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Literature summary extracted from

  • Ehrmann, A.; Richter, K.; Busch, F.; Reimann, J.; Albers, S.V.; Sterner, R.
    Ligand-induced formation of a transient tryptophan synthase complex with alphabetabeta subunit stoichiometry (2010), Biochemistry, 49, 10842-10853.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.20 genes trpA and trpB2i, expression of wild-type alpha- and beta-subunits, sTrpA and sTrpB2i, and of TrpA mutants in Escherichia coli strain Bl21(DE3) Saccharolobus solfataricus

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.20 S206C site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA Saccharolobus solfataricus
4.2.1.20 S229C site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA Saccharolobus solfataricus
4.2.1.20 W65F site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA Saccharolobus solfataricus
4.2.1.20 W88F site-directed mutagenesis of subunit sTrpA, complex formation with subunit TrpB2i compared to wild-type TrpA Saccharolobus solfataricus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.20 107800 116500 different TrpA-TrpB2i complexes, gel filtration Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate Saccharolobus solfataricus
-
 L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
 ?
4.2.1.20 additional information Saccharolobus solfataricus catalyzed reaction and structure of the tryptophan synthase complex, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Saccharolobus solfataricus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O catalyzed reaction and structure of the tryptophan synthase complex, mechanism, overview. Model of the catalytic cycle of the transient enzyme complex, overview Saccharolobus solfataricus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
 Saccharolobus solfataricus L-tryptophan + glyceraldehyde 3-phosphate + H2O
-
 ?
4.2.1.20 additional information catalyzed reaction and structure of the tryptophan synthase complex, overview Saccharolobus solfataricus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.20 More the hyperthermophilic archaeon Sulfolobus solfataricus does not contain a TrpB1 protein, as other prototypical tryptophan synthases, but instead two members of the phylogenetically distinct family of TrpB2 proteins, which are encoded within, sTrpB2i, and outside, sTrpB2a, the tryptophan operon. sTrpB2a does not functionally or structurally interact with sTrpA, whereas sTrpB2i substantially activates sTrpA in a unidirectional manner. In the absence of catalysis, no physical complex between sTrpB2i and sTrpA is detected. Stoichiometry of the complex is 1 subunit of sTrpA per 2 subunits of sTrpB2i, which corresponds to a alphabetabeta quaternary structure and testifies to a strong negative cooperativity for the binding of the alpha-monomers to the betabeta-dimer. The alphabetabeta complex remains stable during the whole catalytic cycle and disintegrates into alpha- and betabeta-subunits upon the release of the reaction product tryptophan, structure-function relationship, overview Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
4.2.1.20 evolution the family of trpB2 genes, identified in the genomes of several microorganisms and plants, can be further divided into the trpB2i, located within the tryptophan operon, and the trpB2o/trpB2a, located outside the operon, subfamilies. The deduced amino acid sequence identities within and between the TrpB1 andTrpB2 families are about 60% and 30%, respectively Saccharolobus solfataricus
4.2.1.20 additional information the alphabetabeta complex remains stable during the whole catalytic cycle and disintegrates into alpha- and betabeta-subunits upon the release of the reaction product tryptophan, structure-function relationship, overview. The formation of a transient tryptophan synthase complex, together with the observed low affinity of sTrpB2i for L-serine, couples the rate of tryptophan biosynthesis in Sulfolobus solfataricus to the cytosolic availability of L-serine Saccharolobus solfataricus