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Literature summary for 1.4.3.13 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

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

KM Value [mM]

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments ?
-
?
additional information Bos taurus enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments ?
-
?
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 ?
-
?
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
-
?
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
-
?
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

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

Posttranslational Modification

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

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

Reaction

Reaction Comment Organism Reaction ID
[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
[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
[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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
histone H1 + O2 + H2O L-lysine residues in histone H1 Homo sapiens ?
-
?
histone H1 + O2 + H2O L-lysine residues in histone H1 Rattus norvegicus ?
-
?
histone H1 + O2 + H2O L-lysine residues in histone H1 Bos taurus ?
-
?
additional information enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments Rattus norvegicus ?
-
?
additional information enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments Bos taurus ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
n-alkylamine + O2 + H2O synthetic substrates Homo sapiens aldehyde + NH3 + H2O2
-
?
n-alkylamine + O2 + H2O synthetic substrates Rattus norvegicus aldehyde + NH3 + H2O2
-
?
n-alkylamine + O2 + H2O synthetic substrates Bos taurus aldehyde + NH3 + H2O2
-
?
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
-
?
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
-
?
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
-
?
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 ?
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 ?
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

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

Synonyms

Synonyms Comment Organism
LO
-
Homo sapiens
LO
-
Rattus norvegicus
lysyl oxidase
-
Homo sapiens
lysyl oxidase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
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
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
lysyl-tyrosyl quinone essential LTQ cofactor, a unique carbonyl cofactor forming an intramolecular covalent bond, structure overview Homo sapiens