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The subcellular location of 4‐aminobutyrate aminotransferase in Candida boidinii and its probable role in the breakdown of putrescine and spermidine
Author(s) -
Large Peter J.,
Robertson Anne
Publication year - 1988
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320040209
Subject(s) - putrescine , spermidine , biology , biochemistry , subcellular localization , yeast , enzyme , polyamine , methylamine , spermine , ammonium , cytoplasm , chemistry , organic chemistry
4‐Aminobutyrate aminotransferase (EC 2.6.1.19) was elevated in activity by 20‐ to 40‐fold in cells of the yeast Candida boidinii grown on spermidine, putrescine, 4‐acetamidobutyrate and 4‐aminobutyrate compared with activities detected in cells grown on ammonium, methylamine or 6‐aminohexanoate, confirming previous suggesions that it plays a key role in polyamine breakdown. Other enzymes of the proposed route of polymine breakdown were found to be non‐coordinately induced or derepressed during growth on spermidine or its putative breakdown intermediates. The enzyme was not sedimented from spheroplast lysates at 100 000 × g , and it is concluded that it is conclded that it is probably cytosoilc in its subcellular location (although the data do not exclude the possiblity of its being vacuolar).