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1. Open Source Drug Discovery with the Malaria Box Compound Collection for Neglected Diseases and Beyond.

Author

Wesley C Van Voorhis, John H Adams, Roberto Adelfio, Vida Ahyong, Myles H Akabas, Pietro Alano, Aintzane Alday, Yesmalie Alemán Resto, Aishah Alsibaee, Ainhoa Alzualde, Katherine T Andrews, Simon V Avery, Vicky M Avery, Lawrence Ayong, Mark Baker, Stephen Baker, Choukri Ben Mamoun, Sangeeta Bhatia, Quentin Bickle, Lotfi Bounaadja, Tana Bowling, Jürgen Bosch, Lauren E Boucher, Fabrice F Boyom, Jose Brea, Marian Brennan, Audrey Burton, Conor R Caffrey, Grazia Camarda, Manuela Carrasquilla, Dee Carter, Maria Belen Cassera, Ken Chih-Chien Cheng, Worathad Chindaudomsate, Anthony Chubb, Beatrice L Colon, Daisy D Colón-López, Yolanda Corbett, Gregory J Crowther, Noemi Cowan, Sarah D'Alessandro, Na Le Dang, Michael Delves, Joseph L DeRisi, Alan Y Du, Sandra Duffy, Shimaa Abd El-Salam El-Sayed, Michael T Ferdig, José A Fernández Robledo, David A Fidock, Isabelle Florent, Patrick V T Fokou, Ani Galstian, Francisco Javier Gamo, Suzanne Gokool, Ben Gold, Todd Golub, Gregory M Goldgof, Rajarshi Guha, W Armand Guiguemde, Nil Gural, R Kiplin Guy, Michael A E Hansen, Kirsten K Hanson, Andrew Hemphill, Rob Hooft van Huijsduijnen, Takaaki Horii, Paul Horrocks, Tyler B Hughes, Christopher Huston, Ikuo Igarashi, Katrin Ingram-Sieber, Maurice A Itoe, Ajit Jadhav, Amornrat Naranuntarat Jensen, Laran T Jensen, Rays H Y Jiang, Annette Kaiser, Jennifer Keiser, Thomas Ketas, Sebastien Kicka, Sunyoung Kim, Kiaran Kirk, Vidya P Kumar, Dennis E Kyle, Maria Jose Lafuente, Scott Landfear, Nathan Lee, Sukjun Lee, Adele M Lehane, Fengwu Li, David Little, Liqiong Liu, Manuel Llinás, Maria I Loza, Aristea Lubar, Leonardo Lucantoni, Isabelle Lucet, Louis Maes, Dalu Mancama, Nuha R Mansour, Sandra March, Sheena McGowan, Iset Medina Vera, Stephan Meister, Luke Mercer, Jordi Mestres, Alvine N Mfopa, Raj N Misra, Seunghyun Moon, John P Moore, Francielly Morais Rodrigues da Costa, Joachim Müller, Arantza Muriana, Stephen Nakazawa Hewitt, Bakela Nare, Carl Nathan, Nathalie Narraidoo, Sujeevi Nawaratna, Kayode K Ojo, Diana Ortiz, Gordana Panic, George Papadatos, Silvia Parapini, Kailash Patra, Ngoc Pham, Sarah Prats, David M Plouffe, Sally-Ann Poulsen, Anupam Pradhan, Celia Quevedo, Ronald J Quinn, Christopher A Rice, Mohamed Abdo Rizk, Andrea Ruecker, Robert St Onge, Rafaela Salgado Ferreira, Jasmeet Samra, Natalie G Robinett, Ulrich Schlecht, Marjorie Schmitt, Filipe Silva Villela, Francesco Silvestrini, Robert Sinden, Dennis A Smith, Thierry Soldati, Andreas Spitzmüller, Serge Maximilian Stamm, David J Sullivan, William Sullivan, Sundari Suresh, Brian M Suzuki, Yo Suzuki, S Joshua Swamidass, Donatella Taramelli, Lauve R Y Tchokouaha, Anjo Theron, David Thomas, Kathryn F Tonissen, Simon Townson, Abhai K Tripathi, Valentin Trofimov, Kenneth O Udenze, Imran Ullah, Cindy Vallieres, Edgar Vigil, Joseph M Vinetz, Phat Voong Vinh, Hoan Vu, Nao-Aki Watanabe, Kate Weatherby, Pamela M White, Andrew F Wilks, Elizabeth A Winzeler, Edward Wojcik, Melanie Wree, Wesley Wu, Naoaki Yokoyama, Paul H A Zollo, Nada Abla, Benjamin Blasco, Jeremy Burrows, Benoît Laleu, Didier Leroy, Thomas Spangenberg, Timothy Wells, and Paul A Willis

Subjects
Immunologic diseases. Allergy, RC581-607, Biology (General), QH301-705.5
Abstract

A major cause of the paucity of new starting points for drug discovery is the lack of interaction between academia and industry. Much of the global resource in biology is present in universities, whereas the focus of medicinal chemistry is still largely within industry. Open source drug discovery, with sharing of information, is clearly a first step towards overcoming this gap. But the interface could especially be bridged through a scale-up of open sharing of physical compounds, which would accelerate the finding of new starting points for drug discovery. The Medicines for Malaria Venture Malaria Box is a collection of over 400 compounds representing families of structures identified in phenotypic screens of pharmaceutical and academic libraries against the Plasmodium falciparum malaria parasite. The set has now been distributed to almost 200 research groups globally in the last two years, with the only stipulation that information from the screens is deposited in the public domain. This paper reports for the first time on 236 screens that have been carried out against the Malaria Box and compares these results with 55 assays that were previously published, in a format that allows a meta-analysis of the combined dataset. The combined biochemical and cellular assays presented here suggest mechanisms of action for 135 (34%) of the compounds active in killing multiple life-cycle stages of the malaria parasite, including asexual blood, liver, gametocyte, gametes and insect ookinete stages. In addition, many compounds demonstrated activity against other pathogens, showing hits in assays with 16 protozoa, 7 helminths, 9 bacterial and mycobacterial species, the dengue fever mosquito vector, and the NCI60 human cancer cell line panel of 60 human tumor cell lines. Toxicological, pharmacokinetic and metabolic properties were collected on all the compounds, assisting in the selection of the most promising candidates for murine proof-of-concept experiments and medicinal chemistry programs. The data for all of these assays are presented and analyzed to show how outstanding leads for many indications can be selected. These results reveal the immense potential for translating the dispersed expertise in biological assays involving human pathogens into drug discovery starting points, by providing open access to new families of molecules, and emphasize how a small additional investment made to help acquire and distribute compounds, and sharing the data, can catalyze drug discovery for dozens of different indications. Another lesson is that when multiple screens from different groups are run on the same library, results can be integrated quickly to select the most valuable starting points for subsequent medicinal chemistry efforts.

Published
2016
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2. Collaborative Virtual Screening Identifies a 2-Aryl-4-aminoquinazoline Series with Efficacy in an In Vivo Model of Trypanosoma cruzi Infection

Author

Taisuke Tawaraishi, Atsuko Ochida, Yuichiro Akao, Sachiko Itono, Masahiro Kamaura, Thamina Akther, Mitsuyuki Shimada, Stacie Canan, Sanjoy Chowdhury, Yafeng Cao, Kevin Condroski, Ola Engkvist, Amanda Francisco, Sunil Ghosh, Rina Kaki, John M. Kelly, Chiaki Kimura, Thierry Kogej, Kazuya Nagaoka, Akira Naito, Garry Pairaudeau, Constantin Radu, Ieuan Roberts, David Shum, Nao-aki Watanabe, Huanxu Xie, Shuji Yonezawa, Osamu Yoshida, Ryu Yoshida, Charles Mowbray, and Benjamin Perry

Subjects
Drug Discovery, Molecular Medicine
Published
2023
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3. Open Source Drug Discovery with the Malaria Box Compound Collection for Neglected Diseases and Beyond

Author

Christopher D. Huston, Amornrat Naranuntarat Jensen, Louis Maes, Jordi Mestres, Nao Aki Watanabe, Michael Adsetts Edberg Hansen, Roberto Adelfio, Simon Townson, Didier Leroy, Kate Weatherby, Thomas Spangenberg, Manuela Carrasquilla, Kailash P. Patra, Robert E. Sinden, José Brea, Abhai K. Tripathi, W. Armand Guiguemde, Alan Y. Du, Melanie Wree, Katherine T. Andrews, Kirsten K. Hanson, Tyler B. Hughes, Sundari Suresh, Adele M. Lehane, Sangeeta N. Bhatia, Edward J. Wojcik, Andrew Hemphill, Francielly Morais Rodrigues da Costa, Worathad Chindaudomsate, Joseph M. Vinetz, Ben Gold, Sunyoung Kim, Edgar Vigil, Nuha R. Mansour, Mohamed Abdo Rizk, Patrick Valere Tsouh Fokou, Audrey Burton, Laran T. Jensen, David A. Fidock, Aishah Alsibaee, Filipe Silva Villela, Yesmalie Alemán Resto, Rajarshi Guha, Conor R. Caffrey, José A. Fernández Robledo, Thomas J. Ketas, Luke Mercer, Rob Hooft van Huijsduijnen, Maria Jose Lafuente, Wesley C. Van Voorhis, Lauve R. Y. Tchokouaha, Dee A. Carter, Anjo Theron, Benoît Laleu, Kiaran Kirk, Maurice A. Itoe, Robert P. St.Onge, Celia Quevedo, Andrea Ruecker, Paul Henri Amvam Zollo, Francisco-Javier Gamo, Nathan Lee, Alvine Ngoutane Mfopa, Paul Horrocks, Ikuo Igarashi, Nil Gural, Todd R. Golub, Gordana Panic, Jeremy N. Burrows, Phat Voong Vinh, Annette Kaiser, Fabrice Fekam Boyom, Pietro Alano, Anupam Pradhan, Sandra Duffy, Raj N. Misra, Vidya Prasanna Kumar, Aintzane Alday, Timothy N. C. Wells, María Isabel Loza, Sébastien Kicka, William J. Sullivan, Gregory M. Goldgof, Yo Suzuki, Yolanda Corbett, Sally-Ann Poulsen, Vida Ahyong, George Papadatos, Sujeevi Nawaratna, Rafaela Salgado Ferreira, Takaaki Horii, Imran Ullah, Nathalie Narraidoo, Natalie G. Robinett, Simon V. Avery, Grazia Camarda, Iset Medina Vera, Michael T. Ferdig, Fengwu Li, David Plouffe, Joseph L. DeRisi, Jasmeet Samra, Andreas Spitzmüller, Liqiong Liu, Christopher A. Rice, Thierry Soldati, Serge Maximilian Stamm, Suzanne Gokool, Beatrice L. Colon, Shimaa Abd El-Salam El-Sayed, Mark Baker, Kenneth O. Udenze, Na Le Dang, Katrin Ingram-Sieber, Dennis A. Smith, Rays H. Y. Jiang, Marian P. Brennan, Ani Galstian, Paul Willis, Dennis E. Kyle, Ainhoa Alzualde, Sarah Prats, Sheena McGowan, Vicky M. Avery, Jennifer Keiser, John P. Moore, Dalu Mancama, Gregory J. Crowther, Noemi Cowan, Maria B. Cassera, Valentin Trofimov, David Thomas, David J. Sullivan, Diana Ortiz, Nada Abla, S. Joshua Swamidass, Benjamin Blasco, Hoan Vu, Francesco Silvestrini, Anthony J. Chubb, Pamela M. White, Scott M. Landfear, Isabelle Florent, John H. Adams, Ronald J. Quinn, Andrew F. Wilks, Sandra March, Leonardo Lucantoni, Stephen Baker, Tana Bowling, Joachim Müller, Arantza Muriana, Lauren E. Boucher, Ajit Jadhav, Sukjun Lee, Elizabeth A. Winzeler, Choukri Ben Mamoun, Ulrich Schlecht, Daisy D. Colón-López, Marjorie Schmitt, Myles H. Akabas, Isabelle S Lucet, Stephen N. Hewitt, Naoaki Yokoyama, Carl Nathan, Bakela Nare, Cindy Vallières, Lotfi Bounaadja, Kayode K. Ojo, Wesley Wu, Ken Chih-Chien Cheng, Kathryn F. Tonissen, Michael J. Delves, Brian M. Suzuki, Aristea Lubar, Quentin D. Bickle, Stephan Meister, Silvia Parapini, Manuel Llinás, Ngoc Minh Pham, Seunghyun Moon, R. Kiplin Guy, Donatella Taramelli, Lawrence Ayong, Sarah D'Alessandro, Jürgen Bosch, David Little, Istituto Superiore di Sanita [Rome], Zentrum für Infektiologie [Heidelberg, Germany], Universität Heidelberg [Heidelberg]-Heidelberg University Hospital [Heidelberg], University of Nottingham, UK (UON), Eskitis Institute for Drug Discovery, Griffith University [Brisbane], Institut Pasteur Korea - Institut Pasteur de Corée, Réseau International des Instituts Pasteur (RIIP), Oxford University Clinical Research Unit [Ho Chi Minh City] (OUCRU), Laboratoire de génétique moléculaire et cellulaire, Institut National de la Recherche Agronomique (INRA), Agence Française de Sécurité Sanitaire des Aliments (AFSSA), Faculté des Sciences - Yaoundé I, Université de Yaoundé I, Skaggs School of Pharmacy and Pharmaceutical Sciences [San Diego], University of California [San Diego] (UC San Diego), University of California-University of California, Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Università degli Studi di Milano [Milano] (UNIMI), Imperial College London, Eck Institute for Global Health, University of Notre Dame [Indiana] (UND), Columbia University Medical Center (CUMC), Columbia University [New York], Interdisciplinary Nanoscience Centre (iNANO), Institute of Parasitology, University of Bern, MS Project - Initiation (MSPRI), Apollo SSC Genève, Keele University, Swiss Tropical and Public Health Institute [Basel], University of Regina, School of Engineering and Science, University of the West of Scotland (UWS), Research School of Biology [Canberra, Australie], Australian National University (ANU), University of Pennsylvania [Philadelphia], Laboratory of Microbiology, Parasitology and Hygiene [Antwerpen] (LMPH), University of Antwerp (UA), Department of Biochemistry and Molecular Biology, Mayo Clinic, Institute for Wine Biotechnology [University of Stellenbosch - Afrique du Sud], Stellenbosch University, Oregon Health and Science University [Portland] (OHSU), Biozentrum, Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL)-Université de Lausanne (UNIL), Laboratoire d'innovation moléculaire et applications (LIMA), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Advanced Materials Research Laboratories, Department of Chemistry and Center for Optical ((COMSET), Clemson University, Université de Genève (UNIGE), Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, University of California [Santa Cruz] (UCSC), Department of sanità pubblica-microbiologia-virologia, University of California, Département Réseaux, Information, Multimédia (RIM-ENSMSE), École des Mines de Saint-Étienne (Mines Saint-Étienne MSE), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Centre G2I, UC San Diego School of Medicine, Medicines for Malaria Venture [Geneva] (MMV), Princeton University, Institute for Medical Engineering and Science, Harvard University--MIT Division of Health Sciences and Technology, Bhatia, Sangeeta N, Bill & Melinda Gates Foundation, Biochemistry, Center for Drug Discovery, Kicka, Sébastien, Soldati, Thierry, Trofimov, Valentin, and Abla, Nada

Subjects
0301 basic medicine, Plasmodium, [SDV]Life Sciences [q-bio], Medizin, Drug Evaluation, Preclinical, Datasets as Topic, infected erythrocytes, stage plasmodium-falciparum, Q1, Gametocytes, Toxicology, Pathology and Laboratory Medicine, Drug Metabolism, 1108 Medical Microbiology, Animal Cells, inhibitors, Drug Discovery, Medicine and Health Sciences, Biology (General), Genetics, Protozoans, biology, 630 Agriculture, Drug discovery, transmission, Malarial Parasites, Neglected Diseases, 3. Good health, Chemistry, 1107 Immunology, ddc:540, Physical Sciences, 590 Animals (Zoology), Identification (biology), Cellular Types, Medicaments, 0605 Microbiology, Research Article, Drug Research and Development, QH301-705.5, Immunology, Computational biology, in-vitro, Microbiology, target, Small Molecule Libraries, 03 medical and health sciences, Antimalarials, blood, Virology, Parasite Groups, Gametocyte, medicine, Parasitic Diseases, [CHIM]Chemical Sciences, Humans, Pharmacokinetics, Molecular Biology, Biology, theileria parasites, Pharmacology, Toxicity, QH, Malària -- Medicaments, Organisms, Biology and Life Sciences, Plasmodium falciparum, Cell Biology, RC581-607, biology.organism_classification, medicine.disease, Tropical Diseases, Parasitic Protozoans, babesia, Malaria, 030104 developmental biology, Germ Cells, Vector (epidemiology), identification, 570 Life sciences, Parasitology, Human medicine, Medicinal Chemistry, Immunologic diseases. Allergy, Apicomplexa
Abstract

A major cause of the paucity of new starting points for drug discovery is the lack of interaction between academia and industry. Much of the global resource in biology is present in universities, whereas the focus of medicinal chemistry is still largely within industry. Open source drug discovery, with sharing of information, is clearly a first step towards overcoming this gap. But the interface could especially be bridged through a scale-up of open sharing of physical compounds, which would accelerate the finding of new starting points for drug discovery. The Medicines for Malaria Venture Malaria Box is a collection of over 400 compounds representing families of structures identified in phenotypic screens of pharmaceutical and academic libraries against the Plasmodium falciparum malaria parasite. The set has now been distributed to almost 200 research groups globally in the last two years, with the only stipulation that information from the screens is deposited in the public domain. This paper reports for the first time on 236 screens that have been carried out against the Malaria Box and compares these results with 55 assays that were previously published, in a format that allows a meta-analysis of the combined dataset. The combined biochemical and cellular assays presented here suggest mechanisms of action for 135 (34%) of the compounds active in killing multiple life-cycle stages of the malaria parasite, including asexual blood, liver, gametocyte, gametes and insect ookinete stages. In addition, many compounds demonstrated activity against other pathogens, showing hits in assays with 16 protozoa, 7 helminths, 9 bacterial and mycobacterial species, the dengue fever mosquito vector, and the NCI60 human cancer cell line panel of 60 human tumor cell lines. Toxicological, pharmacokinetic and metabolic properties were collected on all the compounds, assisting in the selection of the most promising candidates for murine proof-of-concept experiments and medicinal chemistry programs. The data for all of these assays are presented and analyzed to show how outstanding leads for many indications can be selected. These results reveal the immense potential for translating the dispersed expertise in biological assays involving human pathogens into drug discovery starting points, by providing open access to new families of molecules, and emphasize how a small additional investment made to help acquire and distribute compounds, and sharing the data, can catalyze drug discovery for dozens of different indications. Another lesson is that when multiple screens from different groups are run on the same library, results can be integrated quickly to select the most valuable starting points for subsequent medicinal chemistry efforts., Author Summary Malaria leads to the loss of over 440,000 lives annually; accelerating research to discover new candidate drugs is a priority. Medicines for Malaria Venture (MMV) has distilled over 25,000 compounds that kill malaria parasites in vitro into a group of 400 representative compounds, called the "Malaria Box". These Malaria Box sets were distributed free-of-charge to research laboratories in 30 different countries that work on a wide variety of pathogens. Fifty-five groups compiled >290 assay results for this paper describing the many activities of the Malaria Box compounds. The collective results suggest a potential mechanism of action for over 130 compounds against malaria and illuminate the most promising compounds for further malaria drug development research. Excitingly some of these compounds also showed outstanding activity against other disease agents including fungi, bacteria, other single-cellular parasites, worms, and even human cancer cells. The results have ignited over 30 drug development programs for a variety of diseases. This open access effort was so successful that MMV has begun to distribute another set of compounds with initial activity against a wider range of infectious agents that are of public health concern, called the Pathogen Box, available now to scientific labs all over the world (www.PathogenBox.org).

Published
2016
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4. Medicinal genetics approach towards identifying the molecular target of a novel inhibitor of fungal cell wall assembly

Author

Kappei, Tsukahara, Katsura, Hata, Kazutaka, Nakamoto, Koji, Sagane, Nao-Aki, Watanabe, Junro, Kuromitsu, Junko, Kai, Mamiko, Tsuchiya, Fuminori, Ohba, Yoshifumi, Jigami, Kentaro, Yoshimatsu, and Takeshi, Nagasu

Subjects
Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Cell Wall, Glycosylphosphatidylinositols, Candida albicans, Molecular Sequence Data, Cell Adhesion, Amino Acid Sequence, Isoquinolines, Inositol
Abstract

Glycosylphosphatidylinositol (GPI)-anchored cell wall mannoproteins are required for the adhesion of pathogenic fungi, such as Candida albicans, to human epithelium. Small molecular inhibitors of the cell surface presentation of GPI-anchored mannoproteins would be promising candidate drugs to block the establishment of fungal infections. Here, we describe a medicinal genetics approach to identifying the gene encoding a novel target protein that is required for the localization of GPI-anchored cell wall mannoproteins. By means of a yeast cell-based screening procedure, we discovered a compound, 1-[4-butylbenzyl]isoquinoline (BIQ), that inhibits cell wall localization of GPI-anchored mannoproteins in Saccharomyces cerevisiae. Treatment of C. albicans cells with this compound resulted in reduced adherence to a rat intestine epithelial cell monolayer. A previously uncharacterized gene YJL091c, named GWT1, was cloned as a dosage-dependent suppressor of the BIQ-induced phenotypes. GWT1 knock-out cells showed similar phenotypes to BIQ-treated wild-type cells in terms of cell wall structure and transcriptional profiles. Two different mutants resistant to BIQ each contained a single missense mutation in the coding region of the GWT1 gene. These results all suggest that the GWT1 gene product is the primary target of the compound.

Published
2003

5. Activation and cleavage of the carbon-cobalt bond of adeninylethylcobalamin by diol dehydrase

Author

Kazutoshi Ushio, Masakazu Ichikawa, Nao-aki Watanabe, Takeshi Matsumoto, Tetsuo Toraya, and Saburo Fukui

Subjects
Magnetic Resonance Spectroscopy, Propanediol Dehydratase, Stereochemistry, Propanediol dehydratase, Cleavage (embryo), Photochemistry, Biochemistry, Heterolysis, medicine, Molecular Biology, Bond cleavage, Hydro-Lyases, Carbanion, Chemistry, Adenine, Cell Biology, Adenosylcobalamin, Homolysis, Kinetics, Klebsiella pneumoniae, Vitamin B 12, Covalent bond, Spectrophotometry, Indicators and Reagents, Chromatography, Thin Layer, medicine.drug
Abstract

Adeninylethylcobalamin (AdeEtCbl) underwent cleavage of the C-Co bond by interaction with apoprotein of diol dehydrase from Klebsiella pneumoniae ATCC 8724, although this analog was quite inactive as coenzyme. Spectroscopic observation indicates that AdeEtCbl was converted to the enzyme-bound hydroxocobalamin without intermediates. The conversion was stoichiometric (1:1) and obeyed the second-order reaction kinetics (k = 0.027 min-1 microM-1 at 37 degrees C) depending upon concentrations of apoprotein and AdeEtCbl. This suggests that the complex formation is the rate-determining step and that AdeEtCbl undergoes rapid C-Co bond cleavage once it binds to the apoenzyme. Substrates and oxygen did apparently not affect the rate of the C-Co bond cleavage. The experiments using [adenine-U-14C]AdeEtCbl and [1(3)-3H]glycerol demonstrated that 9-ethyladenine was the only product formed from the adeninylethyl group of AdeEtCbl during the conversion and that an additional hydrogen atom in the 9-ethyladenine is not derived from the substrate. 1H NMR measurement of the 9-ethyladenine formed enzymatically from AdeEtCbl and DL-1,2-[1,1,2-2H3]propanediol also led to the same conclusion. All of these results indicate that the C-Co bond of AdeEtCbl is activated by diol dehydrase and undergoes heterolysis forming Co(III) and a carbanion or a carbanion-like species, in clear contrast to the homolysis of the C-Co bond of adenosylcobalamin in the normal catalytic process. 9-Ethyladenine formed remained tightly associated with the enzyme. Longer chain homologs, i.e. adeninylpropylcobalamin, adeninylbutylcobalamin, and adeninylpentylcobalamin did not undergo such cleavage of the C-Co bond by diol dehydrase.

Published
1987

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