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Literature summary for 4.2.1.20 extracted from

  • Nagao, R.T.; Moore, T.C.
    Partial purification and properties of tryptophan synthase of pea plants (1972), Arch. Biochem. Biophys., 149, 402-443.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 1-(indol-3-yl)glycerol 3-phosphate
-
 Pisum sativum
0.05
-
 indole cosubstrate L-Ser Pisum sativum
5.7
-
 L-Ser cosubstrate indole Pisum sativum

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
bud terminal, of young plants Pisum sativum
-
seedling activity highest in shoot tips, less activity in young leaves and internodes, activity declines with maturation Pisum sativum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10.53
-
-
 Pisum sativum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(indol-3-yl)glycerol 3-phosphate + L-serine
-
 Pisum sativum L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
 ?
indole + D-glyceraldehyde 3-phosphate r Pisum sativum indole-3-glycerol phosphate r ?
indole + L-serine
-
 Pisum sativum L-tryptophan + H2O
-
 ?
indole-3-glycerol phosphate r Pisum sativum indole + D-glyceraldehyde 3-phosphate r ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 optimum for the reactions: 1. indole-3-glycerol phosphate + L-Ser, 2. indole + L-Ser Pisum sativum