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Literature DB >> 873933

Steady state kinetics of 4-hydroxyphenylpyruvate dioxygenase from human liver (III).

Abstract

Kinetic experiments have been made with an apparently homogenous preparation of human liver 4-hydroxyphenylpyruvate dioxygenase Form 3 (4-hydroxyphenylpyruvate: oxygen oxidoreductase (hydroxylating, decarboxylating), EC 1.13.11.27) at 37 degrees in 0.2 M Tris/HCL, pH 7.5, by measuring the evolved carbon dioxide from the 1-14C-labeled substrate or the formation of homogentisate from the U-14C-labeled substrate. The effect of variations in the concentrations of substrates, products, and metal chelators on the velocity of the forward reaction was studied. The results agree with an Ordered Bi Bi kinetic mechanism (Cleland, W. W. (1963) Biochim. Biophys. Acta 67, 104--137), where 4-hydroxyphenylpyruvate is added prior to oxygen and CO2 released before homogentisate. A Theorell-Chance mechanism has not been excluded.

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Year: 1977 PMID： 873933

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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Cited

9 in total

1. 4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme.

Authors: Corinne Raspail; Matthieu Graindorge; Yohann Moreau; Serge Crouzy; Bertrand Lefèbvre; Adeline Y Robin; Renaud Dumas; Michel Matringe
Journal: J Biol Chem Date: 2011-05-25 Impact factor: 5.157

2. Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes.

Authors: Michael L Neidig; Andrea Decker; Oliver W Choroba; Fanglu Huang; Michael Kavana; Graham R Moran; Jonathan B Spencer; Edward I Solomon
Journal: Proc Natl Acad Sci U S A Date: 2006-08-18 Impact factor: 11.205

9. Identification and molecular characterization of the homogentisate pathway responsible for pyomelanin production, the major melanin constituents in Aeromonas media WS.

Authors: He Wang; Yunqian Qiao; Baozhong Chai; Chenxi Qiu; Xiangdong Chen
Journal: PLoS One Date: 2015-03-20 Impact factor: 3.240

9 in total

Steady state kinetics of 4-hydroxyphenylpyruvate dioxygenase from human liver (III).

1. 4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme.

2. Spectroscopic and electronic structure studies of aromatic electrophilic attack and hydrogen-atom abstraction by non-heme iron enzymes.

Review 3. Tyrosinaemia type I and NTBC (2-(2-nitro-4-trifluoromethylbenzoyl)-1,3-cyclohexanedione).

4. The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.

5. Inverse solvent isotope effects arising from substrate triggering in the factor inhibiting hypoxia inducible factor.

6. Steady-state kinetics and inhibition of anaerobically purified human homogentisate 1,2-dioxygenase.

7. Burkholderia cenocepacia C5424 produces a pigment with antioxidant properties using a homogentisate intermediate.

Review 8. The diverse and pervasive chemistries of the alpha-keto acid dependent enzymes.

9. Identification and molecular characterization of the homogentisate pathway responsible for pyomelanin production, the major melanin constituents in Aeromonas media WS.