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Results 1 - 10 of 139 > >>
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
L-arogenate + NAD+
-
L-tyrosine + NADH + CO2
-
?
L-arogenate + NAD+
-
L-tyrosine + NADH + CO2
-
?
L-arogenate + NAD+
-
L-tyrosine + NADH + CO2
-
?
more
a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview
?
-
-
more
no activity with arogenate
?
-
-
more
no activity with arogenate
?
-
-
more
a dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain. Absence of an alpha/beta motif in HinfPDH that is present in other TyrA proteins. Residues from this motif are involved in discrimination between NADP+ and NAD+. The loop between beta5 and beta6 in the N-terminal domain is much shorter in HinfPDH and an extra helix is present at the C-terminus. Furthermore, HinfPDH adopts a more closed conformation compared with TyrA proteins that do not have tyrosine bound. This conformational change brings the substrate, cofactor and active-site residues into close proximity for catalysis. An ionic network consisting of Arg297, a key residue for tyrosine binding, a water molecule, Asp206, from the loop between beta5 and beta6, and Arg365', from the additional C-terminal helix of the adjacent monomer, is observed that might be involved in gating the active site. Active site structure, overview
?
-
-
prephenate + NAD+
-
4-hydroxyphenylpyruvate + NADH + CO2
-
?
prephenate + NAD+
-
4-hydroxyphenylpyruvate + NADH + CO2
-
?
prephenate + NAD+
-
4-hydroxyphenylpyruvate + NADH + CO2
-
-
Results 1 - 10 of 139 > >>