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B6db references: 93190676

type Journal Article
authors Paszkowski, A.
title On the possibility of involvement of glutamate:glyoxylate and serine:glyoxylate aminotransferases from rye (Secale cereale L.) seedlings in the metabolism of tetrapyrrole compounds
journal Acta Biochim Pol
ui 93190676
year (1992)
volume 39
number 4
pages 345-53
keywords Glyoxylates/metabolism
abstract The activity of highly purified L-serine:glyoxylate aminotransferase (SGAT, EC from rye seedlings was inhibited competitively by 5- aminolevulinate (ALA, Ki = 5 mM) SGAT was activated by hematin. Protoporphyrin IX and hematin inhibited irreversibly the activity of highly purified glutamate:glyoxylate aminotransferase (GGAT, EC from rye seedlings. SGAT was found to catalyse transamination between ALA and hydroxypyruvate, whereas GGAT that between ALA and 2- oxoglutarate or pyruvate. It is suggested that SGAT is involved in the process of degradation of the excess ALA which has not been incorporated into porphyrin compounds.
last changed 2002/11/12 16:17

B6db references