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Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme.

Artikel i vetenskaplig tidskrift
Författare Ulla Rüetschi
Birgit Odelhög
Sven Lindstedt
Jane Barros-Söderling
B Persson
Hans Jörnvall
Publicerad i European journal of biochemistry / FEBS
Volym 205
Nummer/häfte 2
Sidor 459-66
ISSN 0014-2956
Publiceringsår 1992
Publicerad vid Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin
Sidor 459-66
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord 4-Hydroxyphenylpyruvate Dioxygenase, chemistry, Amino Acid Sequence, Chromatography, Gel, Chromatography, High Pressure Liquid, Cyanogen Bromide, Humans, Hydroxylamine, Hydroxylamines, Molecular Sequence Data, Peptide Fragments, isolation & purification, Protein Conformation, Pseudomonas, enzymology, Trypsin
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

The primary structure of Pseudomonas 4-hydroxyphenylpyruvate dioxygenase was determined. Sequence degradation of the intact protein and of peptides from three different digests of the carboxymethylated protein established a 357-residue polypeptide chain with a free alpha-amino group. Hydroxylamine cleavage at a single Asn-Gly sequence was useful. Comparisons with known structures in data banks revealed no close relationship with other characterized proteins. The human enzyme has a related composition, suggesting that also the eukaryotic form belongs to this protein type, but with a blocked N-terminus like in many other eukaryotic intracellular proteins. Secondary structure predictions suggest an alpha/beta mixed structure, fairly typical of globular proteins, without long segments of hydrophobicity or charge, although a region in the middle of the C-terminal third of the subunit appears to have the most extreme properties. A ferric centre, correlating with enzyme activity and absorbance at 595 nm, has previously been assigned to tyrosinate coordination. The Tyr and His distributions, and the position of a single Cys residue, all suggest a few likely sites, outside the C-terminal segment, for this centre.

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