| Aliphatic aldoxime dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.99.1.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an aliphatic aldoxime dehydratase ( EC 4.99.1.5) is an enzyme that catalyzes the chemical reaction
- an aliphatic aldoxime an aliphatic nitrile + H2O
This dehydratase converts an aldoxime on an aliphatic substrate to a nitrile as the product structure with water as byproduct.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming). Other names in common use include OxdA, and aliphatic aldoxime hydro-lyase.
- D-amino acid oxidase, sometimes also referred to as OXDA
- Kobayashi M; Hashimoto, Y; Konishi, K; Goda, M; Noguchi, T; Higashibata, H; Kobayashi, M (2003). "Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization". J. Biol. Chem. 278 (32): 29600–8. doi: 10.1074/jbc.M211832200. PMID 12773527.
- Xie SX, Kato Y, Komeda H, Yoshida S, Asano Y (2003). "A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4". Biochemistry. 42 (41): 12056–66. CiteSeerX 10.1.1.513.2481. doi: 10.1021/bi035092u. PMID 14556637.
- Kato Y, Yoshida S, Xie SX, Asano Y (2004). "Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771". J. Biosci. Bioeng. 97 (4): 250–9. doi: 10.1016/S1389-1723(04)70200-5. PMID 16233624.
| Aliphatic aldoxime dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.99.1.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an aliphatic aldoxime dehydratase ( EC 4.99.1.5) is an enzyme that catalyzes the chemical reaction
- an aliphatic aldoxime an aliphatic nitrile + H2O
This dehydratase converts an aldoxime on an aliphatic substrate to a nitrile as the product structure with water as byproduct.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is aliphatic aldoxime hydro-lyase (aliphatic-nitrile-forming). Other names in common use include OxdA, and aliphatic aldoxime hydro-lyase.
- D-amino acid oxidase, sometimes also referred to as OXDA
- Kobayashi M; Hashimoto, Y; Konishi, K; Goda, M; Noguchi, T; Higashibata, H; Kobayashi, M (2003). "Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization". J. Biol. Chem. 278 (32): 29600–8. doi: 10.1074/jbc.M211832200. PMID 12773527.
- Xie SX, Kato Y, Komeda H, Yoshida S, Asano Y (2003). "A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4". Biochemistry. 42 (41): 12056–66. CiteSeerX 10.1.1.513.2481. doi: 10.1021/bi035092u. PMID 14556637.
- Kato Y, Yoshida S, Xie SX, Asano Y (2004). "Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771". J. Biosci. Bioeng. 97 (4): 250–9. doi: 10.1016/S1389-1723(04)70200-5. PMID 16233624.