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Literature summary extracted from

  • Mihara, H.; Esaki, N.
    Bacterial cysteine desulfurases: their function and mechanisms (2002), Appl. Microbiol. Biotechnol., 60, 12-23.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.1.7 mitochondrial matrix
-
 Mus musculus 5759
-
2.8.1.7 mitochondrial matrix
-
 Homo sapiens 5759
-
2.8.1.7 mitochondrial matrix
-
 Saccharomyces cerevisiae 5759
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.1.6 FeCl3 binds 1 [Fe4-S4] cluster per monomer Escherichia coli
2.8.1.6 FeCl3 sulfur of the iron-sulfur cluster is provided by cysteine desulfurase EC 2.8.1.7 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.1.6 76000
-
 dimeric form Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.7 L-cysteine + [enzyme]-cysteine Escherichia coli
-
 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine Azotobacter vinelandii
-
 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine Synechocystis sp.
-
 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine Synechocystis sp. PCC6714
-
 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 additional information Saccharomyces cerevisiae
-
 ?
-
 ?
2.8.1.7 additional information Azotobacter vinelandii enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro ?
-
 ?
2.8.1.7 additional information Haemophilus influenzae isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins ?
-
 ?
2.8.1.7 additional information Escherichia coli isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins ?
-
 ?
2.8.1.7 additional information Pseudomonas aeruginosa isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins ?
-
 ?
2.8.1.7 additional information Escherichia coli enzyme is involved in selenoprotein biosynthesis ?
-
 ?
2.8.1.7 additional information Azotobacter vinelandii enzyme is involved in selenoprotein biosynthesis ?
-
 ?
2.8.1.7 additional information Escherichia coli involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.6 Escherichia coli
-
-
-
2.8.1.7 Azotobacter vinelandii
-
-
-
2.8.1.7 Escherichia coli
-
-
-
2.8.1.7 Haemophilus influenzae
-
-
-
2.8.1.7 Homo sapiens
-
-
-
2.8.1.7 Mus musculus
-
-
-
2.8.1.7 Pseudomonas aeruginosa
-
-
-
2.8.1.7 Saccharomyces cerevisiae
-
-
-
2.8.1.7 Synechocystis sp.
-
 PCC6714
-
2.8.1.7 Synechocystis sp. PCC6714
-
 PCC6714
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.1.7 L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor mechanism Escherichia coli
a
2.8.1.7 L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor mechanism Azotobacter vinelandii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.6 dethiobiotin + sulfur
-
 Escherichia coli biotin
-
 ?
2.8.1.7 L-cysteine unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site Synechocystis sp. L-alanine + sulfide
-
 ?
2.8.1.7 L-cysteine unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site Synechocystis sp. PCC6714 L-alanine + sulfide
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine
-
 Escherichia coli L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine
-
 Azotobacter vinelandii L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine
-
 Synechocystis sp. L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue Azotobacter vinelandii L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase Escherichia coli L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-cysteine + [enzyme]-cysteine
-
 Synechocystis sp. PCC6714 L-alanine + [enzyme]-S-sulfanylcysteine
-
 ?
2.8.1.7 L-selenocysteine
-
 Escherichia coli L-alanine + selenium
-
 ?
2.8.1.7 L-selenocysteine
-
 Azotobacter vinelandii L-alanine + selenium
-
 ?
2.8.1.7 L-selenocysteine
-
 Synechocystis sp. L-alanine + selenium
-
 ?
2.8.1.7 L-selenocysteine
-
 Synechocystis sp. PCC6714 L-alanine + selenium
-
 ?
2.8.1.7 additional information
-
 Saccharomyces cerevisiae ?
-
 ?
2.8.1.7 additional information enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro Azotobacter vinelandii ?
-
 ?
2.8.1.7 additional information isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins Haemophilus influenzae ?
-
 ?
2.8.1.7 additional information isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins Escherichia coli ?
-
 ?
2.8.1.7 additional information isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins Pseudomonas aeruginosa ?
-
 ?
2.8.1.7 additional information enzyme is involved in selenoprotein biosynthesis Escherichia coli ?
-
 ?
2.8.1.7 additional information enzyme is involved in selenoprotein biosynthesis Azotobacter vinelandii ?
-
 ?
2.8.1.7 additional information involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.8.1.6 dimer homodimer Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.1.7 pyridoxal 5'-phosphate
-
 Escherichia coli
2.8.1.7 pyridoxal 5'-phosphate
-
 Azotobacter vinelandii