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Mutation Of TYR-383 in Leukotriene A4 Hydrolase: Effects on Enzyme Activities

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Recent Advances in Prostaglandin, Thromboxane, and Leukotriene Research

Abstract

Leukotriene (LT) A4 hydrolase catalyzes hydrolysis of LTA4 (5(S)-trans-5,6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid) into the proinflammatory compound LTB4 (5(S), 12 (R)-6,14-cis-8,10-trans-dihydroxyeicosatetraenoic acid, in a reaction without any cofactor requirement. The substrate LTA4 is in turn derived from arachidonic acid by two consecutive reactions catalyzed by 5-lipoxygenase1.

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References

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© 1997 Springer Science+Business Media New York

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Andberg, M., Wetterholm, A., Haeggström, J.Z. (1997). Mutation Of TYR-383 in Leukotriene A4 Hydrolase: Effects on Enzyme Activities. In: Sinzinger, H., Samuelsson, B., Vane, J.R., Paoletti, R., Ramwell, P., Wong, P.YK. (eds) Recent Advances in Prostaglandin, Thromboxane, and Leukotriene Research. Advances in Experimental Medicine and Biology, vol 433. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1810-9_30

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  • DOI: https://doi.org/10.1007/978-1-4899-1810-9_30

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  • Print ISBN: 978-1-4899-1812-3

  • Online ISBN: 978-1-4899-1810-9

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