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Literature summary for 2.8.1.15 extracted from

  • Chen, M.; Asai, S.; Narai, S.; Nambu, S.; Omura, N.; Sakaguchi, Y.; Suzuki, T.; Ikeda-Saito, M.; Watanabe, K.; Yao, M.; Shigi, N.; Tanaka, Y.
    Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA (2017), Proc. Natl. Acad. Sci. USA, 114, 4954-4959.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the TtuA-TtuB complex, at a resolution of 2.5 A, showing the S transfer of TtuB to tRNA using its C-terminal thiocarboxylate group. The active site of TtuA is connected to the outside by two channels, one occupied by TtuB and the other used for tRNA binding Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 3.84 mol per mol of enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O Thermus thermophilus
-
AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly
-
?
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O Thermus thermophilus DSM 7039
-
AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q72LF3
-
-
Thermus thermophilus DSM 7039 Q72LF3
-
-

Oxidation Stability

Oxidation Stability Organism
TtuA is an oxygen-labile iron-sulfur protein Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O
-
Thermus thermophilus AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly
-
?
ATP + [TtuB sulfur-carrier protein]-Gly-NH-CH2-C(O)SH + 5-methyuracil54 in tRNA + H2O
-
Thermus thermophilus DSM 7039 AMP + diphosphate + 5-methyl-2-thiouracil54 in tRNA + [TtuB sulfur-carrier protein]-Gly-Gly
-
?

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center TtuA requires oxygen-labile [4Fe-4S]-type iron (Fe)-S clusters for its enzymatic activity. The [4Fe-4S] cluster is coordinated by three highly conserved cysteine residues, and one of the Fe atoms is exposed to the active site. The cluster is coordinated by conserved residues Cys130, Cys133, and Cys222 Thermus thermophilus