Abstract:
:Phenylalanine acts as an allosteric activator of the tetrahydropterin-dependent enzyme phenylalanine hydroxylase. Hydrogen/deuterium exchange monitored by mass spectrometry has been used to gain insight into local conformational changes accompanying activation of rat phenylalanine hydroxylase by phenylalanine. Peptides in the regulatory and catalytic domains that lie in the interface between these two domains show large increases in the extent of deuterium incorporation from solvent in the presence of phenylalanine. In contrast, the effects of phenylalanine on the exchange kinetics of a mutant enzyme lacking the regulatory domain are limited to peptides surrounding the binding site for the amino acid substrate. These results support a model in which the N-terminus of the protein acts as an inhibitory peptide, with phenylalanine binding causing a conformational change in the regulatory domain that alters the interaction between the catalytic and regulatory domains.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Li J,Dangott LJ,Fitzpatrick PFdoi
10.1021/bi1001294subject
Has Abstractpub_date
2010-04-20 00:00:00pages
3327-35issue
15eissn
0006-2960issn
1520-4995journal_volume
49pub_type
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