|
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 |
Activity |
2.6.1.45 |
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 2.6.1.45) 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 2.6.1.2) 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 |
|