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Literature summary for 6.1.1.7 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
Search for more literature for 6.1.1.7

Activating Compound

Activating Compound Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamics, pre-steady-state and single turnover kinetics, steady-state and transient kinetic analyses, recombinant His-tagged enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-alanine + tRNAAla Escherichia coli
-
 AMP + diphosphate + L-alanyl-tRNAAla
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAAla
-
 Escherichia coli AMP + diphosphate + L-alanyl-tRNAAla
-
 ?
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
-
 ?

Synonyms

Synonyms Comment Organism
alanyl tRNA ligase
-
 Escherichia coli
More the enzyme belongs to the MurMN/Fem-ABX family of tRNA-dependent ligases Escherichia coli
MurM
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2
-
 tRNAAla
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli