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Literature summary for 4.2.1.20 extracted from

  • Leopoldseder, S.; Hettwer, S.; Sterner, R.
    Evolution of multi-enzyme complexes: the case of tryptophan synthase (2006), Biochemistry, 45, 14111-14119.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25500
-
2 * 25500 + 2 * 41750, gel filtration Saccharolobus solfataricus
41750
-
2 * 25500 + 2 * 41750, gel filtration Saccharolobus solfataricus
134500
-
gel filtration Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
heterotetramer 2 * 25500 + 2 * 41750, gel filtration Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
tryptophan synthase subunit TrpA catalyzes the reversible cleavage of indole-3-glycerol phosphate (IGP1) into glyceraldehyde-3-phosphate and indole, the indole migrates through a hydrophobic channel to an active site of an attached TrpB1 subunit, where it condenses with L-serine in a pyridoxal phosphate dependent irreversible reaction to form L-tryptophan Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent Saccharolobus solfataricus