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Literature summary for 1.14.16.1 extracted from

  • Loaiza, A.; Armstrong, K.M.; Baker, B.M.; Abu-Omar, M.M.
    Kinetics of thermal unfolding of phenylalanine hydroxylase variants containing different metal cofactors (FeII, CoII, and ZnII) and their isokinetic relationship (2008), Inorg. Chem., 47, 4877-4883.
    View publication on PubMed
Search for more literature for 1.14.16.1

Cloned(Commentary)

Cloned (Comment) Organism
gene pah, expression in Escherichia coli Chromobacterium violaceum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamics, overview Chromobacterium violaceum

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity Chromobacterium violaceum
Fe2+ native metal cofactor, determination of binding affinity, binding structure, overview Chromobacterium violaceum
Zn2+ can substitute for Fe2+, but is less efficient at higher temperature, determination of binding affinity Chromobacterium violaceum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Chromobacterium violaceum
-
 L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum P30967
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli by anion exchange chromatography and gel filtration Chromobacterium violaceum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2
-
 Chromobacterium violaceum L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Synonyms

Synonyms Comment Organism
PAH
-
 Chromobacterium violaceum
phenylalanine hydroxylase
-
 Chromobacterium violaceum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
44 76 pH 7.4, kinetics of thermal unfolding of apo- and holo-enzymes within the temperature range and with different metal cofactors: native Fe2+, or artificial Zn2+ or Co2+, unfolding profiles, transition-state analysis shows a common mechanism for all enzyme variants, at higher temperatures the unfolding rates of Zn- and Co-PAH are affected significantly by entropy, while the unfolding rates of apo- and Fe-PAH are dominated by enthalpy even at higher temperatures, overview Chromobacterium violaceum

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
 Chromobacterium violaceum