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Literature summary extracted from

  • Kagan, H.M.; Li, W.
    Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell (2003), J. Cell. Biochem., 88, 660-672.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.4.3.13 enzyme is resistant to high urea concentrations Homo sapiens
1.4.3.13 enzyme is resistant to high urea concentrations Rattus norvegicus
1.4.3.13 enzyme is resistant to high urea concentrations Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.13 additional information
-
 additional information kinetic mechanism Homo sapiens
1.4.3.13 additional information
-
 additional information kinetic mechanism Rattus norvegicus
1.4.3.13 additional information
-
 additional information kinetic mechanism Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.4.3.13 extracellular inactive proenzyme proLO is secreted Homo sapiens
-
-
1.4.3.13 extracellular inactive proenzyme proLO is secreted Bos taurus
-
-
1.4.3.13 extracellular inactive proenzyme proLO is secreted into the medium of cell culture Rattus norvegicus
-
-
1.4.3.13 Golgi apparatus passage of unprocessed proenzyme Homo sapiens 5794
-
1.4.3.13 Golgi apparatus passage of unprocessed proenzyme Rattus norvegicus 5794
-
1.4.3.13 Golgi apparatus passage of unprocessed proenzyme Bos taurus 5794
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.3.13 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 Homo sapiens
1.4.3.13 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 Rattus norvegicus
1.4.3.13 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 Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.13 28000
-
 x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE Homo sapiens
1.4.3.13 32000
-
 x * 32000, active enzyme, SDS-PAGE Bos taurus
1.4.3.13 32000
-
 x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE Rattus norvegicus
1.4.3.13 46000
-
 x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE Homo sapiens
1.4.3.13 50000
-
 x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.13 additional information Rattus norvegicus enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments ?
-
 ?
1.4.3.13 additional information Bos taurus enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments ?
-
 ?
1.4.3.13 additional information Homo sapiens 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 ?
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O Homo sapiens 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-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O Rattus norvegicus 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-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O Bos taurus 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-allysyl-peptide + NH3 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.13 Bos taurus
-
 4 isozymes
-
1.4.3.13 Homo sapiens
-
 lysyl oxidase LO and several lysyloxidase-like proteins LOXL1-4
-
1.4.3.13 Rattus norvegicus
-
 lysyl oxidase LO and several lysyloxidase-like proteins LOXL
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.4.3.13 glycoprotein 2 NRT-consensus sequences for N-glycosylation Homo sapiens
1.4.3.13 glycoprotein 2 NRT-consensus sequences for N-glycosylation Rattus norvegicus
1.4.3.13 glycoprotein 2 NRT-consensus sequences for N-glycosylation Bos taurus
1.4.3.13 proteolytic modification enzyme contains a catalysis-suppressing propeptide signal domain at the N-terminus Homo sapiens
1.4.3.13 proteolytic modification proenzyme proLO contains a catalysis-suppressing domain and an N-terminal signal peptide Bos taurus
1.4.3.13 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 Rattus norvegicus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.13 from aorta, to homogeneity, solubilization from connective tissue by 4-6 M urea Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.4.3.13 [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 Homo sapiens
a
1.4.3.13 [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 Rattus norvegicus
a
1.4.3.13 [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 Bos taurus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.13 aorta
-
 Bos taurus
-
1.4.3.13 connective tissue
-
 Homo sapiens
-
1.4.3.13 connective tissue
-
 Rattus norvegicus
-
1.4.3.13 connective tissue
-
 Bos taurus
-
1.4.3.13 fibroblast secretion of free soluble enzyme Homo sapiens
-
1.4.3.13 fibroblast secretion of free soluble enzyme Rattus norvegicus
-
1.4.3.13 fibroblast secretion of free soluble enzyme Bos taurus
-
1.4.3.13 heart
-
 Homo sapiens
-
1.4.3.13 kidney
-
 Homo sapiens
-
1.4.3.13 liver
-
 Homo sapiens
-
1.4.3.13 lung
-
 Homo sapiens
-
1.4.3.13 pancreas
-
 Homo sapiens
-
1.4.3.13 placenta
-
 Homo sapiens
-
1.4.3.13 skeletal muscle
-
 Homo sapiens
-
1.4.3.13 vascular smooth muscle
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.13 histone H1 + O2 + H2O L-lysine residues in histone H1 Homo sapiens ?
-
 ?
1.4.3.13 histone H1 + O2 + H2O L-lysine residues in histone H1 Rattus norvegicus ?
-
 ?
1.4.3.13 histone H1 + O2 + H2O L-lysine residues in histone H1 Bos taurus ?
-
 ?
1.4.3.13 additional information enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments Rattus norvegicus ?
-
 ?
1.4.3.13 additional information enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments Bos taurus ?
-
 ?
1.4.3.13 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 Homo sapiens ?
-
 ?
1.4.3.13 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 Homo sapiens ?
-
 ?
1.4.3.13 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 Rattus norvegicus ?
-
 ?
1.4.3.13 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 Bos taurus ?
-
 ?
1.4.3.13 n-alkylamine + O2 + H2O synthetic substrates Homo sapiens aldehyde + NH3 + H2O2
-
 ?
1.4.3.13 n-alkylamine + O2 + H2O synthetic substrates Rattus norvegicus aldehyde + NH3 + H2O2
-
 ?
1.4.3.13 n-alkylamine + O2 + H2O synthetic substrates Bos taurus aldehyde + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O 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 Homo sapiens peptidyl-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O 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 Rattus norvegicus peptidyl-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O 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 Bos taurus peptidyl-allysyl-peptide + NH3 + H2O2
-
 ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O in a variatey of basic globular proteins Homo sapiens peptidyl-allysyl-peptide + NH3 + H2O2 i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O in a variatey of basic globular proteins Rattus norvegicus peptidyl-allysyl-peptide + NH3 + H2O2 i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde ?
1.4.3.13 peptidyl-L-lysyl-peptide + O2 + H2O in a variety of basic globular proteins Bos taurus peptidyl-allysyl-peptide + NH3 + H2O2 i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde ?

Subunits

EC Number Subunits Comment Organism
1.4.3.13 ? x * 32000, active enzyme, SDS-PAGE Bos taurus
1.4.3.13 ? x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE Homo sapiens
1.4.3.13 ? x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE Rattus norvegicus
1.4.3.13 More structural implications of primary sequence, overview Bos taurus
1.4.3.13 More structural implications of primary sequence, profile of ionic residues in LO and LOXL-1, overview Homo sapiens
1.4.3.13 More structural implications of primary sequence, profile of ionic residues, overview Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
1.4.3.13 LO
-
 Homo sapiens
1.4.3.13 LO
-
 Rattus norvegicus
1.4.3.13 lysyl oxidase
-
 Homo sapiens
1.4.3.13 lysyl oxidase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.13 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 Bos taurus
1.4.3.13 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 Rattus norvegicus
1.4.3.13 lysyl-tyrosyl quinone essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, structure overview Homo sapiens