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Information on EC 1.4.3.13 - protein-lysine 6-oxidase
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1.4.3.13 protein-lysine 6-oxidaseIUBMB 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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Word Map
- 1.4.3.13
- collagen
- fibrosis
- metastasis
- fiber
- copper
-
crosslinking
- amine
-
elastic
- glaucoma
- aortic
-
stiff
- beta-aminopropionitrile
- tropoelastin
-
copper-dependent
-
fibril
- metalloproteinases
- procollagens
-
biomechanical
- propeptide
-
exfoliation
-
fibrillar
-
tensile
- myofibroblasts
- aneurysm
-
pseudoexfoliation
- cutis
-
copper-binding
- fibrillin-1
-
open-angle
- menkes
-
copper-deficient
-
prolapse
-
fibrillogenesis
-
cross-linkage
- desmosine
-
copper-containing
- medicine
- benzylamine
- diagnostics
-
pentosidine
- synthesis
-
microfibrillar
-
microfibrils
-
elastosis
- ehlers-danlos
-
elastolytic
-
col3a1
-
semicarbazide-sensitive
-
cuproenzymes
-
c-proteinase
-
fibulins
- hydroxylysine
-
pyridinoline
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Synonyms
lysyl oxidase, loxl2, loxl1, loxl4, loxl3, lox-pp, lysyl oxidases, lysyl oxidase-like 1, lysyl oxidase-like 2, lysyl oxidase-like, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LO
LOX
LOXL
LOXL1
Loxl2
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 propetide
-
has biological activity as a tumor suppressor, and it inhibits Erk1/2 Map kinase activation
lysyl oxidase-like 1
lysyl oxidase-like 2
lysyl oxidase-like protein
RAS excision protein
-
-
-
-
additional information
-
enzymes belong to the lysyl oxidase family of copper amine oxidases
LOX
-
-
LOX
-
-
LOX
-
LOXactivity is essential to generate optimal chemotactic sensitivity of cells to chemoattractants by oxidizing specific cell surface proteins, such as platelet-derived growth factor-beta
LOX
-
LOXactivity is essential to generate optimal chemotactic sensitivity of cells to chemoattractants by oxidizing specific cell surface proteins, such as platelet-derived growth factor-beta
LOXL1
-
-
lysyl oxidase
-
amine oxidase, oxidative deamination
lysyl oxidase
-
-
lysyl oxidase
-
-
lysyl oxidase-like 1
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
-
-
-
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
information about the activation mechanism of copper
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
preprotein, lysyl oxidase gene family, amine oxidation through ping pong bi ter kinetic mechanism
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
Also acts on protein 5-hydroxylysine
-
-
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
active site structure, a unique funnel defines substrate specificity
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview
-
[protein]-L-lysine + O2 + H2O = [protein]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
ping-pong mechanism of 2 half-reactions completing the catalytic cycle, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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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].
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CAS REGISTRY NUMBER
COMMENTARY
99676-44-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
collagen 2a1 + O2 + H2O
?
-
-
-
?
histone H2 + O2 + H2O
?
-
recombinant mature LOX and C-terminally deleted enzyme
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
tropoelastin + O2 + H2O
? + H2O2 + NH3
-
oxidation of L-lysine residues, substrate from mammalia
-
-
?
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
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
-
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
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
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
-
-
?
histone H1 + O2 + H2O
?
-
recombinant mature LOX and C-terminally deleted enzyme
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
part of tropocollagen and tropoelastin
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
deamination of lysyl and hydroxylysyl residues is part of the pyridinoline biosynthetic pathway, pyridinoline is involved in formation of intracellular and extracellular collagen cross-links responsible for aging of connective tissue
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variety of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
key enzyme in formation of lysine cross-links in side collagen and elastin molecules
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
substrates are proteins of the extracellular matrix
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variatey of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in collagen and elastin fibrills
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
formation of cross-links in mature fibrillar collagen and elastin fibers in the extracellular space
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
initiation of covalent intermolecular cross-linking of collagen by the enzyme action on telopeptidyl lysine and hydroxylysine residues
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
lysyl oxidase plays a critical role in the formation of the extracellular matrix, and its activity is required for the normal maturation and cross-linking of collagen and elastin
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variatey of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of tropocollagen and tropoelastin
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of elastin and collagen
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of elastin and collagen
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
crosslinkage in fibrillar collagen and elastin
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
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
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
the enzyme does not affect smooth muscle cell proliferation nor elastin precursor, tropoelastin, synthesis, nor total elastin synthesis in a per-cell-basis
-
-
?
additional information
?
-
-
critical role for lysyl oxidase in zebrafish notochord morphogenesis
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport
-
-
?
additional information
?
-
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
-
the enzyme forms are differently involved in tumor suppression, cellular senescence, and chemotaxis
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
potential role of lysyl oxidase/placental lactogen interactions in breast epithelial cell proliferation and migration
-
-
?
additional information
?
-
-
LOXL3 encodes two variants, LOXL3 and LOXL3-sv1, both of which function as amine oxidases with distinct tissue and substrate specificities
-
-
?
additional information
?
-
-
catalyzes the cross-linking of collagens or elastin in the extracellular compartment, thereby regulating the tensile strength of tissues
-
-
?
additional information
?
-
-
purifiedLOXreadily oxidizes peptidyl lysines in basic globular proteins with isoelectric points greater than pH 8, whereas no oxidation is detected in neutral or acidic proteins with isoelectric points less than pH 8
-
-
?
additional information
?
-
-
LOX is a copper-dependent amine oxidase that initiates the covalent cross-linking of collagen and elastin side chains and thereby contributes to extracellular matrix integrity
-
-
?
additional information
?
-
-
LOX is an extracellular matrix-remodeling enzyme involved in regulation of tumor metastasis
-
-
?
additional information
?
-
-
LOX secreted by hypoxic breast tumor cells accumulates at premetastatic sites, crosslinks collagen IV in the basement membrane, and is essential for CD11b+ myeloid cell recruitment. LOX inhibition prevents CD11b+ cell recruitment and metastatic growth. CD11b+ cells and LOX also colocalize in biopsies of human metastases, detailed overview
-
-
?
additional information
?
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC12 cells
-
-
?
additional information
?
-
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC12 cells
-
-
?
additional information
?
-
-
enzymatic activity is assayed using a peroxide-coupled assay and the nonpeptidyl substrate 1,5-diaminopentane producing the corresponding aldehyde
-
-
?
additional information
?
-
-
enzyme is responsible for the cross-linking of collagen and elastin, and is required for vascular and diaphragmatic development during embryogenesis
-
-
?
additional information
?
-
-
expression of isozymes LOXL1,3,4 during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
-
-
?
additional information
?
-
-
LOX is essential for collagen and elastin matrix stability and newborn animal survival
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
lysyl oxidase is essential for normal development and function of the respiratory system and for the integrity of elastic and collagen fibers in various tissues
-
-
?
additional information
?
-
-
catalyzes the cross-linking of collagens or elastin in the extracellular compartment, thereby regulating the tensile strength of tissues
-
-
?
additional information
?
-
-
purified LOX readily oxidizes peptidyl lysines in basic globular proteins with isoelectric points greater than pH 8, whereas no oxidation is detected in neutral or acidic proteins with isoelectric points less than pH 8
-
-
?
additional information
?
-
-
lysyl oxidase, an amine oxidase, is critical for the initiation of collagen and elastin cross-linking, binds transforming growth factor-beta, and regulates its signaling via amine oxidase activity, mechanism, overview. LOX suppresses TGF-beta1-induced Smad3 phosphorylation likely through its amine oxidase activity
-
-
?
additional information
?
-
-
the enzyme forms desmosine crosslinking structures in elastic fibers contributing to the elasticity
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix
-
-
?
additional information
?
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC-12 cells
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
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
-
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
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
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
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
deamination of lysyl and hydroxylysyl residues is part of the pyridinoline biosynthetic pathway, pyridinoline is involved in formation of intracellular and extracellular collagen cross-links responsible for aging of connective tissue
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
key enzyme in formation of lysine cross-links in side collagen and elastin molecules
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
substrates are proteins of the extracellular matrix
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
formation of cross-links in mature fibrillar collagen and elastin fibers in the extracellular space
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
initiation of covalent intermolecular cross-linking of collagen by the enzyme action on telopeptidyl lysine and hydroxylysine residues
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
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
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
the enzyme does not affect smooth muscle cell proliferation nor elastin precursor, tropoelastin, synthesis, nor total elastin synthesis in a per-cell-basis
-
-
?
additional information
?
-
-
critical role for lysyl oxidase in zebrafish notochord morphogenesis
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport
-
-
?
additional information
?
-
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
-
the enzyme forms are differently involved in tumor suppression, cellular senescence, and chemotaxis
-
-
?
additional information
?
-
-
potential role of lysyl oxidase/placental lactogen interactions in breast epithelial cell proliferation and migration
-
-
?
additional information
?
-
-
LOX is a copper-dependent amine oxidase that initiates the covalent cross-linking of collagen and elastin side chains and thereby contributes to extracellular matrix integrity
-
-
?
additional information
?
-
-
LOX is an extracellular matrix-remodeling enzyme involved in regulation of tumor metastasis
-
-
?
additional information
?
-
-
LOX secreted by hypoxic breast tumor cells accumulates at premetastatic sites, crosslinks collagen IV in the basement membrane, and is essential for CD11b+ myeloid cell recruitment. LOX inhibition prevents CD11b+ cell recruitment and metastatic growth. CD11b+ cells and LOX also colocalize in biopsies of human metastases, detailed overview
-
-
?
additional information
?
-
-
enzyme is responsible for the cross-linking of collagen and elastin, and is required for vascular and diaphragmatic development during embryogenesis
-
-
?
additional information
?
-
-
expression of isozymes LOXL1,3,4 during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
-
-
?
additional information
?
-
-
LOX is essential for collagen and elastin matrix stability and newborn animal survival
-
-
?
additional information
?
-
-
lysyl oxidase is essential for normal development and function of the respiratory system and for the integrity of elastic and collagen fibers in various tissues
-
-
?
additional information
?
-
-
lysyl oxidase, an amine oxidase, is critical for the initiation of collagen and elastin cross-linking, binds transforming growth factor-beta, and regulates its signaling via amine oxidase activity, mechanism, overview. LOX suppresses TGF-beta1-induced Smad3 phosphorylation likely through its amine oxidase activity
-
-
?
additional information
?
-
-
the enzyme forms desmosine crosslinking structures in elastic fibers contributing to the elasticity
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
topaquinone
-
i.e. TPQ or 2,4,5-trihydroxyphenylalanine quinone, formed by posttranslational modification of a tyrosine residue
additional information
-
enzyme contains a cross-linked quinone, cross-linking via lysyl- and tyrosyl residues
-
lysyl-tyrosyl quinone
-
essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, autcatalytic hydroxylation and oxidation of a Tyr residue, structure overview
lysyl-tyrosyl quinone
-
essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, Lys314 and Tyr349 are progenitors of the cofactor, autcatalytic hydroxylation and oxidation of Tyr349, structure overview
lysyl-tyrosyl quinone
-
essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, structure overview
lysyl-tyrosyl quinone
Lys-653 and Tyr-689 are the precursor residues for the lysyl-tyrosyl quinone cofactor of the enzyme
lysyl-tyrosyl-quinone
-
LOX, LOXL1, LOXL2, LOXL3, and LOXL4 contain binding residues
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
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
-
enzyme is a copper amino axidase, contains 1 type II copper atom per subunit
Cu2+
Cu2+
-
enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction
Cu2+
copper-cofactor, lysyl oxidase and LOX-like proteins LOXL-1 and LOXL-2, conserved binding domain
Cu2+
0.6 g atom of copper per monomer of rDMLOXL, tetragonal Cu(II) site with nitrogen and oxygen ligands
Cu2+
-
copper metalloenzyme, activation and induction of enzyme synthesis, copper-induced activation maximal at 0.005 mg of copper/ml
Cu2+
-
copper metalloenzyme contains 0.14% copper, important for enzymatic function
Cu2+
-
dependent on, copper-binding domain in LOX, LOXL1, LOXL2, LOXL3, and LOXL4
Cu2+
-
enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction
Cu2+
copper loading activates hLOXL2 and supports lysyl tyrosylquinone formation
Cu2+
-
tightly bound in a tetragonally distorted, octahedrally coordinated ligand field, one per mol
Cu2+
-
enzyme has a copper-binding domain, copper-cofactor is required, tightly bound at the active site, may play a conformational role in the initial half-reaction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
-
ascorbic acid
-
inhibits the purified enzyme in vitro, and the formation of cross-linked collagen
Disulfiram
-
a dithiocarbamate and Cu2+-chelator, inhibits the enzyme and causes teratogenic effects, malformations, distorted notochord development, and shortened anterior to posterior axis in zebrafish, overview
N-[2-([2-[(1-oxidopyridin-2-yl)sulfanyl]ethyl]amino)ethyl]-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide
-
fully effective at 0.02 mM
tert-butyl [2-[(1-oxidopyridin-2-yl)sulfanyl]ethyl]carbamate
-
fully effective at 0.002 mM
thiram
-
a dithiocarbamate and Cu2+-chelator, inhibits the enzyme and causes teratogenic effects, malformations, distorted notochord development, and shortened anterior to posterior axis in zebrafish, overview
VE-statin/egfl7 protein
-
interacts with the catalytic domain of lysyl oxidase thereby preventing the crosslink of tropoelastin molecules into mature elastin polymers and regulating vascular elastogenesis
-
beta-aminopropionitrile
-
beta-aminopropionitrile
-
lathyrogen, organic nitrile group, blocks active site irreversibly and binds covalently
beta-aminopropionitrile
-
inhibition of active recombinant LOX, LOXL1, and LOXL2, specific
beta-aminopropionitrile
a specific lysyl oxidase inhibitor, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview
beta-aminopropionitrile
a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
beta-aminopropionitrile
-
LOX activity is inhibited by 0.5 mM and above concentrations
beta-aminopropionitrile
-
reduces LOX activity and significantly increases MCP-1 secretion in vascular smooth uscle cells
beta-aminopropionitrile
a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
cycloheximide
-
inhibits incorporation of lysine and Cu2+ into enzyme, blocks activating process
Isonicotinic acid hydrazide
-
reversible, 61.8% of full activity restored by pyridoxal or 30.1% by pyrroloquinoline-quinone
low-density lipoprotein
-
decreases lysyl oxidase mRNA levels in endothelial cells
-
Semicarbazide
-
reversible, 21.2% of full activity restored by pyridoxal or 10% by pyrroloquinoline-quinone
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 endothelial LOX enzymatic activity
-
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
-
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 endothelial LOX enzymatic activity
-
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 endothelial LOX enzymatic activity
-
tumor necrosis factor-alpha
-
inhibits LOX mRNA transcription and LOX activity
-
additional information
-
LOXL4 suppresses the expression of laminins and alpha3 integrin and the activity of matrix metalloproteinase-2
-
additional information
-
LOX propeptide expression in Her-2/neu-driven breast cancer cells in culture suppresses Akt, extracellular signal-regulated kinase, and nuclear factor-kappaB activation
-
additional information
-
TNF-alpha-stimulated matrix metalloproteinase-9 expression and Erk1/2 activation are both significantly inhibited by LOX-PP
-
additional information
-
hypercholesterolemia down-regulates LOX expression and activity
-
additional information
alkylamino derivatives of 4-aminomethylpyridine, substrate-like, reversible inhibitors
-
additional information
-
hypercholesterolemia down-regulates LOX expression and activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hypoxia inducible factor-1
-
hypoxia-induced LOX expression is partially mediated by hypoxia inducible factor-1
tumor growth factor-beta1
-
stabilizes LOX mRNA leading to an increase in LOX activity
-
transforming growth factor-beta1
-
fibrogenic cytokine, strongly promotes enzyme expression in fibroblasts of neonatal rat lung, human embryos and rat vascular smooth muscle cells
-
transforming growth factor-beta1
-
fibrogenic cytokine, strongly promotes enzyme expression in fibroblasts of neonatal rat lung, human embryos and rat vascular smooth muscle cells
-
additional information
-
active LOX promotes focal adhesion kinase activation and invasive/migratory behaviour of astrocytes
-
additional information
-
hypoxia/reoxygenation drives poorly invasive breast cancer cells toward a more aggressive phenotype by up-regulating LOX expression and catalytic activity
-
additional information
-
LOX regulates also the promoter of elastin und collagen III, treatment with tumor growth factor-beta1 and CTGF abolishes completely the activation induced by LOX
-
additional information
-
the transcriptional level of LOX is significantly upregulated in dilated cardiomyopathy hearts
-
additional information
-
the lysyl oxidase gene is induced by quiescence in general rather than specific to serum deprivation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.373
1,5-Diaminopentane
pH 8.2, temperature not specified in the publication
additional information
additional information
-
kinetics of the interaction with elastin and histones for recombinant mature enzyme and C-terminally deleted enzyme form
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7290
1,5-Diaminopentane
pH 8.2, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000321
1-([2,3'-bipyridin]-4-yl)methanamine
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
0.1
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
Sus scrofa
-
0.1
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
Sus scrofa
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.2
additional information
additional information
-
0.0214 cpm of titrated water formed per h per g wet weight of tissue
additional information
-
4.533 cpm/mg protein for elastin and 1.633 cpm/mg for collagen as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 6.5
-
pH 5.8: about 30% of maximal activity, pH 6.5: about 40% of maximal activity
7.5 - 8.5
pH 7.5: about 55% of maximal activity, pH 8.5: about 85% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression is sensitively modulated by specific cytokines, growth factors and related intercellular molecular messengers
-
-
brenda
LOXL-1; lysyl oxidase and 2 LOX-like proteins LOXL and LOXL2
SwissProt
brenda
LOXL-2; lysyl oxidase and 2 LOX-like proteins LOXL and LOXL2
SwissProt
brenda
-
391742, 658190, 673118, 673475, 674712, 674870, 684316, 684802, 684931, 685931, 685943, 685957, 686038, 686141, 686947, 687028, 687037, 687183, 687203, 687205, 687919, 687920, 688584, 688796, 688955, 689098, 689099, 689100, 689101, 689102, 689104, 689199, 695612, 697071, 698212, 698383, 699125, 699715, 700903
-
-
brenda
enzyme forms: lysyl oxidase and 4 LOX-like proteins LOXL1, LOXL2, LOXL3, and LOXL4
-
-
brenda
structurally and functionally diverse enzyme forms: lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4, probably existing splicing variants of LOXL3
-
-
brenda
-
391742, 659197, 671208, 684322, 684376, 685781, 685940, 685949, 685981, 686106, 686366, 686392, 687198, 687204, 687751, 687919, 696829, 698849, 724520, 742476, 743281
-
-
brenda
adult B6SJLF1 mice, structurally and functionally diverse enzyme forms: lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4, probably existing splicing variants of LOXL3
-
-
brenda
C57BL/6 mice, enzyme forms: lysyl oxidase LOX and lysyl oxidase-like protein LOXL
-
-
brenda
-
-
-
brenda
LOU and Brown-Norway rats, male inbred BN/Rij rats, two inbred strains with different susceptibilities to arterial fragility, genes and isozymes LOXL1 and LOX
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
LOX is highly expressed in early gestational amnion tissue (12-14 weeks)
brenda
-
LOX on the surface of pyramidal cells in the grey matter, LOXL in the nuclei of cortex cells and in the cytosol of capillary endothelial cells
brenda
-
of lung: LOX and LOXL, renal tubules: only LOXL, intestinal: only LOXL
brenda
-
including dermal papillae, follicular sheaths, sebaceous glands
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
-
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
brenda
-
LOX gene expression is reduced in pancreatic cancer cells
brenda
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC-12 cells
brenda
-
pepsin-secreting, in the basal part of the stomach, only LOX, no LOXL
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
additional information
-
different spatial and temporal expression of LOX and LOXL1 during growth and aging, expression analysis of LOXL1 and LOX in the aorta during the development, growth, and aging of LOU rats, overview
brenda
subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy
brenda
-
subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy
-
brenda
-
localization of LOX and LOXL in different tissue areas, LOXL is found in the apical surface of columnar absorbing cells, LOX is located in the submucosa
brenda
from days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells
brenda
-
from days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells
-
brenda
-
lysyl oxidase protein expression is very scarce in normal hearts, it is highly expressed in failing hearts
brenda
-
overexpressed in head and neck squamous cell carcinoma compared to normal squamous epithelium
brenda
-
co-localization of LOX and LOXL in alveoli and the epithelia of bronchus and bronchiole
brenda
-
osteoblastic cell, CRL-2593, expression of LOXL1, 3, and 4, not 2, expression patterns during cell differentiatin and matrix mineralization, 4 weeks, overview
brenda
-
from mantle, fins and arms. Fins show the highest LOX activity
brenda
-
expression of isozymes during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
brenda
-
localization of LOX and LOXL in different tissue areas, LOX is located in the inner surface of the pigmented epithelia in the photoreceptor layer, LOXL is located in the inner nuclear layer within the outer plexiform layer and in the ganglion cells
brenda
-
extract obtained from dill stimulates the LOXL gene expression in dermal equivalents. The stimulation by the dill extract is correlated with increased elastin detection, suggesting an increase in elastogenesis efficiency
brenda
-
LOXL, lamia propria and straited border, not of Goblet cells
brenda
additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, no expression of LOXL-2 in larvae, pupae, and embryos, overview
brenda
additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, no expression of LOXL-2 in larvae, pupae, and embryos, overview
brenda
additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, overview
brenda
additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, overview
brenda
additional information
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization, expression patterns, LOX and LOXL are expressed in most tissues
brenda
additional information
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization
brenda
additional information
-
nearly no enzyme content in blood vessels, expression level of LOX and LOXL in different tissues during development from embryonic, newborn, and young to adult mice, overview
brenda
additional information
-
high aortic LOX expression early in the development, i.e. embryonic day 15, followed by a drastic reduction in adulthood, whereas LOXL1 is mainly detectable in the intima and media and is expressed throughout life in the LOU rat
brenda
additional information
quantitative expression analysis of LOX isozymes in different subcellular compartments in PC-12 cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
LOX is secreted as a glycosylated proenzyme with a MW of 50 kDa, and is proteolytically processed by procollagen C proteinase, i.e. bone morphogenic protein-1, into a mature, biologically active MW 32 kDa form
-
brenda
-
mature LOX and mature TGF-beta1 are colocalized in the extracellular matrix in an osteoblastic cell culture system
-
brenda
-
inactive proenzyme proLO is secreted into the medium of cell culture
-
brenda
quantitative expression analysis of LOX isozymes, overview
brenda
additional information
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization
-
brenda
additional information
-
not present in nuclei of transfected cells. LOXL3 encodes two variants, LOXL3 and LOXL3-sv1, both of which function as amine oxidases with distinct tissue and substrate specificities from one another
-
brenda
additional information
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization
-
brenda
additional information
-
the enzyme is secreted as inactive enzyme of about 50 kDa and processed to a mature about 30 kDa enzyme
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
the enzyme is a promising therapeutic target for the progression of cancer and fibrosis
evolution
J9NZK5
the protein is very well conserved throughout the course of evolution
malfunction
metabolism
physiological function
additional information
malfunction
-
association between enzyme polymorphisms and oral submucous fibrosis in older male areca chewers
malfunction
-
excess collagen deposition in ovarian stroma in polycystic ovary syndrome involves increased enzyme activity due to stimulation by advenced glycation end products
malfunction
-
reduced enzyme expression is involved in the vitreous of proliferative diabetic retinopathy, PDR, and rhegmatogenous retinal detachment, RRD
malfunction
-
the enzyme regulates collagen cross-linking, which is increased in heart failure patients compared with healthy hearts. Enzyme overexpression is associated with enhanced collagen cross-linking in the failing human heart. Ability of torasemide to correct both lysyl oxidase overexpression and enhanced collagen cross-linking
malfunction
-
enzyme inhibition stops early mechanical development of tendon constructs and leads to irregularly shaped collagen fibrils
malfunction
-
inhibition of lysyl oxidase activity stabilizes oncogenic stress-induced senescence, delays tumorigenesis, and increases survival
metabolism
-
the enzyme is linked to crosslinking of elastin and collagen, it enhances tropoelastin crosslinking into matrix structures and elastin matrix yield, overview
metabolism
-
the enzyme is linked to crosslinking of elastin and collagen, it enhances tropoelastin crosslinking into matrix structures and elastin synthesis and matrix yield, overview
metabolism
-
by deacetylating and deacetyliminating Stat3 on multiple acetyl-lysine sites in nuclei, the enzyme regulates Stat3 dimerization and transcriptional activity. Furthermore, CD4+ T cell differentiation in inflammatory responses is regulated by the enzyme-Stat3 signaling pathway
metabolism
co-overexpression of specific protein 1 (SP1) and LOXL2 significantly correlates with poor prognosis in patients with pancreatic cancer
metabolism
the enzyme catalyzes cross-linking of collagen and elastin in the extracellular matrix
metabolism
-
the enzyme catalyzes cross-linking of collagen and elastin in the extracellular matrix
-
physiological function
-
LOX cross-links the side chain of collagen and elastin and thereby contributes to extracellular matrix integrity
physiological function
-
LOX is a copper-activated enzyme critical for collagen cross-linking and organization of extracellular matrix
physiological function
-
lysyl oxidase acts as both a matrix modifying enzyme and an oncogene suppressor
physiological function
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix. LOX mediates suppression of MCP-1, one of the highly upregulated chemokines, and subsequent inflammatory responses, overview
physiological function
-
lysyl oxidases play a critical role in matrix assembly by crosslinking elastin and collagen monomers into fibers
physiological function
-
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
physiological function
-
role for lysyl oxidase-like, LOXL1, in adult elastin synthesis and a role for its isoform, lysyl oxidase, LOX, in the synthesis of both collagens and elastin during development. Specific roles for LOX and LOXL1 in the synthesis and remodeling of elastic and collagen fibers, overview
physiological function
-
the enzyme binds to mature TGF-beta1 and enzymatically regulates its signaling in bone and plays an important role in bone maintenance and remodeling
physiological function
-
the enzyme is involved n collagen synthesis. It catalyzes the collagen and elastin cross-linking and plays an essential role in coordinating the control of ovarian extracellular matrix during ovarian follicle development, overview
physiological function
the extracellular matrix remodeling enzyme has a role in promoting breast cancer cell motility and invasiveness. LOX activity is required during extravasation and/or initial tissue colonization by circulating MDA-MB-231 cells, metastasis model and drug administration study in mice, overview
physiological function
LOX is the principal enzyme involved in crosslinking of collagen. Nuclear lysyl oxidase probably regulates nuclear growth, and thereby modulates cell proliferation, overview
physiological function
LOX is the principal enzyme involved in crosslinking of collagen. Nuclear lysyl oxidase probably regulates nuclear growth, and thereby modulates cell proliferation, overview
physiological function
the enzyme induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion
physiological function
-
the lysyl oxidases LOX and LOXL2 are necessary and sufficient to repress E-cadherin in hypoxia, thereby inducing epithelial to mesenchymal transition
physiological function
-
enzyme activity contributes to collagen stabilization during liver fibrosis progression and limits spontaneous fibrosis reversal
physiological function
-
lysyl oxidase activity is required for ordered collagen fibrillogenesis by tendon cells
physiological function
-
the enzyme participates in primary tumor growth by directly impacting the senescence stability
physiological function
-
the enzyme restricts Stat3-dependent cell proliferation and immune cell differentiation and inflammatory response
physiological function
J9NZK5
role in interlinking of collagen and elastin by oxidizing lysine residues
physiological function
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
additional information
LOX expression opposes the effect of mutationally activated Ras, which is present in about 30% of human cancers. Proliferating cells dramatically increase their nuclear protein content when exposed to beta-aminopropionitrile, a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
additional information
-
LOX expression opposes the effect of mutationally activated Ras, which is present in about 30% of human cancers. Proliferating cells dramatically increase their nuclear protein content when exposed to beta-aminopropionitrile, a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
additional information
LOX is a hypoxia-inducible amine oxidase, the activity of which enhances breast cancer cell invasion in vitro and in vivo. Specific inhibition of LOX activity by beta-aminopropionitrile or small interfering RNA decreased the invasiveness of T-47D and MCF-7 breast cancer cells attenuated for Pdcd4 function. Tumor suppressor Pdcd4 inhibits breast cancer cell migration and invasion in vitro. Loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of lysyl oxidase mRNA
additional information
-
LOX is a hypoxia-inducible amine oxidase, the activity of which enhances breast cancer cell invasion in vitro and in vivo. Specific inhibition of LOX activity by beta-aminopropionitrile or small interfering RNA decreased the invasiveness of T-47D and MCF-7 breast cancer cells attenuated for Pdcd4 function. Tumor suppressor Pdcd4 inhibits breast cancer cell migration and invasion in vitro. Loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of lysyl oxidase mRNA
additional information
-
lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview. LOX inhibition might be useful in metastasis prevention
additional information
lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview. LOX inhibition might be useful in metastasis prevention
additional information
-
partial knockdown of three LOX genes, lox,loxl1 and loxl5b, sensitizes the developing embryo to dithiocarbamate exposure
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
28000
29000
30000
32000
34000
35000
36000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
46000
50000
51000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
59000
-
x * 59000, x * 61000, SDS-PAGE, may be isoenzymes or heterologous subunits
61000
-
x * 59000, x * 61000, SDS-PAGE, may be isoenzymes or heterologous subunits
83600
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
97000
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
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
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
32000
-
ProLOX is subsequently cleaved into its catalytically mature 32000Da protein (LOX) and an 18000 Da LOX-propeptide
32000
-
ProLOX is subsequently cleaved into its catalytically mature 32000Da protein (LOX) and an 18000 Da LOX-propeptide
32000
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
34000
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
46000
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
50000
-
N-glycosylated and secreted from the cell as a catalytically inactive 50000 Da proenzyme protein (proLOX)
50000
-
N-glycosylated and secreted from the cell as a catalytically inactive 50000 Da proenzyme protein (proLOX)
50000
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
?
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
?
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
?
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
?
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
additional information
domain structure of LOX-like protein, LOXL-1 and LOXL-2 contain SRCR domains
additional information
domain structure of LOX-like protein, LOXL-1 and LOXL-2 contain SRCR domains
additional information
-
structural implications of primary sequence, profile of ionic residues in LO and LOXL-1, overview
additional information
-
the enzymes' tertiary and quarternary fold is similar but the active site structure is more exposed and accesible compared to the structure of other quinone-containing copper amine oxidases
additional information
-
LOX and LOXL are immunologically distinct, specific antibodies do not cross-react
additional information
-
structural implications of primary sequence, profile of ionic residues, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
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
the LOX propeptide is glycosylated. Glycosylation is not required for secretion and extracellular processing of pro-enzyme but it is required for optimal enzyme activity of the resulting mature enzyme
proteolytic modification
-
proenzyme proLO contains a catalysis-suppressing domain and an N-terminal signal peptide
proteolytic modification
-
activation of the proenzyme by cleavage, enzyme contains a BMP-1 cleavage site
proteolytic modification
-
enzyme contains a catalysis-suppressing propeptide signal domain at the N-terminus
proteolytic modification
-
LOX, LOXL1, LOXL2, LOXL3, and LOXL4, enzymes contain a conserved BMP-1 cleavage site at Gly134-Asp135 and Ser337-Asp338
proteolytic modification
-
N-terminal processing by BMP-1 of lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 in the extracellular matrix results in active proteins
proteolytic modification
-
LOX is secreted as a glycosylated proenzyme with a MW of 50 kDa, and is proteolytically processed by procollagen C proteinase, i.e. bone morphogenic protein-1, into a mature, biologically active MW 32 kDa form
proteolytic modification
-
lysyl oxidase is synthesized and exported to the extracellular space as a 50 kDa inactive preproprotein. In the extracellular space, it is cleaved at the specific Gly168-Asp169 by procollagen C-proteinase to yield the active 29 kDa enzyme
proteolytic modification
-
proteolytically cleaved to the 32 kDa catalytically active enzyme
proteolytic modification
-
N-terminal processing by BMP-1 of lysyl oxidase and LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 in the extracellular matrix results in active proteins
proteolytic modification
-
the enzyme is secereted as inactive enzyme of about 50 kDa and processed into a mature about 30 kDa enzyme and a 18 kDa propeptide
proteolytic modification
-
proenzyme proLO contains a catalysis-suppressing domain, cleavage site is Gly162-Asp163, and an N-terminal signal peptide, cleavage site is Cys21-Ala22, cleavage of the proenzyme domain by metalloendoprotease procollagen C-proteinase
additional information
-
LOX suffers different posttranslational modifications including signal peptide cleavage, glycosylation, copper incorporation and formation of the lysyl-tyrosyl-quinone cofactor
additional information
-
LOX suffers different posttranslational modifications including signal peptide cleavage, glycosylation, copper incorporation and formation of the lysyl-tyrosyl-quinone cofactor
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at 18°C, crystal structure of the enzyme at 2.4 A resolution
purified recombinant enzyme, X-ray structure determination and analysis at 1.65 A resolution, modelling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G153D
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
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
G153D
-
mutant with strong association to pseudoexfoliation and pseudoexfoliation glaucoma
G153D
-
the mutation is highly associated with exfoliation syndrome and exfoliation glaucoma
R141L
-
mutant with strong association to pseudoexfoliation and pseudoexfoliation glaucoma
R141L
-
the mutation is associated with the occurence of exfoliation glaucoma
R141L
-
the mutation is highly associated with exfoliation syndrome and exfoliation glaucoma
additional information
-
LOXL1 gene variants play no significant role in the pathogenesis of primary open-angle glaucoma
additional information
-
construction of a deletion mutant by targeted mutagenesis, the mutant mice lacking the enzyme activity dies soon after parturition exhibiting cardivascular instability with ruptured arterial aneurysms and diaphragmatic rupture due to fragmented elastic fiber architecture in the aorta, overview, the homozygous mutants show about 60% reduced activity in lung and aorta compared to the wild-type mice
additional information
-
mutations of the Lox or LoxL1 genes result in a poorly formed vessel wall that is prone to breakdown and aneurysm
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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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
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
46.9fold from aorta by DEAE-cellulose ion exchange chromatography and gel filtration
-
immobilized metal chelate column chromatography
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
-
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
-
truncated enzyme without the N-terminal peptide. Metal affinity chromatography under denaturing conditions followed by refolding
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from cDNA library, DNA and amino acid sequence determination and analysis, expression of C-terminally His6-tagged LOX in Escherichia coli
-
expressed in Escherichia coli
expressed in immature dendritic cells derived from peripheral blod mononuclear cells
-
expression in Escherichia coli
expression in Escherichia coli. Heterologously expression yields an active recombinant enzyme with important biochemical features conserved
-
expression of mature enzyme and C-terminally deleted enzyme as N-terminally His6-tagged enzymes
-
expression of mature enzyme, proenzyme, and of isolated propeptide in Escherichia coli strain BL21-A1
-
expression of proenzyme, mature enzyme, isolated propeptide, and mutant enzymes in HEK-293 cells as HA-tagged proteins
-
expression of proteolytically processed forms of LOX, LOXL1, and LOXL2 in Escherichia coli as N-terminally His6-tagged proteins
-
genes and isozymes LOXL1 and LOX, detailed expression analysis in aorta during growth and development, overview
-
LOX genotyping of Asian non-areca nut chewers and arec nut chewers of different ages, overview
-
LOX propeptide is expressed in mouse mammary tumor virus Her-2/neu-driven breast cancer cell line
-
real-time quantitative PCR enzyme expression analysis in wild-type and mutant mice
-
RT-PCR enzyme expression analysis in esophageal squamous cell carcinoma cells, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ability of torasemide to correct both lysyl oxidase overexpression and enhanced collagen cross-linking
-
in MIA Paca-2 cells, silencing of apecific protein 1 (SP1) induces a reduction of LOXL2 expression
lineage-specific mutation of the type II TGFbeta receptor gene, Tgfbetar2, in both neural crest- and mesoderm-derived vascular smooth muscle precursors leads to absence of TGFbeta receptor function and reduced lysyl oxidase expression. The result is a poorly organized vascular elastic matrix in late-stage embryos, which is prone to dilation and aneurysm, due to a failure to initiate formation of the elastic matrix, rather than a failure to maintain a preexisting matrix, phenotype of Wnt1Cre/Tgfbr2 mutant embryos, overview
-
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
on day 5, the signals for Lox mRNA and protein are detected in the subluminal stroma surrounding the implanting blastocyst at implantation sites while no signal is observed at interimplantation sites. From days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells. The expression of Lox is under the control of estrogen via the GSK-3beta/beta-catenin/c-myc pathway
the enzyme expression is not influenced by diurnal variations, but significantly by the gender, female mice show lower enzyme mRNA expression than male ones
-
the enzyme is highly up-regulated in metastatic breast cancer cells and tissues
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
on day 5, the signals for Lox mRNA and protein are detected in the subluminal stroma surrounding the implanting blastocyst at implantation sites while no signal is observed at interimplantation sites. From days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells. The expression of Lox is under the control of estrogen via the GSK-3beta/beta-catenin/c-myc pathway
on day 5, the signals for Lox mRNA and protein are detected in the subluminal stroma surrounding the implanting blastocyst at implantation sites while no signal is observed at interimplantation sites. From days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells. The expression of Lox is under the control of estrogen via the GSK-3beta/beta-catenin/c-myc pathway
-
-
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
synthesis
-
required for the normal biosynthesis and maturation of collagen and elastin
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
diagnostics
co-overexpression of SP1 and LOXL2 significantly correlates with poor prognosis in patients with pancreatic cancer
medicine
-
cutis laxa, indicated by hyperextensible skin with marked deficiency of skin elastic fibers, is caused by deficiency of lysyl oxidase expression. Fibrosis is a symptom of scleroderma, where lysyl oxidase is markedly elevated in affected tissues. Menkes syndrome may involve abnormalities in the expression of several genes coding for connective tissue proteins
medicine
-
increase in the expression of lysyl oxidase during wound healing in skin and in aorta, lung and skin of developing and aging rats. Implication of lysyl oxidase as a target gene for IRF-1 in tumor suppression. Lysly oxidase has unusual and important roles in cellular homeostasis
medicine
-
chronic inhalation of cadmium induces emphysema. Long-term Cd exposure induces inhibition of Cu-dependent lysyl oxidase and its substrates, by upregulation of Cu scavenging thiols in pulmonary fibroblasts. Downregulation of lysyl oxidase results from limitated Cu bioavailability as a central event contributing to Cd-induced extracellular matrix damage. Restoration of LO levels in Cd-insulted lung cells or tissues by replenishing Cu may have a protective or therapeutic effect on Cd-induced emphysema
medicine
-
treatment of rat dermal wound with lysyl oxidase-producing gene activated matrix leads to significantly enhanced mechanical strength of the wound site
medicine
-
genetic variation in the LOXL1 gene might play a role as a risk factor for spontaneous cervical artery dissection
medicine
-
LOX could play a key role in vascular homeostasis and, hence, it emerges as a new player in cardiovascular diseases
medicine
-
LOX is a potent metastasis-promoting gene in breast carcinomas that facilitates metastatic tumor progression by inducing cell motility and migration and has the potential for novel anti-metastatic cancer therapeutics
medicine
-
LOX is a potent metastasis-promoting gene in breast carcinomas that facilitates metastatic tumor progression by inducing cell motility and migration and has the potential for novel anti-metastatic cancer therapeutics
medicine
-
LOXL1 and LOXL4 are frequently hypermethylated and lose expression in primary bladder tumors
medicine
-
Loxl1 knockout mice have lower urinary tract dysfunction, most likely due to urethral dysfunction
medicine
-
LOXL2 can be used as a poor prognosis indicator in human squamous cell carcinomas promoting malignant transformation
medicine
-
LOXL2 may play an important role in susceptibility to intracranial aneurysm
medicine
-
lysyl oxidase like-1 protein knockout mice develop pelvic organ prolapse
medicine
LOX inhibition might be useful in metastasis prevention, metastasis model and drug administration study in mice, overview
medicine
an extracellular matrix (ECM)-targeting nanotherapeutic is engineered using a lipid-based nanoparticle chemically linked to an inhibitor of the ECM-related enzyme, lysyl oxidase 1 (LOX), that inhibits the crosslinking of elastin and collagen fibers. When the conjugated vesicles are loaded with the chemotherapeutic epirubicin, superior inhibition of triple negative breast cancer (TNBC) cell growth is observed both in vitro and in vivo
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