Enzyme

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EC Tree
     3. Hydrolases
        3.7 Acting on carbon-carbon bonds
            3.7.1 In ketonic substances
ID:3.7.1.2
Description:Fumarylacetoacetase.
Alternative Name: Fumarylacetoacetate hydrolase.
Beta-diketonase.
Cath: 3.90.850.10; 2.30.30.230;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.7.1.2
BRENDA Enzyme Link: BRENDA 3.7.1.2
KEGG Enzyme Link: KEGG3.7.1.2
BioCyc Enzyme Link: BioCyc 3.7.1.2
ExPASy Enzyme Link: ExPASy3.7.1.2
EC2PDB Enzyme Link: EC2PDB 3.7.1.2
ExplorEnz Enzyme Link: ExplorEnz 3.7.1.2
PRIAM enzyme-specific profiles Link: PRIAM 3.7.1.2
IntEnz Enzyme Link: IntEnz 3.7.1.2
MEDLINE Enzyme Link: MEDLINE 3.7.1.2
MSA:

3.7.1.2;

Phylogenetic Tree:

3.7.1.2;

Uniprot:
M-CSA:
RHEA:10244 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[CH2;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity.Labelle Y, Phaneuf D, Leclerc B, Tanguay RM1993 Jul8364576
Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal models for the human genetic disorder hereditary tyrosinemia type 1.Aponte JL, Sega GA, Hauser LJ, Dhar MS, Withrow CM, Carpenter DA, Rinchik EM, Culiat CT, Johnson DK2001 Jan 1611209059
Mechanistic inferences from the crystal structure of fumarylacetoacetate hydrolase with a bound phosphorus-based inhibitor.Bateman RL, Bhanumoorthy P, Witte JF, McClard RW, Grompe M, Timm DE2001 May 411154690
Crystal structure and mechanism of a carbon-carbon bond hydrolase.Timm DE, Mueller HA, Bhanumoorthy P, Harp JM, Bunick GJ1999 Sep 1510508789