Any feedback?
Literature summary extracted from
- Flavoprotein oxygenases (1974), Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, , 245-283.
No PubMed abstract available
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.6 | m-cresol | increases activity | Pseudomonas fluorescens |  |
| 1.14.13.6 | m-cresol | increases activity | Pseudomonas putida | |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.13.5 | - |
Pseudomonas sp. |
| 1.14.13.6 | - |
Pseudomonas putida |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 1.13.12.1 | dithionite and thioglycolate protect against inactivation by O2 | Streptomyces griseus |
| 1.13.12.1 | L-arginine protects against inactivation by O2 | Streptomyces griseus |
| 1.13.12.1 | storage in N2-atmosphere protects against inactivation by O2 | Streptomyces griseus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.12.1 | diethyldicarbonate | modifies one histidyl residue per flavin | Streptomyces griseus | |
| 1.13.12.1 | homoarginine | competitive to L-arginine | Streptomyces griseus | |
| 1.13.12.2 | SDS | - |
Pseudomonas fluorescens | |
| 1.13.12.2 | sulfhydryl inhibitors | - |
Pseudomonas fluorescens | |
| 1.13.12.4 | phosphate | competitive inhibitor | Mycolicibacterium smegmatis | |
| 1.14.13.5 | p-chloromercuribenzoate | - |
Pseudomonas sp. | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.4 | 0.0013 | - |
melilotate | overview | Pseudomonas sp. | |
| 1.14.13.4 | 0.0047 | - |
NADH | overview | Pseudomonas sp. | |
| 1.14.13.4 | 0.05 | - |
O2 | overview | Pseudomonas sp. | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.12.2 | additional information | metals play no role in lysine monooxygenase | Pseudomonas fluorescens |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.2 | 191000 | - |
sedimentation velocity experiments | Pseudomonas fluorescens |
| 1.13.12.4 | 300000 | - |
sucrose density gradient centrifugation | Mycolicibacterium smegmatis |
| 1.13.12.4 | 341000 | - |
sedimentation velocity data | Mycolicibacterium smegmatis |
| 1.14.13.4 | 65000 | - |
- |
Arthrobacter sp. |
| 1.14.13.4 | 238000 | 250000 | - |
Pseudomonas sp. |
| 1.14.13.5 | 87000 | 90000 | sedimentation equilibrium, gel filtration | Pseudomonas sp. |
| 1.14.13.6 | 60000 | 70000 | gel filtration | Pseudomonas putida |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.12.4 | (S)-lactate + O2 | Mycolicibacterium smegmatis | - |
acetate + CO2 + H2O | - |
? | |
| 1.13.12.4 | (S)-lactate + O2 | Mycolicibacterium phlei | - |
acetate + CO2 + H2O | - |
? | |
| 1.14.13.5 | 4-imidazoleacetate + NADH + O2 | Pseudomonas sp. | the enzyme is part of the histidine catabolic pathway in which imidazaloneacetate is converted to aspartic acid by way of formiminoaspartic acid | 5-hydroxy-4-imidazoleacetate + NAD+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.12.1 | Streptomyces griseus | - |
- |
- |
| 1.13.12.2 | Pseudomonas fluorescens | - |
- |
- |
| 1.13.12.4 | Mycolicibacterium phlei | - |
- |
- |
| 1.13.12.4 | Mycolicibacterium smegmatis | - |
- |
- |
| 1.14.13.4 | Arthrobacter sp. | - |
- |
- |
| 1.14.13.4 | Pseudomonas sp. | - |
- |
- |
| 1.14.13.5 | Pseudomonas sp. | - |
- |
- |
| 1.14.13.6 | Pseudomonas fluorescens | - |
- |
- |
| 1.14.13.6 | Pseudomonas putida | - |
01 | - |
| 1.14.13.6 | Pseudomonas putida 1 | - |
01 | - |
Oxidation Stability
| EC Number | Oxidation Stability | Organism |
|---|---|---|
| 1.13.12.1 | partially purified enzyme extremely unstable in presence of O2 | Streptomyces griseus |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.13.4 | 3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O | mechanism | Pseudomonas sp. | |
| 1.14.13.4 | 3-(2-hydroxyphenyl)propanoate + NADH + H+ + O2 = 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O | mechanism | Arthrobacter sp. |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.13.12.1 | mycelium | - |
Streptomyces griseus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.12.1 | canavanine + O2 | i.e. 2-amino-4-(guanidinooxy)butyrate, poor substrate | Streptomyces griseus | 3-guanidoxypropionamide + CO2 + H2O | - |
? | |
| 1.13.12.1 | homoarginine + O2 | - |
Streptomyces griseus | 5-guanidinovaleramide + CO2 + H2O | - |
? | |
| 1.13.12.1 | L-arginine + O2 | - |
Streptomyces griseus | 4-guanidinobutanamide + CO2 + H2O | - |
? | |
| 1.13.12.1 | additional information | no activity with L-lysine | Streptomyces griseus | ? | - |
? | |
| 1.13.12.2 | L-lysine + O2 | monooxygenase activity | Pseudomonas fluorescens | 5-aminopentanamide + CO2 + H2O | - |
? | |
| 1.13.12.2 | L-lysine + O2 | oxidase activity | Pseudomonas fluorescens | 2-keto-6-amino-n-hexanoate + NH3 + H2O2 | - |
? | |
| 1.13.12.4 | (S)-lactate + O2 | - |
Mycolicibacterium smegmatis | acetate + CO2 + H2O | - |
? | |
| 1.13.12.4 | (S)-lactate + O2 | - |
Mycolicibacterium phlei | acetate + CO2 + H2O | - |
? | |
| 1.14.13.4 | 3-(2-hydroxyphenyl)propanoate + NADH + O2 | - |
Pseudomonas sp. | 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O | - |
? | |
| 1.14.13.4 | 3-(2-hydroxyphenyl)propanoate + NADH + O2 | - |
Arthrobacter sp. | 3-(2,3-dihydroxyphenyl)propanoate + NAD+ + H2O | - |
? | |
| 1.14.13.5 | 4-imidazoleacetate + NAD(P)H + O2 + H+ | - |
Pseudomonas sp. | 5-hydroxy-4-imidazoleacetate + NAD(P)+ + H2O | - |
? | |
| 1.14.13.5 | 4-imidazoleacetate + NADH + O2 | the enzyme is part of the histidine catabolic pathway in which imidazaloneacetate is converted to aspartic acid by way of formiminoaspartic acid | Pseudomonas sp. | 5-hydroxy-4-imidazoleacetate + NAD+ + H2O | - |
? | |
| 1.14.13.6 | 3-cresol + NADH + O2 | nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated | Pseudomonas fluorescens | 3-methylcatechol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | 3-cresol + NADH + O2 | nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated | Pseudomonas putida | 3-methylcatechol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | 3-cresol + NADH + O2 | nonsubstrate effector, which increases NADH oxidase activity without being hydroxylated | Pseudomonas putida 1 | 3-methylcatechol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | orcinol + NADH + O2 | highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol | Pseudomonas fluorescens | 2,3,5-trihydroxytoluene + NAD+ + H2O | - |
? | |
| 1.14.13.6 | orcinol + NADH + O2 | highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol | Pseudomonas putida | 2,3,5-trihydroxytoluene + NAD+ + H2O | - |
? | |
| 1.14.13.6 | orcinol + NADH + O2 | highly specific for orcinol, i.e. 5-methyl-1,3-benzenediol | Pseudomonas putida 1 | 2,3,5-trihydroxytoluene + NAD+ + H2O | - |
? | |
| 1.14.13.6 | resorcinol + NADH + O2 | hydroxylated to a limited extent | Pseudomonas fluorescens | hydroxyquinol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | resorcinol + NADH + O2 | hydroxylated to a limited extent | Pseudomonas putida | hydroxyquinol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | resorcinol + NADH + O2 | behaves both as a substrate and a nonsubstrate effector | Pseudomonas fluorescens | hydroxyquinol + NAD+ + H2O | - |
? | |
| 1.14.13.6 | resorcinol + NADH + O2 | hydroxylated to a limited extent | Pseudomonas putida 1 | hydroxyquinol + NAD+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.4 | tetramer | - |
Pseudomonas sp. |
| 1.14.13.6 | monomer | 1 * 60000-70000 | Pseudomonas putida |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.1 | 6.1 | - |
canavanine | Streptomyces griseus |
| 1.13.12.1 | 8 | - |
homoarginine | Streptomyces griseus |
| 1.13.12.1 | 9 | - |
L-arginine | Streptomyces griseus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.12.1 | flavin | flavoprotein | Streptomyces griseus | |
| 1.13.12.2 | FAD | flavoprotein | Pseudomonas fluorescens | |
| 1.13.12.2 | FAD | FAD cannot be replaced by FMN or riboflavin | Pseudomonas fluorescens | |
| 1.14.13.4 | FAD | flavoprotein | Pseudomonas sp. | |
| 1.14.13.4 | FAD | flavoprotein | Arthrobacter sp. | |
| 1.14.13.4 | FAD | FAD: prosthetic group | Pseudomonas sp. | |
| 1.14.13.4 | FAD | FAD: prosthetic group | Arthrobacter sp. | |
| 1.14.13.4 | NADH | - |
Pseudomonas sp. | |
| 1.14.13.4 | NADH | - |
Arthrobacter sp. | |
| 1.14.13.5 | FAD | 1 mol per mol enzyme | Pseudomonas sp. | |
| 1.14.13.5 | FAD | FAD is the only prosthetic group | Pseudomonas sp. | |
| 1.14.13.5 | NADH | - |
Pseudomonas sp. | |
| 1.14.13.5 | NADPH | less efficient than NADH | Pseudomonas sp. | |
| 1.14.13.6 | 3-Acetyl pyridine nucleotide | reduced | Pseudomonas fluorescens | |
| 1.14.13.6 | 3-Acetyl pyridine nucleotide | reduced | Pseudomonas putida | |
| 1.14.13.6 | FAD | flavoprotein | Pseudomonas fluorescens | |
| 1.14.13.6 | FAD | flavoprotein | Pseudomonas putida | |
| 1.14.13.6 | FAD | 1 mol of FAD per mol of protein | Pseudomonas putida | |
| 1.14.13.6 | NADH | the best donor | Pseudomonas fluorescens | |
| 1.14.13.6 | NADH | the best donor | Pseudomonas putida | |
| 1.14.13.6 | NADPH | - |
Pseudomonas fluorescens | |
| 1.14.13.6 | NADPH | - |
Pseudomonas putida | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
