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Literature summary extracted from

  • Wogulis, M.; Chew, E.R.; Donohoue, P.D.; Wilson, D.K.
    Identification of formyl kynurenine formamidase and kynurenine aminotransferase from Saccharomyces cerevisiae using crystallographic, bioinformatic and biochemical evidence (2008), Biochemistry, 47, 1608-1621.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.9 expressed in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.7 diffraction to 2.0 A resolution, comparison with crystallization data from Aspergillus fumigatus, Dictyostelium discoideum, Aedes aegypti, Trypanosoma brucei, Rattus norvegicus, and Homo sapiens Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.9 0.18
-
N-formyl-L-kynurenine
-
Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.7 Saccharomyces cerevisiae P47039 isoform Bna3 is not an formyl kynurenine formamidase, but kynurenine aminotransferase
-
3.5.1.9 Saccharomyces cerevisiae Q04066
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.9
-
Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.9 N-formyl-L-kynurenine + H2O
-
Saccharomyces cerevisiae L-kynurenine + formate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.7 Bna3
-
Saccharomyces cerevisiae
3.5.1.9 Bna7p
-
Saccharomyces cerevisiae
3.5.1.9 FKF
-
Saccharomyces cerevisiae
3.5.1.9 formyl kynurenine formamidase
-
Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.9 161
-
N-formyl-L-kynurenine
-
Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
3.5.1.9 pyridoxal 5'-phosphate dependent Saccharomyces cerevisiae