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Literature summary for 6.1.1.20 extracted from

  • Shiraki, K.; Tsuji, M.; Hashimoto, Y.; Fujimoto, K.; Fujiwara, S.; Takagi, M.; Imanaka, T.
    Genetic, enzymatic, and structural analyses of phenylalanyl-tRNA synthetase from Thermococcus kodakaraensis KOD1 (2003), J. Biochem., 134, 567-574.
    View publication on PubMed
Search for more literature for 6.1.1.20

Cloned(Commentary)

Cloned (Comment) Organism
genes encoding alpha- and beta-subunit, DNA and amino acid sequence determination and analysis, expression of alpha-subunit and of beta-subunit in Escherichia coli Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57600
-
 x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination Thermococcus kodakarensis
66200
-
 x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe Thermococcus kodakarensis
-
 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
additional information Thermococcus kodakarensis phylogenetic analysis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q76KA8 and Q76KA8 KOD1, class II enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha- and beta-subunit both expressed in Escherichia coli Thermococcus kodakarensis

Reaction

Reaction Comment Organism Reaction ID
ATP + L-phenylalanine + tRNAPhe = AMP + diphosphate + L-phenylalanyl-tRNAPhe Phe391 in motif 2 and Arg472 in motif 3 bind to the adenosine moiety of tRNAPhe, Arg379 in motif 2 and Arg463 in motif 3 restrain the conformation with the triphosphate that interacts with the ribosyl hydroxyl and gamma-phosphate, Asp395 in motif 2 is unique and binds to phenylalanine to assure proper positioning of the substrate Thermococcus kodakarensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe
-
 Thermococcus kodakarensis AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
additional information phylogenetic analysis Thermococcus kodakarensis ?
-
 ?

Subunits

Subunits Comment Organism
? x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
CML33
-
 Thermococcus kodakarensis
FRS
-
 Thermococcus kodakarensis
HSPC173
-
 Thermococcus kodakarensis
L-Phenylalanyl-tRNA synthetase
-
 Thermococcus kodakarensis
Phenylalanine translase
-
 Thermococcus kodakarensis
Phenylalanine--tRNA ligase
-
 Thermococcus kodakarensis
Phenylalanine-tRNA synthetase
-
 Thermococcus kodakarensis
Phenylalanyl transfer ribonucleic acid synthetase
-
 Thermococcus kodakarensis
Phenylalanyl-transfer ribonucleate synthetase
-
 Thermococcus kodakarensis
Phenylalanyl-transfer RNA ligase
-
 Thermococcus kodakarensis
Phenylalanyl-transfer RNA synthetase
-
 Thermococcus kodakarensis
Phenylalanyl-tRNA ligase
-
 Thermococcus kodakarensis
Phenylalanyl-tRNA synthetase
-
 Thermococcus kodakarensis
PheRS
-
 Thermococcus kodakarensis
Synthetase, phenylalanyl-transfer ribonucleate
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
 Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
98
-
 enzyme retains its tertiary structure Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Thermococcus kodakarensis

pI Value

Organism Comment pI Value Maximum pI Value
Thermococcus kodakarensis beta-subunit 4.7 4.6
Thermococcus kodakarensis alpha-subunit
-
 9.4