Abstract:
:A catalase-related allene oxide synthase (cAOS) and true catalases that metabolize hydrogen peroxide have similar structure around the heme. One of the distal heme residues considered to help control catalysis is a highly conserved asparagine. Here we addressed the role of this residue in metabolism of the natural substrate 8R-hydroperoxyeicosatetraenoic acid by cAOS and in H(2)O(2) breakdown by catalase. In cAOS, the mutations N137A, N137Q, N137S, N137D, and N137H drastically reduced the rate of reaction (to 0.8-4% of wild-type), yet the mutants all formed the allene oxide as product. This is remarkable because there are many potential heme-catalyzed transformations of fatty acid hydroperoxides and special enzymatic control must be required. In human catalase, the N148A, N148S, or N148D mutations only reduced rates to approximately 20% of wild-type. The distal heme Asn is not essential in either catalase or cAOS. Its conservation throughout evolution may relate to a role in optimizing catalysis.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Gao B,Boeglin WE,Brash ARdoi
10.1016/j.abb.2008.07.011subject
Has Abstractpub_date
2008-09-15 00:00:00pages
285-90issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(08)00349-4journal_volume
477pub_type
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