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Literature summary for 4.2.1.20 extracted from

  • Rocha, V.; Brennan, E.F.
    Purification and partial characterization of the B subunit of Serratia marcescens tryptophan synthetase (1978), J. Bacteriol., 134, 950-957.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE Serratia marcescens
89000
-
89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
B subunit Serratia marcescens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.05
-
-
Serratia marcescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + L-serine
-
Serratia marcescens L-tryptophan + H2O
-
?

Subunits

Subunits Comment Organism
? 89000, B2 subunit, polyacrylamide gel electrophoresis, 2 * 43000, B subunit, SDS-PAGE Serratia marcescens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Serratia marcescens