Abstract
Polyamine oxidase catalyses the oxidation of the secondary amino group of spermine, spermidine and their acetyl derivatives. The enzyme plays an important role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of maize polyamine oxidase have been grown by the hanging-drop vapour-diffusion technique. The crystals are in hexagonal space group P6122 (or P6522) with cell dimensions a = b = 184.6, c = 280.9 A. A native data set has been collected to 2.7 A resolution at a synchrotron radiation source.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Catalysis
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Crystallization
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Crystallography, X-Ray
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Flavin-Adenine Dinucleotide / metabolism
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Oxidoreductases Acting on CH-NH Group Donors / chemistry*
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Oxidoreductases Acting on CH-NH Group Donors / isolation & purification
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Oxidoreductases Acting on CH-NH Group Donors / metabolism
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Plant Proteins / chemistry*
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Plant Proteins / isolation & purification
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Plant Proteins / metabolism
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Polyamine Oxidase
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Protein Conformation
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Spermidine / metabolism
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Substrate Specificity
Substances
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Plant Proteins
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Flavin-Adenine Dinucleotide
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Oxidoreductases Acting on CH-NH Group Donors
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Spermidine