Leukotriene-A4 hydrolase
| leukotriene-A4 hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.3.2.6 | ||||||||
| CAS no. | 90119-07-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| leukotriene A4 hydrolase | |||||||
|---|---|---|---|---|---|---|---|
 Crystallographic structure of LTA4H (rainbow colored N-terminus = blue, C-terminus = red) complexed with the protease inhibitor bestatin (space-filling model, carbon = white, oxygen = red, nitrogen = blue) based on the PDB: 1HS6 structure. | |||||||
| Identifiers | |||||||
| Symbol | LTA4H | ||||||
| NCBI gene | 4048 | ||||||
| HGNC | 6710 | ||||||
| OMIM | 151570 | ||||||
| PDB | 1SQM | ||||||
| RefSeq | NM_000895 | ||||||
| UniProt | P09960 | ||||||
| Other data | |||||||
| EC number | 3.3.2.6 | ||||||
| Locus | Chr. 12 q22 | ||||||
| |||||||
Leukotriene A4 hydrolase, also known as LTA4H is a human gene.[1][2][3] The protein encoded by this gene is a bifunctional enzyme (EC 3.3.2.6) which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.[4]
Function[]
This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate hydrolase. Other names in common use include LTA4 hydrolase, LTA4H, and leukotriene A4 hydrolase. This enzyme participates in arachidonic acid metabolism.
Catalyzed reaction[]
The chemical reaction catalyzed by LTA4H.
Structure[]
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1GW6, 1H19, 1HS6, and 1SQM.
References[]
- ^ Minami M, Ohno S, Kawasaki H, Rådmark O, Samuelsson B, Jörnvall H, Shimizu T, Seyama Y, Suzuki K (October 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. doi:10.1016/S0021-9258(18)47872-6. PMID 3654641.
- ^ FFunk CD, Rådmark O, Fu JY, Matsumoto T, Jörnvall H, Shimizu T, Samuelsson B (October 1987). "Molecular cloning and amino acid sequence of leukotriene A4 hydrolase". Proc. Natl. Acad. Sci. U.S.A. 84 (19): 6677–81. Bibcode:1987PNAS...84.6677F. doi:10.1073/pnas.84.19.6677. PMC 299146. PMID 2821541.
- ^ Mancini JA, Evans JF (July 1995). "Cloning and characterization of the human leukotriene A4 hydrolase gene". Eur. J. Biochem. 231 (1): 65–71. doi:10.1111/j.1432-1033.1995.tb20671.x. PMID 7628486.
- ^ Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggström JZ (June 2004). "Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates". J. Biol. Chem. 279 (26): 27376–82. doi:10.1074/jbc.M401031200. PMID 15078870.
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. doi:10.1016/0304-4165(85)90160-6. 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. doi:10.1016/S0021-9258(18)47872-6. 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. doi:10.1016/S0021-9258(19)84567-2. 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. doi:10.1016/j.plipres.2004.10.001. PMID 15748653.
- Fretland AJ, Omiecinski CJ (2000). "Epoxide hydrolases: biochemistry and molecular biology" (PDF). Chem. Biol. Interact. 129 (1–2): 41–59. CiteSeerX 10.1.1.462.3157. doi:10.1016/S0009-2797(00)00197-6. 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. doi:10.1016/S0021-9258(19)78120-4. 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. doi:10.1016/S0021-9258(18)61098-1. PMID 3038871.
External links[]
- leukotriene A4 hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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Categories:
- Genes on human chromosome 12
- EC 3.3.2
- Enzymes of known structure
- Hydrolase stubs