Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase

Roche, P.; Moorehead, Thomas J.; Hamilton, Gordon A.

doi:10.1016/0003-9861(82)90188-6

Cited by 30 publications

(21 citation statements)

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“…Preparations of the enzyme from chicken [ 5 ] , pig [4] and Pseudomonas [l] all give an EPR signal at g = 4.3, indicating a high-spin ferric center in a rhombic ligand field. Further studies of the Pseudomonas enzyme by Raman spectroscopy revealed the presence of enhanced vibrations, characteristic of tyrosinate co-ordination to the iron centre [12].…”

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confidence: 99%

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Human 4‐hydroxyphenylpyruvate dioxygenase

Rüetschi

Dellsèn

Sahlin

et al. 1993

European Journal of Biochemistry

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We report the primary structure of 4-hydroxyphenylpyruvate dioxygenase [4-hydroxyphenylpyruvate : oxygen oxidoreductase (hydroxylating, decarboxylating)]. The work is based on the isolation of cDNA clones from human liver Agtll libraries. Several overlapping clones covering the coding sequence were characterized. In parallel, peptides from four different digests of the purified protein were analysed for their amino-acid sequence. These peptide sequences covered 86% of the cDNA-derived amino-acid sequence. This gives the sequence for a polypeptide of 392 amino acids with a calculated molecular mass of 44.8 kDa.There is more than 80% identity between the human and the pig enzymes and also between these enzymes and the F antigen from rat and the two allelic forms of this antigen from mouse. The enzyme has 53% conserved amino acids and 27% identical amino acids in common with 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. P. J. 874 and 52% conserved and 28% identical residues, with a protein from Shewanella colwellinna. At the C-terminus there is 61 % identity between the seven proteins. These results indicate that these proteins are all 4-hydroxyphenylpyruvate dioxygenases. The identity of the C-terminus makes this part of the molecule a candidate for a functional role in the catalytic process. At conserved positions in all seven enzymes, there are two tyrosine residues and three histidine residues, i. e. amino acids which have been implicated as ligands for iron in 2-oxoacid-dependent dioxygenases. The gene encoding the enzyme was localized to chromosome 12q14 + qter by Southern-blot analysis of human-rodent somatic-cell hybrids.

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confidence: 99%

“…4-Hydroxyphenylpyruvate dioxygenase has been purified from a Pseudomonas species [1] and from livers of human [2, 31, pig [4] and chicken [5]. The mammalian enzymes are dimers of equally sized subunits with masses of approximately 45 kDa, whereas the bacterial enzyme is a tetramer with a subunit molecular mass of 40 kDa.…”

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Human 4‐hydroxyphenylpyruvate dioxygenase

Rüetschi

Dellsèn

Sahlin

et al. 1993

European Journal of Biochemistry

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“…This activity is often present at very high levels and is involved in Phe and Tyr degradation. HPPDase has been purified from several mammalian and bacterial sources (Wada et al, 1975;Lindstedt et al, 1977;Roche et al, 1982;Endo et al, 1992), and in all cases the active enzyme was found to be a homodimer or, less commonly, a homotetramer, with subunits of approximately 40 to 48 kD. As a result of the central role HPPDase serves in aromatic amino acid metabolism in mammals and plastidic quinone synthesis in plants, a class of competitive inhibitors of HPPDases collectively known as triketones has been developed and used for a variety of clinical and agricultural purposes (Lindstedt et al, 1992;Schultz et al, 1993;Secor, 1994).…”

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Complementation of the Arabidopsispds1Mutation with the Gene Encodingp-Hydroxyphenylpyruvate Dioxygenase

1998

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Plastoquinone and tocopherols are the two major quinone compounds in higher plant chloroplasts and are synthesized by a common pathway. In previous studies we characterized two loci in Arabidopsis defining key steps of this biosynthetic pathway. Mutation of the PDS1 locus disrupts the activity of p-hydroxyphenylpyruvate dioxygenase (HPPDase), the first committed step in the synthesis of both plastoquinone and tocopherols in plants. Although plants homozygous for the pds1 mutation could be rescued by growth in the presence of homogentisic acid, the product of HPPDase, we were unable to determine if the mutation directly or indirectly disrupted HPPDase activity. This paper reports the isolation of a cDNA, pHPPD, encoding Arabidopsis HPPDase and its functional characterization by expression in both plants and Escherichia coli. pHPPD encodes a 50-kD polypeptide with homology to previously identified HPPDases, including 37 highly conserved amino acid residues clustered in the carboxyl region of the protein. Expression of pHPPD in E. coli catalyzes the accumulation of homogentisic acid, indicating that it encodes a functional HPPDase enzyme. Mapping of pHPPD and co-segregation analysis of the pds1 mutation and the HPPD gene indicate tight linkage. Constitutive expression of pHPPD in a pds1 mutant background complements this mutation. Finally, comparison of the HPPD genomic sequences from wild type and pds1 identified a 17-bp deletion in the pds1 allele that results in deletion of the carboxyterminal 26 amino acids of the HPPDase protein. Together, these data conclusively demonstrate that pds1 is a mutation in the HPPDase structural gene.

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“…This reaction proceeds through an oxidative decarboxylation of the 2-oxoacid side chain of the substrate, which is accompanied by hydroxylation of the aromatic ring and a 1,2-migration of the carboxymethyl group (Jefford and Cadby, 1981). The purified enzyme was shown to contain nonheme-reduced iron, which is essential for catalytic activity (Wada et al, 1975;Lindblad et al, 1977;Roche et al, 1982;Endo et al, 1992;Rû etschi et al, 1993). This enzyme belongs to the extradiol ␣-ketoaciddependent group of dioxygenases.…”

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“…In most organisms this enzyme activity is involved in the catabolism of the aromatic amino acid Tyr (Goodwin, 1972). All mammalian 4HPPDs purified so far behave as homodimers, with subunits of 43 to 49 kD (Wada et al, 1975;Lindblad et al, 1977;Roche et al, 1982;Endo et al, 1992;Rû etschi et al, 1993). In contrast, the Pseudomonas sp.…”

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confidence: 99%

Characterization and Subcellular Compartmentation of Recombinant 4-Hydroxyphenylpyruvate Dioxygenase from Arabidopsis in Transgenic Tobacco1

Garcia

Rodgers²,

Pepin

et al. 1999

Plant Physiology

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4-Hydroxyphenylpyruvate dioxygenase (4HPPD) catalyzes the formation of homogentisate (2,5-dihydroxyphenylacetate) from p-hydroxyphenylpyruvate and molecular oxygen. In plants this enzyme activity is involved in two distinct metabolic processes, the biosynthesis of prenylquinones and the catabolism of tyrosine. We report here the molecular and biochemical characterization of an Arabidopsis 4HPPD and the compartmentation of the recombinant protein in chlorophyllous tissues. We isolated a 1508-bp cDNA with one large open reading frame of 1338 bp. Southern analysis strongly suggested that this Arabidopsis 4HPPD is encoded by a single-copy gene. We investigated the biochemical characteristics of this 4HPPD by overproducing the recombinant protein in Escherichia coli JM105. The subcellular localization of the recombinant 4HPPD in chlorophyllous tissues was examined by overexpressing its complete coding sequence in transgenic tobacco (Nicotiana tabacum), using Agrobacterium tumefaciens transformation. We performed western analyses for the immunodetection of protein extracts from purified chloroplasts and total leaf extracts and for the immunocytochemistry on tissue sections. These analyses clearly revealed that 4HPPD was confined to the cytosol compartment, not targeted to the chloroplast. Western analyses confirmed the presence of a cytosolic form of 4HPPD in cultured green Arabidopsis cells.

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Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase

Cited by 30 publications

References 28 publications

Human 4‐hydroxyphenylpyruvate dioxygenase

Human 4‐hydroxyphenylpyruvate dioxygenase

Complementation of the Arabidopsispds1Mutation with the Gene Encodingp-Hydroxyphenylpyruvate Dioxygenase

Characterization and Subcellular Compartmentation of Recombinant 4-Hydroxyphenylpyruvate Dioxygenase from Arabidopsis in Transgenic Tobacco1

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