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Journal of Theoretical Biology

Volumn 183, Issue 2, 1996, Pages 179-183

A new approach for determination of the selectively favoured kinetic design of enzyme reactions

(1) Pettersson, Gösta a

a LUND UNIVERSITY (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CONCENTRATION RESPONSE; ENZYME BINDING; ENZYME KINETICS; METABOLIC RATE; MICHAELIS MENTEN KINETICS; PRIORITY JOURNAL;

EID: 0030597334 PISSN: 00225193 EISSN: None Source Type: Journal
DOI: 10.1006/jtbi.1996.0211 Document Type: Article

Times cited : (7)

References (14)

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2
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3
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4
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- Cornish-Bowden, A.¹

5
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- Catalysis, binding and enzyme-substrate complementarity
- FERSHT, A. R. (1974). Catalysis, binding and enzyme-substrate complementarity. Proc. Roy. Soc. Ser. B. 187, 397-407.
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- Fersht, A.R.¹

6
- 0021782084
- Efficiency and design of simple metabolic systems
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7
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- Mathematical analysis of enzymic reaction systems using optimization principles
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- Heinrich, R.¹ Schuster, S.² Holzhütter, H.-G.³

8
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- A schematic method of deriving the rate laws for enzyme-catalyzed reactions
- KING, E. L. & ALTMAN, C. (1956). A schematic method of deriving the rate laws for enzyme-catalyzed reactions. J. Phys. Chem. 60, 1375-1378.
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9
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- Evolutionary optimization of enzyme kinetic parameters; Effect of constraints
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10
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- Perfection in enzyme catalysis: The energetics of triosephosphate isomerase
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11
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13
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14
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.