Allosteric Transitions of Glutamate Dehydrogenase

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1968 English Publisher:Springer Science and Business Media LLCJournal:Nature, volume 219, pages 947-949 (issn: 0028-0836, eissn: 1476-4687,

Copyright policy )

Authors: A D, Malcolm; G K, Radda;

doi: 10.1038/219947a0

pmid: 5673010

Allosteric Transitions of Glutamate Dehydrogenase

- Summary
- Subjects
- Metrics

Abstract

L-GLUTAMATE dehydrogenase from beef liver, GDH (EC 1.4.1.3), has a molecular weight of 310,000 (referred to as the oligomer) consisting of six identical subunits1 and six active sites2.

Related Organizations

University of Oxford
United Kingdom

Keywords

Kinetics, Binding Sites, Glutamate Dehydrogenase, Models, Chemical, Salicylamides, Guanine Nucleotides

Impact byBIP!

	selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	27
	popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.	Average
	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 10%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 10%