(Redirected from
Naad)
| 3-Fumarylpyruvate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.7.1.20 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
3-Fumarylpyruvate hydrolase ( EC 3.7.1.20, nagK (gene), naaD (gene)) is an enzyme with systematic name 3-fumarylpyruvate hydrolyase. [1] [2] This enzyme catalyses the following chemical reaction
- 3-fumarylpyruvate + H2O fumarate + pyruvate
The enzyme is involved in bacterial degradation of 5-substituted salicylates.
References
- ^ Zhou NY, Fuenmayor SL, Williams PA (January 2001). "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism". Journal of Bacteriology. 183 (2): 700–8. doi: 10.1128/JB.183.2.700-708.2001. PMC 94927. PMID 11133965.
- ^ Qu Y, Spain JC (June 2011). "Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329". Journal of Bacteriology. 193 (12): 3057–63. doi: 10.1128/JB.01188-10. PMC 3133195. PMID 21498645.
External links
- 3-fumarylpyruvate+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
Naad)
| 3-Fumarylpyruvate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.7.1.20 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
3-Fumarylpyruvate hydrolase ( EC 3.7.1.20, nagK (gene), naaD (gene)) is an enzyme with systematic name 3-fumarylpyruvate hydrolyase. [1] [2] This enzyme catalyses the following chemical reaction
- 3-fumarylpyruvate + H2O fumarate + pyruvate
The enzyme is involved in bacterial degradation of 5-substituted salicylates.
References
- ^ Zhou NY, Fuenmayor SL, Williams PA (January 2001). "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism". Journal of Bacteriology. 183 (2): 700–8. doi: 10.1128/JB.183.2.700-708.2001. PMC 94927. PMID 11133965.
- ^ Qu Y, Spain JC (June 2011). "Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329". Journal of Bacteriology. 193 (12): 3057–63. doi: 10.1128/JB.01188-10. PMC 3133195. PMID 21498645.
External links
- 3-fumarylpyruvate+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)