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Literature summary for 4.2.1.20 extracted from

  • Buller, A.; Van Roye, P.; Murciano-Calles, J.; Arnold, F.
    tryptophan synthase uses an atypical mechanism to achieve substrate specificity (2016), Biochemistry, 55, 7043-7046 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.20

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 1-C-(indol-3-yl)glycerol 3-phosphate cosubstrate L-serine, pH 8.0, temperature not specified in the publication Pyrococcus furiosus
0.6
-
 L-serine pH 8.0, temperature not specified in the publication Pyrococcus furiosus
1.3
-
 L-threonine pH 8.0, temperature not specified in the publication Pyrococcus furiosus
1.4
-
 1-C-(indol-3-yl)glycerol 3-phosphate cosubstrate L-threonine, pH 8.0, temperature not specified in the publication Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U093
-
-
Pyrococcus furiosus ATCC 43587 Q8U093
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
 Pyrococcus furiosus L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
 Pyrococcus furiosus ATCC 43587 L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
 Pyrococcus furiosus (2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
L-threonine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
 Pyrococcus furiosus ATCC 43587 (2S,3S)-beta-methyltryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
additional information native tryptophan synthase can also catalyze a productive reaction with L-threonine, leading to (2S,3S)-beta-methyltryptophan. Substitution occurs in vitro with a 3.4fold higher catalytic efficiency for Ser over Thr using saturating indole. Threonine binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle Pyrococcus furiosus ?
-
 ?
additional information native tryptophan synthase can also catalyze a productive reaction with L-threonine, leading to (2S,3S)-beta-methyltryptophan. Substitution occurs in vitro with a 3.4fold higher catalytic efficiency for Ser over Thr using saturating indole. Threonine binds efficiently but decreases the affinity for indole and disrupts the allosteric signaling that regulates the catalytic cycle Pyrococcus furiosus ATCC 43587 ?
-
 ?

Synonyms

Synonyms Comment Organism
TrpB1 beta subunit Pyrococcus furiosus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.61
-
 L-threonine pH 8.0, temperature not specified in the publication Pyrococcus furiosus
1
-
 L-serine pH 8.0, temperature not specified in the publication Pyrococcus furiosus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.46
-
 1-C-(indol-3-yl)glycerol 3-phosphate cosubstrate L-threonine, pH 8.0, temperature not specified in the publication Pyrococcus furiosus
0.47
-
 L-threonine pH 8.0, temperature not specified in the publication Pyrococcus furiosus
1.6
-
 L-serine pH 8.0, temperature not specified in the publication Pyrococcus furiosus
50
-
 1-C-(indol-3-yl)glycerol 3-phosphate cosubstrate L-serine, pH 8.0, temperature not specified in the publication Pyrococcus furiosus