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Literature summary for 2.6.1.27 extracted from

  • O'Neil, S.R.; DeMoss, R.D.
    Tryptophan transaminase from Clostridium sporogenes (1968), Arch. Biochem. Biophys., 127, 361-369.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information high salt concentrations activate Clostridium sporogenes
additional information no activation by: pyridoxine, pyridoxal, pyridoxamine Clostridium sporogenes

General Stability

General Stability Organism
low buffer concentrations: loss of activity Clostridium sporogenes
unstable upon freezing and thawing Clostridium sporogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.158
-
2-oxoglutarate cosubstrate phenylalanine , pH 8.4, 22°C approximately Clostridium sporogenes
2.68
-
L-tryptophan cosubstrate tryptophan, pH 8.4, 22°C approximately Clostridium sporogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
97000
-
sucrose density gradient centrifugation Clostridium sporogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + 2-oxoglutarate Clostridium sporogenes first step in metabolic path for the conversion of L-tryptophan to indolepropionate L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tryptophan + 2-oxoglutarate Clostridium sporogenes 175 first step in metabolic path for the conversion of L-tryptophan to indolepropionate L-glutamate + 3-indole-2-oxopropanoate
-
?

Organism

Organism UniProt Comment Textmining
Clostridium sporogenes
-
-
-
Clostridium sporogenes 175
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial, 200fold Clostridium sporogenes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
23.6
-
partially purified enzyme Clostridium sporogenes

Storage Stability

Storage Stability Organism
0°C, partially purified enzyme, stable for at least 48 h Clostridium sporogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 2-oxoglutarate
-
Clostridium sporogenes L-glutamate + phenylpyruvate
-
?
L-phenylalanine + 2-oxoglutarate
-
Clostridium sporogenes 175 L-glutamate + phenylpyruvate
-
?
L-tryptophan + 2-oxoglutarate
-
Clostridium sporogenes L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tryptophan + 2-oxoglutarate first step in metabolic path for the conversion of L-tryptophan to indolepropionate Clostridium sporogenes L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tryptophan + 2-oxoglutarate
-
Clostridium sporogenes 175 L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tryptophan + 2-oxoglutarate first step in metabolic path for the conversion of L-tryptophan to indolepropionate Clostridium sporogenes 175 L-glutamate + 3-indole-2-oxopropanoate
-
?
L-tyrosine + 2-oxoglutarate
-
Clostridium sporogenes L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
?
L-tyrosine + 2-oxoglutarate
-
Clostridium sporogenes 175 L-glutamate + 3-(4-hydroxyphenyl)-2-oxopropanoate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Clostridium sporogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
Clostridium sporogenes

pH Range

pH Minimum pH Maximum Comment Organism
7 9.3 pH 7.0: about 55% of activity maximum, pH 9.3: about 60% of activity maximum Clostridium sporogenes

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate Km: 0.00218 mM Clostridium sporogenes
pyridoxal 5'-phosphate required for full activation Clostridium sporogenes
pyridoxamine 5'-phosphate activates Clostridium sporogenes