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Literature summary extracted from

  • Liu, Y.; Dos Santos, P.C.; Zhu, X.; Orlando, R.; Dean, D.R.; Soell, D.; Yuan, J.
    Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide (2012), J. Biol. Chem., 287, 5426-5433.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.73 expression in Escherchia coli Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.73 C113A activity similar to wild-type Methanocaldococcus jannaschii
2.5.1.73 C209A activity similar to wild-type Methanocaldococcus jannaschii
2.5.1.73 C272A loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation Methanocaldococcus jannaschii
2.5.1.73 C64A loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation Methanocaldococcus jannaschii
2.5.1.73 C67A loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation Methanocaldococcus jannaschii
2.5.1.73 K234A complete loss of activtiy Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.73 Methanocaldococcus jannaschii Q59072
-
-
2.5.1.73 Methanocaldococcus jannaschii DSM 2661 Q59072
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.73
-
 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.73 additional information the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates Methanocaldococcus jannaschii ?
-
 ?
2.5.1.73 additional information the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates Methanocaldococcus jannaschii DSM 2661 ?
-
 ?
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis Methanocaldococcus jannaschii L-cysteinyl-tRNACys + phosphate
-
 ?
2.5.1.73 O-phospho-L-seryl-tRNACys + sulfide all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis Methanocaldococcus jannaschii DSM 2661 L-cysteinyl-tRNACys + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.73 MJ1678
-
 Methanocaldococcus jannaschii
2.5.1.73 Sep-tRNA:Cys-tRNA synthase
-
 Methanocaldococcus jannaschii
2.5.1.73 SepCysS
-
 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
2.5.1.73 physiological function wild-type enzyme can complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation Methanocaldococcus jannaschii