Oxidative deamination of Se-(1-carboxyethyl)-,Se-(1-carboxypropyl)- and Se-(2-carboxyethyl)-selenocysteine by snake venom L-aminoacid oxidase.
Details are reported for the synthesis of Se-(1-carboxyethyl)-selenocysteine (1-CESeC), Se-(1-carboxypropyl)-selenocysteine (1-CPSeC) and Se-(2-carboxyethyl)-selenocysteine (2-CESeC). They can be obtained in pure cristalline form with good yield. Some chromatographic properties, useful for their identification, are described. The three aminoacids are good substrates for snake venom L-aminoacid oxidase, giving the corresponding alpha-ketoacids as reaction products.
Coccia
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Dipartimento di Scienze Biochimiche-Universitá La Sapienza, Roma, Italy.
Blarzino
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Foppoli
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Cini
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C
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D003545:Cysteine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D007202:Indicators and Reagents; D007700:Kinetics; D050830:L-Amino Acid Oxidase; D010101:Oxygen Consumption; D012643:Selenium / Q000138:chemical synthesis / Q000378:metabolism*; D017279:Selenocysteine; D012910:Snake Venoms; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D007202:Indicators and Reagents; D012910:Snake Venoms; D017279:Selenocysteine; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase; D012643:Selenium; D003545:Cysteine