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Literature summary for 1.3.1.12 extracted from

  • Chiu, H.J.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Clayton, T.; Das, D.; Deller, M.C.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Grzechnik, A.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Kumar, A.; Marciano, D.; McMullan, D.; Miller, M.D.; Morse, A.T.
    The structure of Haemophilus influenzae prephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes (2010), Acta Crystallogr. Sect. F, 66, 1317-1325.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.1.12

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment) Organism
prephenate dehydrogenase component of the TyrA protein from strain Rd KW20 in complex with inhibitor tyrosine and cofactor NAD+, sitting drop vapour diffusion method, 200 nl of 19.6 mg/ml protein in 20 mM HEPES pH 8.0, 200 mM NaCl, 40 mM imidazole, 1 mM TCEP are mixed with 200 nl reservoir solution containing 0.04 M potassium dihydrogen phosphate, 20.0% v/v glycerol and 16.0% w/v PEG 8000, X-ray diffrraction structure determination and analysis at 2.0 A resolution Haemophilus influenzae

Inhibitors

Inhibitors Comment Organism Structure
tyrosine is bound directly at the catalytic site as a competitive inhibitor Haemophilus influenzae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prephenate + NAD+ Haemophilus influenzae
-
 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?
prephenate + NAD+ Haemophilus influenzae KW20
-
 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Haemophilus influenzae P43902
-
-
Haemophilus influenzae KW20 P43902
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, cleavage of the tag by TEV protease Haemophilus influenzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 ?
-
 ?
additional information 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 ?
-
 ?
prephenate + NAD+
-
 Haemophilus influenzae 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?
prephenate + NAD+ key active-site residues are located at the domain interface, including His200, Arg297 and Ser179, that are involved in catalysis and/or ligand binding and are highly conserved in TyrA proteins Haemophilus influenzae 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?
prephenate + NAD+
-
 Haemophilus influenzae KW20 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?
prephenate + NAD+ key active-site residues are located at the domain interface, including His200, Arg297 and Ser179, that are involved in catalysis and/or ligand binding and are highly conserved in TyrA proteins Haemophilus influenzae KW20 4-hydroxyphenylpyruvate + CO2 + NADH + H+
-
 ?

Subunits

Subunits Comment Organism
dimer SDS-PAGE and gel filtration, the dimeric enzyme, with each monomer consisting of an N-terminal alpha/beta dinucleotide-binding domain and a C-terminal alpha-helical dimerization domain, structure comparisons, overview Haemophilus influenzae

Synonyms

Synonyms Comment Organism
PDH
-
 Haemophilus influenzae
tyrA
-
 Haemophilus influenzae

Cofactor

Cofactor Comment Organism Structure
NAD+ binding mode Haemophilus influenzae

General Information

General Information Comment Organism
metabolism chorismate mutase/prephenate dehydrogenase from Haemophilus influenzae Rd KW20 is a bifunctional enzyme that catalyzes the rearrangement of chorismate to prephenate and the NAD(P)+-dependent oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate in tyrosine biosynthesis Haemophilus influenzae