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Literature summary for 6.1.1.20 extracted from

  • Roy, H.; Ibba, M.
    Phenylalanyl-tRNA synthetase contains a dispensable RNA-binding domain that contributes to the editing of noncognate aminoacyl-tRNA (2006), Biochemistry, 45, 9156-9162.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
complementatiom of a growth mutant defective in phenylalanylation in vivo by wild-type full-length PheRS from Saccharomyces cerevisiae, the full-length Escherichia coli enzyme A294G, and the truncated mutant PheRSDELTAB2, overexpression of full-length mutant A294G and truncated mutant PheRSDELTAB2A294G in strain XL-1 Blue Escherichia coli

Protein Variants

Protein Variants Comment Organism
A294G thermosensitive active site mutant strain NP37 enzyme Escherichia coli
additional information construction of a truncated mutant PheRSDELTAB2A294G, lacking the B2 domain, which shows kinetics for in vitro aminoacylation comparable to the wild-type enzyme, a 2-fold drop compared to full-length PheRS in the catalytic efficiency of Tyr-tRNAPhe hydrolysis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information full-length PheRSA294G and truncated mutant PheRSDELTAB2A294G show comparable kinetics for in vitro aminoacylation, kinetics, overview Escherichia coli
0.0022
-
tRNAPhe pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae Escherichia coli
0.0025
-
tRNAPhe pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli Escherichia coli
0.0027
-
tRNAPhe pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli Escherichia coli
0.0041
-
tRNAPhe pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae Escherichia coli
0.0049
-
L-phenylalanine pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G Escherichia coli
0.0053
-
L-phenylalanine pH 7.2, 37°C, full-length PheRSA294G 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-phenylalanine + tRNAPhe Escherichia coli the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe Escherichia coli NP37 the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
carrying the thermosensitive point mutation A294G in the active site
-
Escherichia coli NP37
-
carrying the thermosensitive point mutation A294G in the active site
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis Escherichia coli NP37 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?
ATP + L-phenylalanine + tRNAPhe a two-step reaction, tRNAPhe substrate from Escherichia coli and Saccharomyces cerevisiae, the enzyme contains the dispensable B2 RNA-binding domain that contributes to the post-transfer editing of noncognate aminoacyl-tRNA, the B2 domain does not enhance tRNA folding, overview Escherichia coli NP37 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
?

Subunits

Subunits Comment Organism
oligomer PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe Escherichia coli

Synonyms

Synonyms Comment Organism
Phenylalanyl-tRNA synthetase
-
Escherichia coli
PheRS
-
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
0.077
-
tRNAPhe pH 7.2, 37°C, full-length PheRSA294G, substrate from Saccharomyces cerevisiae Escherichia coli
0.11
-
tRNAPhe pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Saccharomyces cerevisiae Escherichia coli
0.78
-
tRNAPhe pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G, substrate from Escherichia coli Escherichia coli
0.82
-
tRNAPhe pH 7.2, 37°C, full-length PheRSA294G, substrate from Escherichia coli Escherichia coli
3.27
-
L-phenylalanine pH 7.2, 37°C, truncated mutant PheRSDELTAB2A294G Escherichia coli
3.34
-
L-phenylalanine pH 7.2, 37°C, full-length PheRSA294G Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli