Abstract:
:We have compared the urea stability of the human aromatic amino acid hydroxylases (AAAHs), key enzymes involved in neurotransmitter biosynthesis and amino acid homeostasis. Tyrosine-, tryptophan- and phenylalanine hydroxylase (TH, TPH and PAH, respectively) were transiently activated at low urea concentrations and rapidly inactivated in >3 M urea. The denaturation of TH occurred through two cooperative transitions, with denaturation midpoints of 1.41+/-0.06 and 5.13+/-0.05 M urea, respectively. Partially denatured human TH (hTH) retained more of its secondary structure than human PAH (hPAH), and was found to exist as tetramers, whereas hPAH dissociated into dimers. Furthermore, the urea-induced aggregation of hPAH was 100-fold higher than for hTH. These results suggest that the denatured state properties of the AAAHs contribute significantly to the stability of these enzymes and their tolerance towards missense mutations.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kleppe R,Haavik Jdoi
10.1016/j.febslet.2004.03.092keywords:
subject
Has Abstractpub_date
2004-05-07 00:00:00pages
155-9issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304004132journal_volume
565pub_type
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