抄録
The examination of model robustness in the previous paper (Shiraishi, F., and Savageau, M. A. (1992) J. Biol. Chem. 267, 22919-22925 led to the suggestion that the current model for the tricarboxylic acid cycle in Dictyostelium discoideum is ill-determined with respect to one or more of the features reflecting pyruvate metabolism. This conclusion is further supported here by results of steady state and dynamic analyses. The tricarboxylic acid cycle, according to the current model, is poised on a knife's edge with its behavior rigidly determined; any alteration of the system's components leads to nonviable behavior, as exemplified by explosive accumulation of pyruvate and loss of steady state in response to a minute change in the level of malate dehydrogenase. With the additional results in this paper, we are able to refine the diagnosis of the problem and suggest three different areas of the current model that might profitably be re-examined by experiment. These include the kinetics of the reactions at the malate branch point, the turnover times for the alanine, glutamate, and aspartate pools in vivo, and the dynamic mass balances for the cofactor NAD. We also suggest a minimal modification in the current model that could alleviate or circumvent some of these problems.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 22926-22933 |
| ページ数 | 8 |
| ジャーナル | Journal of Biological Chemistry |
| 巻 | 267 |
| 発行部数 | 32 |
| 出版物ステータス | 出版済み - 1 1 1992 |
| 外部発表 | Yes |
Fingerprint
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
これを引用
The tricarboxylic acid cycle in Dictyostelium discoideum. III. Analysis of steady state and dynamic behavior. / Shiraishi, F.; Savageau, M. A.
：: Journal of Biological Chemistry, 巻 267, 番号 32, 01.01.1992, p. 22926-22933.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - The tricarboxylic acid cycle in Dictyostelium discoideum. III. Analysis of steady state and dynamic behavior
AU - Shiraishi, F.
AU - Savageau, M. A.
PY - 1992/1/1
Y1 - 1992/1/1
N2 - The examination of model robustness in the previous paper (Shiraishi, F., and Savageau, M. A. (1992) J. Biol. Chem. 267, 22919-22925 led to the suggestion that the current model for the tricarboxylic acid cycle in Dictyostelium discoideum is ill-determined with respect to one or more of the features reflecting pyruvate metabolism. This conclusion is further supported here by results of steady state and dynamic analyses. The tricarboxylic acid cycle, according to the current model, is poised on a knife's edge with its behavior rigidly determined; any alteration of the system's components leads to nonviable behavior, as exemplified by explosive accumulation of pyruvate and loss of steady state in response to a minute change in the level of malate dehydrogenase. With the additional results in this paper, we are able to refine the diagnosis of the problem and suggest three different areas of the current model that might profitably be re-examined by experiment. These include the kinetics of the reactions at the malate branch point, the turnover times for the alanine, glutamate, and aspartate pools in vivo, and the dynamic mass balances for the cofactor NAD. We also suggest a minimal modification in the current model that could alleviate or circumvent some of these problems.
AB - The examination of model robustness in the previous paper (Shiraishi, F., and Savageau, M. A. (1992) J. Biol. Chem. 267, 22919-22925 led to the suggestion that the current model for the tricarboxylic acid cycle in Dictyostelium discoideum is ill-determined with respect to one or more of the features reflecting pyruvate metabolism. This conclusion is further supported here by results of steady state and dynamic analyses. The tricarboxylic acid cycle, according to the current model, is poised on a knife's edge with its behavior rigidly determined; any alteration of the system's components leads to nonviable behavior, as exemplified by explosive accumulation of pyruvate and loss of steady state in response to a minute change in the level of malate dehydrogenase. With the additional results in this paper, we are able to refine the diagnosis of the problem and suggest three different areas of the current model that might profitably be re-examined by experiment. These include the kinetics of the reactions at the malate branch point, the turnover times for the alanine, glutamate, and aspartate pools in vivo, and the dynamic mass balances for the cofactor NAD. We also suggest a minimal modification in the current model that could alleviate or circumvent some of these problems.
UR - http://www.scopus.com/inward/record.url?scp=0026470976&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026470976&partnerID=8YFLogxK
M3 - Article
C2 - 1429643
AN - SCOPUS:0026470976
VL - 267
SP - 22926
EP - 22933
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 32
ER -