Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
Article Abstract:
The disease-related mutant forms of the mammalian aromatic amino acid hydroxylases have made these compounds an interesting subject of chemical research. Recent studies have confirmed the existence of a common three-domain organization of phenylalanine and tyrosine hydroxylases, which provides an in-depth understanding of the oligomeric states, catalytic activities and regulatory properties of aromatic amino acid hydroxylases. It was found that these enzymes feature identical secondary structures with similar arrangement and topological connections.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1999
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Partially modified retro-inverso peptides: development, synthesis, and conformational behavior
Article Abstract:
The development of partially modified retro-inverso peptides is aimed at increasing the peptides' biological half-life function, increasing their activities and enhancing peptide selectivity. Since peptides have important functions such as extracellular messengers, neurotransmitters and neuromodulators, modifying these peptides can be suitable in pharmaceutical applications and may yield important information regarding structure-activity relationships of endogenous peptides to overcome metabolic barriers.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1998
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