Abstract
Both glutamine: α-ketoglutarate amidotransferase and glutamate dehydrogenase activities are obtained from Escherichia coli grown in minimal medium containing glucose and ammonia. These activities are not additive, suggesting an interaction between them. Normally both of these activities are equally inhibited by homoserine. In mutants resistant to homoserine inhibition both activities are affected in parallel. Furthermore, the ratio of the wild-type activities remains constant over a 30-fold range in purification. This evidence suggests that these activities are associated with a single complex. A possible role for this complex in the regulation of primary amination is discussed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 41-47 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 48 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 11 1972 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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A possible role in the regulation of primary amination for a complex of glutamine : α-Ketoglutarate amidotransferase and glutamate dehydrogenase in Escherichia coli. / Savageau, Michael A.; Kotre, Ann Marie; Sakamoto, Naoto.
In: Biochemical and Biophysical Research Communications, Vol. 48, No. 1, 11.07.1972, p. 41-47.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A possible role in the regulation of primary amination for a complex of glutamine
T2 - α-Ketoglutarate amidotransferase and glutamate dehydrogenase in Escherichia coli
AU - Savageau, Michael A.
AU - Kotre, Ann Marie
AU - Sakamoto, Naoto
PY - 1972/7/11
Y1 - 1972/7/11
N2 - Both glutamine: α-ketoglutarate amidotransferase and glutamate dehydrogenase activities are obtained from Escherichia coli grown in minimal medium containing glucose and ammonia. These activities are not additive, suggesting an interaction between them. Normally both of these activities are equally inhibited by homoserine. In mutants resistant to homoserine inhibition both activities are affected in parallel. Furthermore, the ratio of the wild-type activities remains constant over a 30-fold range in purification. This evidence suggests that these activities are associated with a single complex. A possible role for this complex in the regulation of primary amination is discussed.
AB - Both glutamine: α-ketoglutarate amidotransferase and glutamate dehydrogenase activities are obtained from Escherichia coli grown in minimal medium containing glucose and ammonia. These activities are not additive, suggesting an interaction between them. Normally both of these activities are equally inhibited by homoserine. In mutants resistant to homoserine inhibition both activities are affected in parallel. Furthermore, the ratio of the wild-type activities remains constant over a 30-fold range in purification. This evidence suggests that these activities are associated with a single complex. A possible role for this complex in the regulation of primary amination is discussed.
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UR - http://www.scopus.com/inward/citedby.url?scp=0015502817&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(72)90341-5
DO - 10.1016/0006-291X(72)90341-5
M3 - Article
C2 - 4557512
AN - SCOPUS:0015502817
VL - 48
SP - 41
EP - 47
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -