Literature summary extracted from
Fujisawa, D.; Yamazaki, Y.; Morita, T.
Re-evaluation of M-LAO, L-amino acid oxidase, from the venom of Gloydius blomhoffi as an anticoagulant protein (2009), J. Biochem., 146, 43-49.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.4.3.2 |
m-chlorobenzoate |
LAO inhibitor, does not inhibit the degradation of fibrinogen |
Gloydius blomhoffii |
|
1.4.3.2 |
o-aminobenzoic acid |
LAO inhibitor, slightly inhibiting the degradation of fibrinogen |
Gloydius blomhoffii |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.4.3.2 |
60000 |
- |
x * 60000, SDS-PAGE |
Gloydius blomhoffii |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.4.3.2 |
additional information |
Gloydius blomhoffii |
the LAO-containing fraction inhibits coagulation factor IX, and it prolongs the APTT, PT and fibrinogen clotting time and cleaves the Aalpha-chain of fibrinogen probably due to the presence of traces of a metalloproteinase in the fraction, overview. The mechanism for the anticoagulant activity of M-LAO fraction is not due to binding to factor IX. The fibrinogenolytic activity of the M-LAO fraction is independent of either LAO enzymatic activity or generated hydrogen peroxide |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.4.3.2 |
Gloydius blomhoffii |
Q90W54 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
1.4.3.2 |
flavoprotein |
- |
Gloydius blomhoffii |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.4.3.2 |
native enzyme by gel filtration, cation and anion exchange chromatography, and hydroxyapatite chromatography |
Gloydius blomhoffii |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.4.3.2 |
DL-norleucine + H2O + O2 |
- |
Gloydius blomhoffii |
2-oxocaproate + NH3 + H2O2 |
- |
? |
|
1.4.3.2 |
additional information |
the LAO-containing fraction inhibits coagulation factor IX, and it prolongs the APTT, PT and fibrinogen clotting time and cleaves the Aalpha-chain of fibrinogen probably due to the presence of traces of a metalloproteinase in the fraction, overview. The mechanism for the anticoagulant activity of M-LAO fraction is not due to binding to factor IX. The fibrinogenolytic activity of the M-LAO fraction is independent of either LAO enzymatic activity or generated hydrogen peroxide |
Gloydius blomhoffii |
? |
- |
? |
|
1.4.3.2 |
additional information |
L-amino acid oxidase is a dimeric glycosylated flavoenzyme that catalyses the oxidative deamination of an L-amino acid substrate to a 2-oxo acid along with the production of ammonia and hydrogen peroxide |
Gloydius blomhoffii |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.4.3.2 |
? |
x * 60000, SDS-PAGE |
Gloydius blomhoffii |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.4.3.2 |
M-LAO |
- |
Gloydius blomhoffii |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.4.3.2 |
37 |
- |
assay at |
Gloydius blomhoffii |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.4.3.2 |
7.4 |
- |
assay at |
Gloydius blomhoffii |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.4.3.2 |
flavin |
LAO is a flavoenzyme |
Gloydius blomhoffii |
|