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Literature summary for 4.2.1.20 extracted from

  • Zitzewitz, J.A.; Matthews, C.R.
    Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein (1999), Biochemistry, 38, 10205-10214.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination of the alpha-subunit of the enzyme, overexpression of the alpha-subunit and the larger N-terminal part of the alpha-subunit, amino acid residues 1-188, in inclusion bodies Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha-subunit and N-terminal part of the alpha-subunit of the enzyme, to over 95% purity Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8) Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
cooperative unfolding and 2-phase refolding mechanism and kinetics of the alpha-subunit and the N-terminas of the alpha-subunit alone, denaturing by urea at 25°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(indol-3-yl)glycerol 3-phosphate alpha-subunit of the bienzyme complex, alpha-reaction Escherichia coli D-glyceraldehyde 3-phosphate + indole
-
?
L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Escherichia coli L-tryptophan + H2O
-
?

Subunits

Subunits Comment Organism
More molecular dissection of the alpha-subunit Escherichia coli

Synonyms

Synonyms Comment Organism
alphaTS
-
Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
thermodynamic stability of alpha-subunit and N-terminal part of the alpha-subunit during folding and unfolding Escherichia coli