Macromolecular compartmentation and channeling - PubMed (original) (raw)
Review
Macromolecular compartmentation and channeling
J Ovádi et al. Int Rev Cytol. 2000.
Abstract
One of the accepted characterizations of the living state is that it is complex to an extraordinary degree. Since our current understanding of the living condition is minimal and fragmentary, it is not surprising that our first descriptions are simplistic. However, in certain areas of metabolism, especially those that have been amenable to experimentation for the longest period of time, the simplistic explanations have been the most difficult to revise. For example, current texts of general biochemistry still view metabolism as occurring by a series of independent enzymes dispersed in a uniform aqueous environment. This notion has been shown to be deeply flawed by both experimental and theoretical considerations. Thus, there is ample evidence that, in many metabolic pathways, specific interactions between sequential enzymes occur as static and/or dynamic complexes. In addition, reversible interactions of enzymes with structural proteins and membranes is a common occurrence. The interactions of enzymes give rise to a higher level of complexity that must be accounted for when one wishes to understand the regulation of metabolism. One of the phenomena that occurs because of sequential enzyme interactions is the process of channeling. This article discusses enzyme interactions and channeling and summarizes experimental and theoretical results from a few well-studied examples.
Similar articles
- On the origin of intracellular compartmentation and organized metabolic systems.
Ovádi J, Saks V. Ovádi J, et al. Mol Cell Biochem. 2004 Jan-Feb;256-257(1-2):5-12. doi: 10.1023/b:mcbi.0000009855.14648.2c. Mol Cell Biochem. 2004. PMID: 14977166 Review. - Enzyme organization and the direction of metabolic flow: physicochemical considerations.
Westerhoff HV, Welch GR. Westerhoff HV, et al. Curr Top Cell Regul. 1992;33:361-90. doi: 10.1016/b978-0-12-152833-1.50026-5. Curr Top Cell Regul. 1992. PMID: 1499341 Review. No abstract available. - Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview.
Beeckmans S, Van Driessche E, Kanarek L. Beeckmans S, et al. J Mol Recognit. 1993 Dec;6(4):195-204. doi: 10.1002/jmr.300060408. J Mol Recognit. 1993. PMID: 7917415 Review. - [The formation of supramolecular complexes as the pathway in the regulation of glycolytic enzyme activity].
Lushchak VI. Lushchak VI. Ukr Biokhim Zh (1978). 1996 Mar-Apr;68(2):20-8. Ukr Biokhim Zh (1978). 1996. PMID: 9005655 Review. Ukrainian. - Enzyme-enzyme interactions as modulators of the metabolic flux through the citric acid cycle.
Beeckmans S, Kanarek L. Beeckmans S, et al. Biochem Soc Symp. 1987;54:163-172. Biochem Soc Symp. 1987. PMID: 3332992 Review.
Cited by
- Specific ATPases drive compartmentalized glycogen utilization in rat skeletal muscle.
Nielsen J, Dubillot P, Stausholm MH, Ørtenblad N. Nielsen J, et al. J Gen Physiol. 2022 Sep 5;154(9):e202113071. doi: 10.1085/jgp.202113071. Epub 2022 Jul 7. J Gen Physiol. 2022. PMID: 35796670 Free PMC article. - Enzyme Complexes of Ptr4CL and PtrHCT Modulate Co-enzyme A Ligation of Hydroxycinnamic Acids for Monolignol Biosynthesis in Populus trichocarpa.
Lin CY, Sun Y, Song J, Chen HC, Shi R, Yang C, Liu J, Tunlaya-Anukit S, Liu B, Loziuk PL, Williams CM, Muddiman DC, Lin YJ, Sederoff RR, Wang JP, Chiang VL. Lin CY, et al. Front Plant Sci. 2021 Oct 6;12:727932. doi: 10.3389/fpls.2021.727932. eCollection 2021. Front Plant Sci. 2021. PMID: 34691108 Free PMC article. - Lipid Droplet-Organelle Contact Sites as Hubs for Fatty Acid Metabolism, Trafficking, and Metabolic Channeling.
Renne MF, Hariri H. Renne MF, et al. Front Cell Dev Biol. 2021 Sep 14;9:726261. doi: 10.3389/fcell.2021.726261. eCollection 2021. Front Cell Dev Biol. 2021. PMID: 34595176 Free PMC article. Review. - Transcription-dependent confined diffusion of enzymes within subcellular spaces of the bacterial cytoplasm.
Rotter DAO, Heger C, Oviedo-Bocanegra LM, Graumann PL. Rotter DAO, et al. BMC Biol. 2021 Sep 2;19(1):183. doi: 10.1186/s12915-021-01083-4. BMC Biol. 2021. PMID: 34474681 Free PMC article. - A New Glycosyltransferase Enzyme from Family 91, UGT91P3, Is Responsible for the Final Glucosylation Step of Crocins in Saffron (Crocus sativus L.).
López-Jimenez AJ, Frusciante S, Niza E, Ahrazem O, Rubio-Moraga Á, Diretto G, Gómez-Gómez L. López-Jimenez AJ, et al. Int J Mol Sci. 2021 Aug 16;22(16):8815. doi: 10.3390/ijms22168815. Int J Mol Sci. 2021. PMID: 34445522 Free PMC article.