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Cited by 903

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Adenosine Triphosphate Conservation in Metabolic Regulation

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Atkinson, Daniel E., Walton, Gordon M.·1967·Journal of Biological Chemistry

Abstract

Abstract The citrate cleavage enzyme (EC 4.1.3.8) of rat liver is inhibited by adenosine diphosphate, which appears to compete with adenosine triphosphate. This effect may ensure that fatty acids are produced only when the ATP level is high. The of the adenylate system, defined as (ATP + ½ ADP)/(AMP + ADP + ATP), is proposed as a fundamental metabolic control parameter. Enzymes that utilize ATP and are inhibited by ADP or AMP will yield steep curves of velocity as a function of energy charge (resembling the steep curves of velocity as a function of substrate concentration that are characteristic of many regulatory enzymes) even in the absence of multiple sites and cooperative binding.

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Metadata

Authors
Atkinson, D. E., & Walton, G. M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1967-07
Volume
242
Issue
13
Pages
3239-3241
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1587804137
Cited by
903
References
0
FWCI
12.03
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Adenosine Triphosphate Conservation in Metabolic Regulation. https://app.cochat.ai/papers/10.1016/s0021-9258(18)95956-9
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Atkinson, D. E., & Walton, G. M. (1967). Adenosine Triphosphate Conservation in Metabolic Regulation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)95956-9

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.