C.; Blaaow, K.; Mercieca, F.; Spiteri, A.; Cobb, C.J.; Damji, K.F.; Tarkkanen, A.; Rezaie, T.; Child, A.H.; Sarfarazi, M.
Evaluation of LOXL1 gene polymorphisms in exfoliation syndrome and exfoliation glaucoma
Mol. Vis.
14
533-541
2008
Homo sapiens
Manually annotated by BRENDA team
Mossboeck, G.; Renner, W.; Faschinger, C.; Schmut, O.; Wedrich, A.; Weger, M.
Lysyl oxidase-like protein 1 (LOXL1) gene polymorphisms and exfoliation glaucoma in a Central European population
Mol. Vis.
14
857-861
2008
Homo sapiens
Manually annotated by BRENDA team
Laczko, R.; Szauter, K.M.; Jansen, M.K.; Hollosi, P.; Muranyi, M.; Molnar, J.; Fong, K.S.; Hinek, A.; Csiszar, K.
Active lysyl oxidase (LOX) correlates with focal adhesion kinase (FAK)/paxillin activation and migration in invasive astrocytes
Neuropathol. Appl. Neurobiol.
33
631-643
2007
Homo sapiens
Manually annotated by BRENDA team
Sakai, M.; Kato, H.; Sano, A.; Tanaka, N.; Inose, T.; Kimura, H.; Sohda, M.; Nakajima, M.; Kuwano, H.
Expression of lysyl oxidase is correlated with lymph node metastasis and poor prognosis in esophageal squamous cell carcinoma
Ann. Surg. Oncol.
16
2494-2501
2009
Homo sapiens
Manually annotated by BRENDA team
Erler, J.T.; Bennewith, K.L.; Cox, T.R.; Lang, G.; Bird, D.; Koong, A.; Le, Q.T.; Giaccia, A.J.
Hypoxia-induced lysyl oxidase is a critical mediator of bone marrow cell recruitment to form the premetastatic niche
Cancer Cell
15
35-44
2009
Homo sapiens
Manually annotated by BRENDA team
Lopez, B.; Querejeta, R.; Gonzalez, A.; Beaumont, J.; Larman, M.; Diez, J.
Impact of treatment on myocardial lysyl oxidase expression and collagen cross-linking in patients with heart failure
Hypertension
53
236-242
2009
Homo sapiens
Manually annotated by BRENDA team
Coral, K.; Angayarkanni, N.; Madhavan, J.; Bharathselvi, M.; Ramakrishnan, S.; Nandi, K.; Rishi, P.; Kasinathan, N.; Krishnakumar, S.
Lysyl oxidase activity in the ocular tissues and the role of LOX in proliferative diabetic retinopathy and rhegmatogenous retinal detachment
Invest. Ophthalmol. Vis. Sci.
49
4746-4752
2008
Homo sapiens
Manually annotated by BRENDA team
Papachroni, K.K.; Piperi, C.; Levidou, G.; Korkolopoulou, P.; Pawelczyk, L.; Diamanti-Kandarakis, E.; Papavassiliou, A.G.
Lysyl oxidase interacts with AGEs signaling to modulate collagen synthesis in polycystic ovarian tissue
J. Cell. Mol. Med.
14
2460-2469
2010
Homo sapiens
Manually annotated by BRENDA team
Shieh, T.M.; Tu, H.F.; Ku, T.H.; Chang, S.S.; Chang, K.W.; Liu, C.J.
Association between lysyl oxidase polymorphisms and oral submucous fibrosis in older male areca chewers
J. Oral Pathol. Med.
38
109-113
2009
Homo sapiens
Manually annotated by BRENDA team
Bondareva, A.; Downey, C.M.; Ayres, F.; Liu, W.; Boyd, S.K.; Hallgrimsson, B.; Jirik, F.R.
The lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the metastatic colonization potential of circulating breast cancer cells
PLoS ONE
4
e5620
2009
Homo sapiens, Homo sapiens (P28300)
Manually annotated by BRENDA team
Saad, F.A.; Torres, M.; Wang, H.; Graham, L.
Intracellular lysyl oxidase: effect of a specific inhibitor on nuclear mass in proliferating cells
Biochem. Biophys. Res. Commun.
396
944-949
2010
Rattus norvegicus (P16636), Homo sapiens (P28300), Homo sapiens
Manually annotated by BRENDA team
Santhanam, A.N.; Baker, A.R.; Hegamyer, G.; Kirschmann, D.A.; Colburn, N.H.
Pdcd4 repression of lysyl oxidase inhibits hypoxia-induced breast cancer cell invasion
Oncogene
29
3921-3932
2010
Homo sapiens (P28300), Homo sapiens
Manually annotated by BRENDA team
Herwald, S.E.; Greenaway, F.T.; Lopez, K.M.
Purification of high yields of catalytically active lysyl oxidase directly from Escherichia coli cell culture
Protein Expr. Purif.
74
116-121
2010
Homo sapiens
Manually annotated by BRENDA team
Schietke, R.; Warnecke, C.; Wacker, I.; Schdel, J.; Mole, D.; Campean, V.; Amann, K.; Goppelt-Struebe, M.; Behrens, J.; Eckardt, K.; Wiesener, M.
The lysyl oxidases LOX and LOXL2 are necessary and sufficient to repress E-cadherin in hypoxia: Insights into cellular transformation processes mediated by HIF-1
J. Biol. Chem.
285
6658-6669
2010
Homo sapiens
Manually annotated by BRENDA team
Xu, L.; Go, E.P.; Finney, J.; Moon, H.; Lantz, M.; Rebecchi, K.; Desaire, H.; Mure, M.
Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells
J. Biol. Chem.
288
5357-5363
2013
Homo sapiens (Q9Y4K0), Homo sapiens
Manually annotated by BRENDA team
Grimsby, J.L.; Lucero, H.A.; Trackman, P.C.; Ravid, K.; Kagan, H.M.
Role of lysyl oxidase propeptide in secretion and enzyme activity
J. Cell. Biochem.
111
1231-1243
2010
Homo sapiens (P28300)
Manually annotated by BRENDA team
Hutchinson, J.H.; Rowbottom, M.W.; Lonergan, D.; Darlington, J.; Prodanovich, P.; King, C.D.; Evans, J.F.; Bain, G.
Small molecule lysyl oxidase-like 2 (LOXL2) inhibitors the identification of an inhibitor selective for LOXL2 over LOX
ACS Med. Chem. Lett.
8
423-427
2017
Homo sapiens
Manually annotated by BRENDA team
Wiel, C.; Augert, A.; Vincent, D.F.; Gitenay, D.; Vindrieux, D.; Le Calve, B.; Arfi, V.; Lallet-Daher, H.; Reynaud, C.; Treilleux, I.; Bartholin, L.; Lelievre, E.; Bernard, D.
Lysyl oxidase activity regulates oncogenic stress response and tumorigenesis
Cell Death Dis.
4
e855
2013
Homo sapiens
Manually annotated by BRENDA team
Smith, M.A.; Gonzalez, J.; Hussain, A.; Oldfield, R.N.; Johnston, K.A.; Lopez, K.M.
Overexpression of soluble recombinant human lysyl oxidase by using solubility tags effects on activity and solubility
Enzyme Res.
2016
5098985
2016
Homo sapiens
Manually annotated by BRENDA team
Herchenhan, A.; Uhlenbrock, F.; Eliasson, P.; Weis, M.; Eyre, D.; Kadler, K.E.; Magnusson, S.P.; Kjaer, M.
Lysyl oxidase activity is required for ordered collagen fibrillogenesis by tendon cells
J. Biol. Chem.
290
16440-16450
2015
Homo sapiens
Manually annotated by BRENDA team
Bhuvanasundar, R.; Ragavachetty, N.; Singh, N.; Coral, K.; Deepa, P.; Sulochana, K.
Expression, purification and characterization of a biologically active and thermally stable human lysyl oxidase
Indian J. Biochem. Biophys.
56
105-116
2019
Homo sapiens (P28300)
-
Manually annotated by BRENDA team
Zhang, X.; Wang, Q.; Wu, J.; Wang, J.; Shi, Y.; Liu, M.
Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state
Proc. Natl. Acad. Sci. USA
115
3828-3833
2018
Homo sapiens (Q9Y4K0), Homo sapiens
Manually annotated by BRENDA team
De Vita, A.; Liverani, C.; Molinaro, R.; Martinez, J.O.; Hartman, K.A.; Spadazzi, C.; Miserocchi, G.; Taraballi, F.; Evangelopoulos, M.; Pieri, F.; Bongiovanni, A.; Mercatali, L.; Tasciotti, E.; Ibrahim, T.
Lysyl oxidase engineered lipid nanovesicles for the treatment of triple negative breast cancer
Sci. Rep.
11
5107
2021
Homo sapiens (Q08397)
Manually annotated by BRENDA team
Kim, I.K.; Lee, Y.S.; Kim, H.S.; Dong, S.M.; Park, J.S.; Yoon, D.S.
Specific protein 1(SP1) regulates the epithelial-mesenchymal transition via lysyl oxidase-like 2(LOXL2) in pancreatic ductal adenocarcinoma
Sci. Rep.
9
5933
2019
Homo sapiens (Q9Y4K0), Homo sapiens
Manually annotated by BRENDA team