Abstract:
:Numerous indolyl amino acids and their derivatives inhibited arginase activity. The inhibition was found to be non-competitive, - at least partly - allosteric, and independent on manganese ions in the active site, and it cannot be explained by the dissociation of arginase homotrimers. Indole alone is weakly inhibitory; however, the presence of three-carbon side chains and their net charges is favorable for the inhibition. The binding of the inhibitory compounds caused only minor changes in the steric structure of arginase: a slight increase in alpha-helix content was detected by circular dichroism together with a decrease in parallel pleated sheet and beta-turn sections. A slight alteration in the tertiary structure was also found using tryptophane fluorescence studies, but buried apolar side chains were not transposed to the protein surface. Computer studies that were performed did not provide additional structural information.
journal_name
Amino Acidsjournal_title
Amino acidsauthors
Hrabák A,Bajor T,Mészáros Gdoi
10.1007/s00726-006-0470-3subject
Has Abstractpub_date
2008-02-01 00:00:00pages
293-300issue
2eissn
0939-4451issn
1438-2199journal_volume
34pub_type
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