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Literature summary extracted from

  • Zhang, C.M.; Perona, J.J.; Ryu, K.; Francklyn, C.; Hou, Y.M.
    Distinct kinetic mechanisms of the two classes of aminoacyl-tRNA synthetases (2006), J. Mol. Biol., 361, 300-311.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.1.1.7 additional information the class II enzyme does not show tight product binding and formation of ternary complexes with EF-Tu, it is not activated by EF-Tu Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.7 additional information
-
 additional information thermodynamics, pre-steady-state and single turnover kinetics, steady-state and transient kinetic analyses, recombinant His-tagged enzyme Escherichia coli
6.1.1.15 additional information
-
 additional information single turnover and burst kinetics, steady-state kinetics, recombinant His-tagged enzyme, overview Deinococcus radiodurans
6.1.1.16 additional information
-
 additional information thermodynamics, single turnover and burst kinetics of CysRS, steady-state and transient kinetic analyses of class I CysRS, the enzyme is rate-limited by release of aminoacyl-tRNA, recombinant His-tagged enzyme, overview Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.7 Mg2+
-
 Escherichia coli
6.1.1.15 Mg2+
-
 Deinococcus radiodurans
6.1.1.16 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.7 ATP + L-alanine + tRNAAla Escherichia coli
-
 AMP + diphosphate + L-alanyl-tRNAAla
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro Deinococcus radiodurans
-
 AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACys Escherichia coli
-
 AMP + diphosphate + L-cysteinyl-tRNACys
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.7 Escherichia coli
-
-
-
6.1.1.15 Deinococcus radiodurans
-
-
-
6.1.1.16 Escherichia coli P21888
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.7 ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla kinetic mechanism, AlaRS belongs to the class II of aminoacyl-tRNA ligases due to the position of aminoacylation on the 3'-terminal tRNA ribose, and the topology and tRNAbinding orientation of the active-site protein fold, class II synthetases are rate-limited by a step prior to aminoacyl transfer, the distinct mechanistic signatures of class I versus class II tRNA synthetases ensure rapid turnover of aminoacyl-tRNAs during protein synthesis Escherichia coli
a
6.1.1.15 ATP + L-proline + tRNAPro = AMP + diphosphate + L-prolyl-tRNAPro class II synthetases are limited by a step prior to aminoacyl transfer Deinococcus radiodurans
a
6.1.1.16 ATP + L-cysteine + tRNACys = AMP + diphosphate + L-cysteinyl-tRNACys the class I tRNA synthetase CysRS is rate-limited by release of aminoacyl-tRNA, class I synthetases share two signature motifs, HIGH and KMSKS, and build their active site by the ubiquitous Rossmann nucleotide-binding fold, the tight aminoacyl-tRNA product binding by class I enzymes correlates with the ability of EF-Tu to form a ternary complex with class I but not class II synthetases, and the further capacity of this protein to enhance the rate of aminoacylation by class I synthetases Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.7 ATP + L-alanine + tRNAAla
-
 Escherichia coli AMP + diphosphate + L-alanyl-tRNAAla
-
 ?
6.1.1.7 ATP + L-alanine + tRNAAla a two-step reaction, class II synthetases are rate-limited by a step prior to aminoacyl transfer Escherichia coli AMP + diphosphate + L-alanyl-tRNAAla
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro
-
 Deinococcus radiodurans AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.15 ATP + L-proline + tRNAPro a two-step reaction Deinococcus radiodurans AMP + diphosphate + L-prolyl-tRNAPro
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACys
-
 Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACys
-
 ?
6.1.1.16 ATP + L-cysteine + tRNACys the enzyme is rate-limited by release of aminoacyl-tRNA Escherichia coli AMP + diphosphate + L-cysteinyl-tRNACys
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.16 More the enzyme forms a class I ternary complex with EF-Tu, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.1.1.7 alanyl tRNA ligase
-
 Escherichia coli
6.1.1.7 More the enzyme belongs to the MurMN/Fem-ABX family of tRNA-dependent ligases Escherichia coli
6.1.1.7 MurM
-
 Escherichia coli
6.1.1.15 class II prolyl-tRNA synthetase
-
 Deinococcus radiodurans
6.1.1.15 class II ProRS
-
 Deinococcus radiodurans
6.1.1.15 Prolyl-tRNA synthetase
-
 Deinococcus radiodurans
6.1.1.15 ProRS
-
 Deinococcus radiodurans
6.1.1.16 class I CysRS
-
 Escherichia coli
6.1.1.16 class I cysteinyl-tRNA synthetase
-
 Escherichia coli
6.1.1.16 CysRS
-
 Escherichia coli
6.1.1.16 Cysteinyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.7 37
-
 assay at Escherichia coli
6.1.1.15 37
-
 assay at Deinococcus radiodurans
6.1.1.16 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.7 2
-
 tRNAAla
-
 Escherichia coli
6.1.1.15 1.8
-
 tRNAPro steady-state Deinococcus radiodurans
6.1.1.15 9.8
-
 tRNAPro single turnover overall aminoacylation Deinococcus radiodurans
6.1.1.15 10.8
-
 tRNAPro single turnover of the transfer step Deinococcus radiodurans
6.1.1.16 2.5
-
 L-cysteine steady-state Escherichia coli
6.1.1.16 2.9
-
 tRNACys steady-state Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.7 7.5
-
 assay at Escherichia coli
6.1.1.15 7.5
-
 assay at Deinococcus radiodurans
6.1.1.16 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.7 ATP
-
 Escherichia coli
6.1.1.15 ATP
-
 Deinococcus radiodurans
6.1.1.16 ATP
-
 Escherichia coli