Activating Compound | Comment | Organism | Structure |
---|---|---|---|
dithiothreitol | activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect | Haloferax volcanii |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Haloferax volcanii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
DTT | activity is strongly dependent on the presence of DTT, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect | Haloferax volcanii | |
L-cysteine | above 0.5 mM | Haloferax volcanii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.97 | - |
L-selenocysteine | pH 7.5, 65°C | Haloferax volcanii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | 0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C | Haloferax volcanii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
46800 | - |
2 * 46800, calculated from sequence | Haloferax volcanii |
60200 | - |
2 * 60200, SDS-PAGE | Haloferax volcanii |
110000 | - |
gel filtration | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Haloferax volcanii | the enzyme is involved in Fe-S cluster assembly in haloarchaea | ? | - |
? | |
additional information | Haloferax volcanii DSM 3757 | the enzyme is involved in Fe-S cluster assembly in haloarchaea | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GYV5 | - |
- |
Haloferax volcanii DSM 3757 | D4GYV5 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Haloferax volcanii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-selenocysteine + reduced acceptor | the enzyme also shows cysteine desulfurase activity, that is 280fold lower than its selenocysteine lyase activity | Haloferax volcanii | L-alanine + selenium + acceptor | - |
? | |
L-selenocysteine + reduced acceptor | the enzyme also shows cysteine desulfurase activity, that is 280fold lower than its selenocysteine lyase activity | Haloferax volcanii DSM 3757 | L-alanine + selenium + acceptor | - |
? | |
additional information | the enzyme is involved in Fe-S cluster assembly in haloarchaea | Haloferax volcanii | ? | - |
? | |
additional information | the enzyme is involved in Fe-S cluster assembly in haloarchaea | Haloferax volcanii DSM 3757 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 60200, SDS-PAGE | Haloferax volcanii |
dimer | 2 * 46800, calculated from sequence | Haloferax volcanii |
Synonyms | Comment | Organism |
---|---|---|
SufS | - |
Haloferax volcanii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | 60 | 0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to 70-75°C | Haloferax volcanii |
65 | - |
assay at | Haloferax volcanii |
70 | 75 | 0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to 70-75°C | Haloferax volcanii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
maximal activity is obtained in 50 mM phosphate buffer, pH 7.5, 2 M KCl at 65°C | Haloferax volcanii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 10 | pH 6.5: about 45% of maximal activity, pH 10.0: about 45% of maximal activity | Haloferax volcanii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in Fe-S cluster assembly in haloarchaea | Haloferax volcanii |