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Literature summary for 6.1.1.11 extracted from

  • Boeker, E.A.; Hays, A.P.; Cantoni, G.L.
    Seryl transfer ribonucleic acid synthetase of Escherichia coli B. Purification, subunit structure, and behavior in the acylation reaction (1973), Biochemistry, 12, 2379-2383.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
diphosphate
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
2 * 53000, SDS-PAGE Escherichia coli
103000
-
meniscus depletion method Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
B
-
Escherichia coli B / ATCC 11303
-
B
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
Escherichia coli AMP + diphosphate + L-seryl-tRNASer
-
?
ATP + L-serine + tRNASer
-
Escherichia coli B / ATCC 11303 AMP + diphosphate + L-seryl-tRNASer
-
?

Subunits

Subunits Comment Organism
dimer 2 * 53000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
Escherichia coli