Leukotriene-A4 hydrolase
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ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| leukotriene A4 hydrolase | |||||||
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Chr. 12 q22 | |||||||
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Leukotriene-A4 hydrolase is an enzyme that catalyzes the reaction which converts Leukotriene A4 to Leukotriene B4.[1] It is a bifunctional zinc enzyme (EC 3.3.2.6) with different amino acids attached to it to aid in the catalysis of the reaction. It also acts as an aminopeptidase. Leukotriene-A4 hydrolase is a cytosolic protein and is found in almost all mammalian cells, tissues and organelles that have been examined.[1]
Function
This enzyme belongs to the family of
Catalyzed reaction
Leukotriene A4 Hydrolase catalyzes the reaction which converts leukotriene A4 to leukotriene B4. The Leukotriene A4 structure contains an epoxide ring functional group, which are highly reactive due to its ring strain making them extremely electrophilic. This drives the reaction forward, favouring the products Leukotriene B4. Leukotriene A4 hydrolase adds a water molecule across the epoxide ring on Leukotriene A4. The addition of the water molecule opens the epoxide ring and causes the formation of the Hydroxy group at the carbon attached to the oxygen from the epoxide. The second carbon involved in the epoxide ring remains the same resulting in leukotriene B4. The water molecule attacking the double bond also forms into a hydroxy group after work-up. The product of the reaction is Leukotriene B4.
Structure
As of late 2007, 4
References
- ^ a b "Leukotriene-A4 Hydrolase - an overview | ScienceDirect Topics". www.sciencedirect.com. Retrieved 2024-04-14.
Further reading
- Evans JF, Dupuis P, Ford-Hutchinson AW (1985). "Purification and characterisation of leukotriene A4 hydrolase from rat neutrophils". Biochim. Biophys. Acta. 840 (1): 43–50. PMID 3995081.
- Shimizu T, Seyama Y, Suzuki K (1987). "Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis". J. Biol. Chem. 262 (29): 13873–6. PMID 3654641.
- Haeggstrom J, Meijer J, Radmark O (1986). "Leukotriene A4. Enzymatic conversion into 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid by mouse liver cytosolic epoxide hydrolase". J. Biol. Chem. 261 (14): 6332–7. PMID 3009453.
- Newman JW, Morisseau C, Hammock BD (2005). "Epoxide hydrolases: their roles and interactions with lipid metabolism". Prog. Lipid Res. 44 (1): 1–51. PMID 15748653.
- Fretland AJ, Omiecinski CJ (2000). "Epoxide hydrolases: biochemistry and molecular biology" (PDF). Chem. Biol. Interact. 129 (1–2): 41–59. PMID 11154734.
- Orning L, Gierse JK, Fitzpatrick FA (1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity". J. Biol. Chem. 269 (15): 11269–73. PMID 8157657.
- Ohishi N, Izumi T, Minami M, Kitamura S, Seyama Y, Ohkawa S, Terao S, Yotsumoto H, Takaku F, Shimizu T (1987). "Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers". J. Biol. Chem. 262 (21): 10200–5. PMID 3038871.
External links
- leukotriene A4 hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)