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Characterization of...
Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme.
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- Rüetschi, Ulla, 1962 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
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- Odelhög, Birgit, 1942 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
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- Lindstedt, Sven (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för laboratoriemedicin, Avdelningen för klinisk kemi/transfusionsmedicin,Institute of Laboratory Medicine, Dept of Clinical Chemistry/Transfusion Medicine
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visa fler...
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Barros-Söderling, Jane (författare)
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Persson, B (författare)
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Jörnvall, Hans (författare)
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visa färre...
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(creator_code:org_t)
- 1992
- 1992
- Engelska.
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Ingår i: European journal of biochemistry / FEBS. - 0014-2956. ; 205:2, s. 459-66
- Relaterad länk:
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https://gup.ub.gu.se...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Nyckelord
- 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
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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