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Literature summary for 3.5.4.24 extracted from

  • Sawada, H.; Kanekatsu, M.; Nakagoshi, M.; Dohke, K.; Iino, T.; Takikawa, S.I.
    Purification and characterization of sepiapterin deaminase from the silkworm, Bombyx mori (1998), Pteridines, 9, 18-21.
No PubMed abstract available
Search for more literature for 3.5.4.24

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 gel filtration Bombyx mori
74000
-
 SDS-PAGE Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bombyx mori

Source Tissue

Source Tissue Comment Organism Textmining
integument larval integument, mutant lemon Bombyx mori
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
178.8
-
-
 Bombyx mori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
isosepiapterin + H2O less effectively deaminated Bombyx mori ?
-
 ?
additional information 7-hydroxybiopterin, L-erythro-neopterin, L-threo-neopterin, D-erythro-neopterin, D-threo-neopterin, L-erythro-biopterin, L-threo-biopterin, D-erythro-biopterin, dihydroneopterin, dihydrobiopterin and tetrahydrobiopterin are no substrates Bombyx mori ?
-
 ?
sepiapterin + H2O
-
 Bombyx mori xanthopterin-B2 + NH3 sepialumazine ?

Subunits

Subunits Comment Organism
monomer 1 * 74000, SDS-PAGE Bombyx mori