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Literature summary extracted from

  • Wan, L.C.K.; Mao, D.Y.L.; Neculai, D.; Strecker, J.; Chiovitti, D.; Kurinov, I.; Poda, G.; Thevakumaran, N.; Yuan, F.; Szilard, R.K.; Lissina, E.; Nislow, C.; Caudy, A.A.; Durocher, D.; Sicheri, F.
    Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system (2013), Nucleic Acids Res., 41, 6332-6346.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.234
-
 Saccharomyces cerevisiae
2.7.7.87 full length Sua5 expressed in Escherichia coli BL21 (DE3) CodonPlus cells harboring an N-terminal hexa-histidine tag Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.234 2.9 A crystal structure of isoform Qri7 reveals a simple homodimer arrangement that is supplanted by the heterodimerization of YgjD with protein YeaZ Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.87 0.00011
-
 L-threonine pH 8.0, temperature not specified in the publication Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.234 Saccharomyces cerevisiae P36132 isoform Kae1
-
2.3.1.234 Saccharomyces cerevisiae P43122 isoform Qri7
-
2.7.7.87 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.87 Ni-NTA affinity chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.234 L-threonylcarbamoyladenylate + adenine37 in tRNA
-
 Saccharomyces cerevisiae AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
 ?
2.3.1.234 L-threonylcarbamoyladenylate + adenine37 in tRNA
-
 Saccharomyces cerevisiae AMP + N6-L-threonylcarbamoyladenine37 in tRNA isoform Qri7 and protein Sua5 are sufficient for N6-threonylcarbamoyladenosine biosynthesis in vitro ?
2.7.7.87 L-threonine + ATP + bicarbonate the combination of Qri7 and Sua5 is necessary and sufficient for L-threonylcarbamoyladenylate biosynthesis Saccharomyces cerevisiae L-threonylcarbamoyladenylate + diphosphate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.234 Kae1
-
 Saccharomyces cerevisiae
2.3.1.234 Qri7
-
 Saccharomyces cerevisiae
2.3.1.234 t(6)A synthase
-
 Saccharomyces cerevisiae
2.3.1.234 t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1
-
 Saccharomyces cerevisiae
2.7.7.87 SUA5
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.3.1.234 physiological function isoform Kae1 is part of a larger macromolecular assembly called KEOPS with Kae1, Bud32, Cgi121, Gon7 and Pcc1 subunits. Kae1 provides a core essential function that other subunits within KEOPS have evolved to support. Isoform Qri7 complements isoform Kae1 function and complements the function of all subunits Saccharomyces cerevisiae
2.3.1.234 physiological function isoform Qri7 complements isoform Kae1 function and complements the function of all subunits of a larger macromolecular assembly called KEOPS with Kae1, Bud32, Cgi121, Gon7 and Pcc1 subunits, in growth, N6-threonylcarbamoyladenosine biosynthesis and, to a partial degree, telomeremaintenance. Qri7 alone is sufficient for N6-threonylcarbamoyladenosine biosynthesis with protein Sua5 in vitro Saccharomyces cerevisiae
2.7.7.87 physiological function the eukaryotic L-threonylcarbamoyladenylate biosynthesis system functions first through Sua5, which generates threonylcarbamoyl-adenylate using its adenylation function and then secondly through Qri7, which binds to threonylcarbamoyl-adenylate to conjugate the threonyl-carbamoyl moiety onto directly bound tRNA substrates Saccharomyces cerevisiae