EC Number   |
Substrates  |
Organism |
Products |
Reversibility |
|---|
    1.3.1.12 | L-arogenate + NAD+ |
- |
Escherichia coli |
L-tyrosine + NADH + CO2 |
- |
? |
| 1.3.1.12 | L-arogenate + NAD+ |
- |
Klebsiella pneumoniae |
L-tyrosine + NADH + CO2 |
- |
? |
| 1.3.1.12 | L-arogenate + NAD+ |
- |
Aquifex aeolicus |
L-tyrosine + NADH + CO2 |
- |
? |
| 1.3.1.12 | 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 |
Haemophilus influenzae |
? |
- |
? |
| 1.3.1.12 | more |
no activity with arogenate |
Saccharomyces cerevisiae |
? |
- |
? |
| 1.3.1.12 | more |
no activity with arogenate |
Pleurotus ostreatus |
? |
- |
? |
| 1.3.1.12 | 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 |
Haemophilus influenzae KW20 |
? |
- |
? |
| 1.3.1.12 | prephenate + NAD+ |
- |
Bacillus subtilis |
4-hydroxyphenylpyruvate + NADH + CO2 |
- |
? |
| 1.3.1.12 | prephenate + NAD+ |
- |
Escherichia coli |
4-hydroxyphenylpyruvate + NADH + CO2 |
- |
? |
| 1.3.1.12 | prephenate + NAD+ |
- |
Saccharomyces cerevisiae |
4-hydroxyphenylpyruvate + NADH + CO2 |
- |
? |
