Abstract:
:We previously obtained evidence for intrinsic aminopeptidase activity for leukotriene (LT)A4 hydrolase, an enzyme characterized to specifically catalyse the hydrolysis of LTA4 to LTB4, a chemotactic compound. From a sequence homology search between LTA4 hydrolase and several aminopeptidases, it became clear that they share a putative active site for known aminopeptidases and a zinc binding domain. Thus, Glu-297 of LTA4 hydrolase is a candidate for the active site of its aminopeptidase activity, while His-296, His-300 and Glu-319 appear to constitute a zinc binding site. To determine whether or not this putative active site is also essential to LTA4 hydrolase activity, site-directed mutagenesis experiments were carried out. Glu-297 was mutated into 4 different amino acids. The mutant E297Q (Glu changed to Gln) conserved LTA4 hydrolase activity but showed little aminopeptidase activity. Other mutants at Glu-297 (E297A, E297D and E297K) showed markedly reduced amounts of both activities. It is thus proposed that either a glutamic or glutamine moiety at 297 is required for full LTA4 hydrolase activity, while the free carboxylic acid of glutamic acid is essential for aminopeptidase.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Minami M,Bito H,Ohishi N,Tsuge H,Miyano M,Mori M,Wada H,Mutoh H,Shimada S,Izumi Tdoi
10.1016/0014-5793(92)80806-rkeywords:
subject
Has Abstract,Author List Incompletepub_date
1992-09-14 00:00:00pages
353-7issue
3eissn
0014-5793issn
1873-3468journal_volume
309pub_type
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