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Literature summary for 1.13.11.52 extracted from

  • Yuasa, H.; Sugiura, M.; Harumoto, T.
    A single amino acid residue regulates the substrate affinity and specificity of indoleamine 2,3-dioxygenase (2018), Arch. Biochem. Biophys., 640, 1-9 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in the Escherichia coli KRX strain Blepharisma stoltei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.589
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei
0.622
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme N127T Blepharisma stoltei
2.85
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme H127E Blepharisma stoltei
13.6
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + O2 Blepharisma stoltei
-
N-formyl-L-kynurenine
-
?

Organism

Organism UniProt Comment Textmining
Blepharisma stoltei
-
-
-
Blepharisma stoltei A0A286T905
-
-
Blepharisma stoltei A0A286TA52
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Blepharisma stoltei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + O2
-
Blepharisma stoltei N-formyl-L-kynurenine
-
?
L-tryptophan + O2 Glu132 in Blepharisma IDO-III is crucial for its high affinity for L-Trp. No activity with 5-hydroxy-L-tryptophan Blepharisma stoltei N-formyl-L-kynurenine
-
?
L-tryptophan + O2 no activity with 5-hydroxy-L-tryptophan Blepharisma stoltei N-formyl-L-kynurenine
-
?

Synonyms

Synonyms Comment Organism
IDO-I
-
Blepharisma stoltei
IDO-II
-
Blepharisma stoltei
IDO-III
-
Blepharisma stoltei
IDO-IV
-
Blepharisma stoltei

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.62
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme H127E Blepharisma stoltei
1.47
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei
3.9
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme N127T Blepharisma stoltei
6.03
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme E132H Blepharisma stoltei
6.5
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei

Cofactor

Cofactor Comment Organism Structure
heme heme-containing enzyme Blepharisma stoltei

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.108
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei
0.98
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme E132H Blepharisma stoltei
6.3
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme N127T Blepharisma stoltei
11
-
L-tryptophan pH 8.0, temperature not specified in the publication, wild-type enzyme Blepharisma stoltei
215
-
L-tryptophan pH 8.0, temperature not specified in the publication, mutant enzyme H127E Blepharisma stoltei