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Literature summary for 1.8.3.2 extracted from
- Human augmenter of liver regeneration probing the catalytic mechanism of a flavin-dependent sulfhydryl oxidase (2013), Biochemistry, 52, 8323-8332 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E143K/E144K | site-directed mutagenesis, substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| DTT | rapid reaction studies show that dithiothreitol generates a transient mixed disulfide intermediate with sfALR signaled by a weak charge-transfer interaction between the thiolate of C145 and the oxidized flavin, reducing the transfer of reducing equivalents and reoxidation of the reduced flavin by molecular oxygen | Homo sapiens |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | pre-steady state kinetics and stopped-flow measurements of sfALR using DTT to slow down the reaction velocity | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Homo sapiens | 5829 | - |
| extracellular | - |
Homo sapiens | - |
- |
| nucleus | - |
Homo sapiens | 5634 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 R'C(R)SH + O2 | Homo sapiens | the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide | R'C(R)S-S(R)CR' + H2O2 | - |
? | |
| additional information | Homo sapiens | nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 | catalytic mechanism model using DTT and O2, overview. Stabilization of mixed disulfide intermediates in enzyme sfALR | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 R'C(R)SH + O2 | the enzyme catalyze the oxidation of thiol substrates with the reduction of molecular oxygen to hydrogen peroxide | Homo sapiens | R'C(R)S-S(R)CR' + H2O2 | - |
? | |
| additional information | nuclear sfALR interacts with the Jun activation-domain binding protein (JAB1) mediating the interaction between ALR and activator protein-1 (AP-1) via the phosphorylation of c-Jun | Homo sapiens | ? | - |
? | |
| additional information | catalytic mechanism of the short, cytokine, form of augmenter of liver regeneration (sfALR) using model thiol substrates of the enzyme. While 2-mercaptoethanol is a very poor substrate of enzyme sfALR, it rapidly generates a mixed disulfide intermediate allowing the thiolate of C145 to form a strong charge-transfer complex with the flavin. Glutathione is unable to form charge-transfer complexes and is no substrate of the oxidase | Homo sapiens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| augmenter of liver regeneration | - |
Homo sapiens |
| flavin-dependent sulfhydryl oxidase | - |
Homo sapiens |
| sfALR | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | at a diminutive FAD binding domain, the isoalloxazine ring of the flavin prosthetic group is bound at the mouth of a 4-helix bundle in each subunit with a 5th small helix adjacent to the adenine moiety of FAD. A proximal redox-active disulfide is located adjacent to the C4a position of the isoalloxazine ring | Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | augmenter of liver regeneration is a member of the ERV family of small flavin-dependent sulfhydryl oxidases that contain a redox-active CxxC disulfide bond in redox communication with the isoalloxazine ring of bound FAD | Homo sapiens |
| malfunction | substitution of the intervening E143 and E144 dipeptide by the charge-reversed KK dipeptide shows minimal effect on the redox potential | Homo sapiens |
| additional information | E143 and E144 are active site residues in the CxxC motif | Homo sapiens |
| physiological function | the inability of the relatively bulky glutathione to attain the in-line geometry required for efficient disulfide exchange in sfALR may be physiologically important in preventing the oxidase from catalyzing the potentially harmful oxidation of intracellular glutathione. sfALR protects against hydrogen peroxide and radiation-induced apoptosis | Homo sapiens |
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Release 2023.1 (January 2023)
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