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Literature summary for 2.8.1.7 extracted from

  • Zafrilla, B.; Martinez-Espinosa, R.M.; Esclapez, J.; Perez-Pomares, F.; Bonete, M.J.
    SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea (2010), Biochim. Biophys. Acta, 1804, 1476-1482.
    View publication on PubMed
Search for more literature for 2.8.1.7

Activating Compound

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(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Haloferax volcanii

Inhibitors

Inhibitors 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
L-cysteine above 0.5 mM Haloferax volcanii

Metals/Ions

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Haloferax volcanii D4GYV5
-
-
Haloferax volcanii DSM 3757 D4GYV5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-cysteine + acceptor overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules) Haloferax volcanii L-alanine + sulfide + ?
-
 ?
L-cysteine + acceptor overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules) Haloferax volcanii DSM 3757 L-alanine + sulfide + ?
-
 ?
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

Subunits Comment Organism
dimer 2 * 60200, SDS-PAGE Haloferax volcanii
dimer 2 * 46800, calculated from sequence Haloferax volcanii

Synonyms

Synonyms Comment Organism
SufS
-
 Haloferax volcanii

Temperature Optimum [°C]

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 between 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 between 70-75°C Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 maximal activity is obtained in 50 mM phosphate buffer, pH7.5, 2 M KCl at 65°C Haloferax volcanii

pH Range

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

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Haloferax volcanii

General Information

General Information Comment Organism
physiological function the enzyme is involved in Fe-S cluster assembly in haloarchaea Haloferax volcanii