抄録
The amplification of a substrate cycle system with reversible closed reaction of two substrates was represented by mathematical equations. The results are summarized as follows: the amplification was affected especially by the affinity of enzyme and substrate, by the rate constant in rate‐limiting reaction step, and by the saturation degree of enzyme by substrate. These amplifications were not simply determined by the values of Km and Vmax, because each rate parameter in the system can affect the degree of amplification independently. The conclusion is that the “apparent” equilibrium constant of this system cannot be uniquely estimated from only data of Km and Vmax even if the reaction occurs in a closed system.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 132-136 |
| ページ数 | 5 |
| ジャーナル | Biotechnology and Bioengineering |
| 巻 | 27 |
| 発行部数 | 2 |
| DOI | |
| 出版物ステータス | 出版済み - 2 1985 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
これを引用
Kinetic characteristics of biochemical cyclic reaction systems : Amplification of substrate cycle system. / Okamoto, Masahiro; Hayashi, Katsuya.
：: Biotechnology and Bioengineering, 巻 27, 番号 2, 02.1985, p. 132-136.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Kinetic characteristics of biochemical cyclic reaction systems
T2 - Amplification of substrate cycle system
AU - Okamoto, Masahiro
AU - Hayashi, Katsuya
PY - 1985/2
Y1 - 1985/2
N2 - The amplification of a substrate cycle system with reversible closed reaction of two substrates was represented by mathematical equations. The results are summarized as follows: the amplification was affected especially by the affinity of enzyme and substrate, by the rate constant in rate‐limiting reaction step, and by the saturation degree of enzyme by substrate. These amplifications were not simply determined by the values of Km and Vmax, because each rate parameter in the system can affect the degree of amplification independently. The conclusion is that the “apparent” equilibrium constant of this system cannot be uniquely estimated from only data of Km and Vmax even if the reaction occurs in a closed system.
AB - The amplification of a substrate cycle system with reversible closed reaction of two substrates was represented by mathematical equations. The results are summarized as follows: the amplification was affected especially by the affinity of enzyme and substrate, by the rate constant in rate‐limiting reaction step, and by the saturation degree of enzyme by substrate. These amplifications were not simply determined by the values of Km and Vmax, because each rate parameter in the system can affect the degree of amplification independently. The conclusion is that the “apparent” equilibrium constant of this system cannot be uniquely estimated from only data of Km and Vmax even if the reaction occurs in a closed system.
UR - http://www.scopus.com/inward/record.url?scp=0022012737&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022012737&partnerID=8YFLogxK
U2 - 10.1002/bit.260270205
DO - 10.1002/bit.260270205
M3 - Article
AN - SCOPUS:0022012737
VL - 27
SP - 132
EP - 136
JO - Biotechnology and Bioengineering
JF - Biotechnology and Bioengineering
SN - 0006-3592
IS - 2
ER -