Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.4 In cyclic amidines
ID:3.5.4.24
Description:Sepiapterin deaminase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.4.24
BRENDA Enzyme Link: BRENDA 3.5.4.24
KEGG Enzyme Link: KEGG3.5.4.24
BioCyc Enzyme Link: BioCyc 3.5.4.24
ExPASy Enzyme Link: ExPASy3.5.4.24
EC2PDB Enzyme Link: EC2PDB 3.5.4.24
ExplorEnz Enzyme Link: ExplorEnz 3.5.4.24
PRIAM enzyme-specific profiles Link: PRIAM 3.5.4.24
IntEnz Enzyme Link: IntEnz 3.5.4.24
MEDLINE Enzyme Link: MEDLINE 3.5.4.24
MSA:

3.5.4.24;

Phylogenetic Tree:

3.5.4.24;

Uniprot:
M-CSA:
RHEA:14025 H(+) + H2O + sepiapterin = NH4(+) + xanthopterin-B2
RULE(radius=1) [*:1]:[c;H0;+0:2](-[NH2;+0:3]):[n;H0;+0:4]:[*:5].[H+;H0:6].[OH2;+0:7]>>[*:1]:[c;H0;+0:2](=[O;H0;+0:7]):[nH;+0:4]:[*:5].[NH3;+0:3]
Reaction
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References

TitleAuthorsDatePubMed ID
Studies on sepiapterin deaminase from the silkworm, Bombyx mori. Purification and some properties of the enzyme.Tsusué M1971 Apr5572808