Atkinson 1967 J Biol Chem: Difference between revisions
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|year=1967 | |year=1967 | ||
|journal=J Biol Chem | |journal=J Biol Chem | ||
|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 | |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 β[[energy charge]]β of the adenylate system, defined as (ATP + Β½ 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. | ||
|keywords=Energy charge | |keywords=[[Energy charge]] | ||
|editor=Gnaiger E | |editor=Gnaiger E | ||
}} | }} | ||
== Discussion == | |||
::::* Controversy: https://www.sciencedirect.com/science/article/abs/pii/0968000477901906 | |||
{{Labeling | {{Labeling | ||
|organism=Rat | |organism=Rat |
Latest revision as of 11:43, 29 March 2021
Atkinson DE, Walton GM (1967) Adenosine triphosphate conservation in metabolic regulation. Rat liver citrate cleavage enzyme. J Biol Chem 242:3239-41. |
Atkinson DE, Walton GM (1967) J Biol Chem
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 βenergy chargeβ of the adenylate system, defined as (ATP + Β½ 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. β’ Keywords: Energy charge β’ Bioblast editor: Gnaiger E
Discussion
Labels:
Organism: Rat
Tissue;cell: Liver
Preparation: Enzyme
Regulation: ADP, ATP, AMP