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Literature summary for 6.1.1.20 extracted from

  • Bobkova, E.V.; Volfson, A.D.; Ankilova, V.N.; Lavrik, O.I.
    Separation and comparative characteristics of subunits of phenylalanyl-tRNA synthetase from Escherichia coli MRE-600 and Thermus thermophilus HB8 (1990), Biokhimiia, 55, 525-533.
    View publication on PubMed
Search for more literature for 6.1.1.20

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Escherichia coli MRE 600
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Thermus thermophilus
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-phenylalanine + tRNAPhe
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 Thermus thermophilus AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-phenylalanine + tRNAPhe
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 Escherichia coli AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-phenylalanine + tRNAPhe
-
 Escherichia coli MRE 600 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?
ATP + L-phenylalanine + tRNAPhe
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-phenylalanyl-tRNAPhe
-
 ?

Subunits

Subunits Comment Organism
More the separated subunits do not possess any detectable tRNA-amino-acylation activity Thermus thermophilus
More the separated subunits do not possess any detectable tRNA-amino-acylation activity Escherichia coli
More beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers Escherichia coli
More both alpha- and beta-subunits mainly exist in the dimeric form Thermus thermophilus