Propanediol dehydratase system. Role of monovalent cations in binding of vitamin B12 coenzyme or its analogs to apoenzyme
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPropanediol dehydratase system. Role of monovalent cations in binding of vitamin B12 coenzyme or its analogs to apoenzymeTetsuo Toraya, Yoshikazu Sugimoto, Yoshikuni Tamao, Shoichi Shimizu, and Saburo FukuiCite this: Biochemistry 1971, 10, 18, 3475–3484Publication Date (Print):August 1, 1971Publication History Published online1 May 2002Published inissue 1 August 1971https://pubs.acs.org/doi/10.1021/bi00794a025https://doi.org/10.1021/bi00794a025research-articleACS PublicationsRequest reuse permissionsArticle Views115Altmetric-Citations60LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore…
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Propanediol dehydratase is activated by K+ with a KM of 0.6 mM.
“For example, propanediol dehydratase is activated by K+ with a KM of 0.6 mM,59 well below the level of the free K+ pool.”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [59]
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Metals in Motion: Understanding Labile Metal Pools in Bacteria
Helmann, J. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00726 · Cited by 49 · see citing works
- Authors
- Toraya, T., Sugimoto, Y., Tamao, Y., Shimizu, S., & Fukui, S.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1971-08-01
- Volume
- 10
- Issue
- 18
- Pages
- 3475-3484
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2050077565
- Cited by
- 70
- References
- 0
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 2 · 2018: 2 · 2017: 1 · 2016: 2 · 2014: 1 · 2013: 1
- FWCI
- 2.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Health Sciences › Medicine › Rheumatology › Folate and B Vitamins Research
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- vitamin B12 coenzyme, apoenzyme, monovalent cations, substrate binding
- MeSH terms
- Quaternary Ammonium Compounds, Binding Sites, Cesium, Chemistry, Physical, Chloromercuribenzoates, Chromatography, Gel, Coenzymes, Deoxyadenosines, Enterobacter, Enzyme Activation, Ethylamines, Hydro-Lyases, Hydroxocobalamin, Kinetics, Lithium, Mathematics, Methylamines, Methylation, Models, Biological, Oxygen, Phosphates, Potassium Chloride, Propylene Glycols, Protein Binding, Rubidium, Sodium, Spectrophotometry, Tromethamine, Vitamin B 12, Chemical Phenomena
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