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Literature summary for 2.5.1.73 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
Search for more literature for 2.5.1.73

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherchia coli Methanocaldococcus jannaschii

Protein Variants

Protein Variants Comment Organism
C113A activity similar to wild-type Methanocaldococcus jannaschii
C209A activity similar to wild-type Methanocaldococcus jannaschii
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
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
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
K234A complete loss of activtiy Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q59072
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-
Methanocaldococcus jannaschii DSM 2661 Q59072
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
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
-
 ?
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

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

General Information

General Information Comment Organism
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