Download Nadine Noelting

Nadine Noelting
Phenylketonuria (PKU)
1.
>gi|4557819|ref|NP_000268.1| phenylalanine-4-hydroxylase [Homo sapiens]
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPS
RLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGA
ELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIF
PLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPE
PDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSS
FGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQR
IEVLDNTQQLKILADSINSEIGILCSALQKIK
2. The furthest back homologs for my protein can be found is in cellular slime molds.
3. Conserved domains are found most readily in the aromatic amino acid hydroxylase
superfamily. This is roughly located between amino acids 120 and 420. The mutations
associated with my gene are found in this conserved domain. The family consists of nonheme, iron (II)- dependent enzymes, including phenylalanine hydroxylase, eukaryotic
tyrosine hydroxylase, and eukaryotic tryptophan hydroxylase. Each enzyme contains an
ion metal binding site. PAH is involved in phenylalanine catabolism, TyrH in the
biosynthesis of catecholamine and TrpH in the biosynthesis of serotonin.
A second conserved domain exists earlier in the sequence located roughly
between amino acids 20 and 110. This is referred to as an ACT domain, which
specifically bind to amino acids or small ligands that lead to enzyme regulation.
Biology Workbench
cd03347: eu_PheOH, with user query added
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterindependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent
enzymes that also includes prokaryotic phenylalanine-4-hydroxylase (pro_PheOH),
eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase
(TrpOH). PheOH catalyzes the first and rate-limiting step in the metabolism of the amino
acid L-phenylalanine (L-Phe), the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor.
The catalytic activity of the tetrameric enzyme is tightly regulated by the binding of LPhe and BH4 as well as by phosphorylation. Mutations in the human enzyme are linked
to a severe variant of phenylketonuria.
Superfamily] cl01244, Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH),
eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts
L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter
biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved
in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all
homotetramers.