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Literature summary for 6.1.1.23 extracted from

  • Feng, L.; Yuan, J.; Toogood, H.; Tumbula-Hansen, D.; Soll, D.
    Aspartyl-tRNA synthetase requires a conserved proline in the anticodon-binding loop for tRNA(Asn) recognition in vivo (2005), J. Biol. Chem., 280, 20638-20641.
    View publication on PubMed
Search for more literature for 6.1.1.23

Protein Variants

Protein Variants Comment Organism
H28Q wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation H28Q leads to a reverse tRNA preference Deinococcus radiodurans
H77K/H28Q wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K/H28Q leads to a reverse tRNA preference Deinococcus radiodurans
P77K wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp. Mutation P77K leads to a reverse tRNA preference and a 3fold increase in specificity for tRNAASp over tRNAAsn Deinococcus radiodurans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0008
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme P77K Deinococcus radiodurans
0.0008
-
 tRNAAsp 37°C, pH 7.0, wild-type enzyme Deinococcus radiodurans
0.0013
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme P77K/H28Q Deinococcus radiodurans
0.0018
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme H28Q Deinococcus radiodurans
0.002
-
 tRNAAsn 37°C, pH 7.0, wild-type enzym Deinococcus radiodurans
0.0035
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme P77K/H28Q Deinococcus radiodurans
0.0038
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme P77K Deinococcus radiodurans
0.0045
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme H28Q Deinococcus radiodurans

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsn aspartyl-tRNA synthetase requires a conserved proline, P77, in the anticodon-binding loop for tRNA(Asn) recognition in vivo. Wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp Deinococcus radiodurans AMP + diphosphate + L-aspartyl-tRNAAsn
-
 ?
ATP + L-aspartate + tRNAAsp aspartyl-tRNA synthetase requires a conserved proline, P77, in the anticodon-binding loop for tRNA(Asn) recognition in vivo. Wild-type enzyme shows a slight preference to tRNAAsn over tRNAAsp Deinococcus radiodurans AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.14
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme P77K/H28Q Deinococcus radiodurans
0.15
-
 tRNAAsp 37°C, pH 7.0, wild-type enzyme Deinococcus radiodurans
0.17
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme H28Q Deinococcus radiodurans
0.22
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme H28Q Deinococcus radiodurans
0.22
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme P77K/H28Q Deinococcus radiodurans
0.28
-
 tRNAAsp 37°C, pH 7.0, mutant enzyme P77K Deinococcus radiodurans
0.51
-
 tRNAAsn 37°C, pH 7.0, wild-type enzym Deinococcus radiodurans
0.6
-
 tRNAAsn 37°C, pH 7.0, mutant enzyme P77K Deinococcus radiodurans