Functional and Phylogenetic Diversity of BSH and PVA Enzymes
Open accessAbstract
Bile salt hydrolase (BSH) and penicillin V acylase (PVA) are related enzymes that are classified as choloylglycine hydrolases (CGH). BSH enzymes have attracted significant interest for their ability to modulate the composition of the bile acid pool, alter bile acid signaling events mediated by the host bile acid receptors FXR and TGR5 and influence cholesterol homeostasis in the host, while PVA enzymes have been widely utilised in an industrial capacity in the production of semi-synthetic antibiotics. The similarities between BSH and PVA enzymes suggest common evolution of these enzymes and shared mechanisms for substrate binding and catalysis. Here, we compare BSH and PVA through analysis of the distribution, phylogeny and biochemistry of these microbial enzymes. The development of new annotation approaches based upon functional enzyme analyses and the potential implications of BSH enzymes for host health are discussed.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
BSH and PVA are evolutionary related enzymes with high similarity in the amino acid residues involved in their active site.
“BSH and PVA are evolutionary related enzymes with high similarity in terms of the amino acid residues involved in their active site [5, 84].”
From Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization (2026) · cites this paper as [84]
The Introduction and §3.2 describe BSH and PVA as likely evolutionarily related and report that five of six major catalytic residues are conserved. The active-site similarity is supported, but the claim states their evolutionary relationship as fact where the paper presents it as likely. Page numbers were not supplied. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Bacterial competition: surviving and thriving in the microbial jungle
Hibbing, M. E., Fuqua, C., Parsek, M. R., & Peterson, S. B. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2259 · Cited by 2,658 · see citing works
Bile acids induce energy expenditure by promoting intracellular thyroid hormone activation
Watanabe, M., Houten, S. M., Mataki, C., Christoffolete, M. A., Kim, B. W., Sato, H., Messaddeq, N., Harney, J. W., Ezaki, O., Kodama, T., et al. (2006) · Nature · doi:10.1038/nature04330 · Cited by 2,220 · see citing works
Bile Salt Hydrolase Activity in Probiotics
Begley, M., Hill, C., & Gahan, C. G. M. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.3.1729-1738.2006 · Cited by 1,187 · see citing works
Self-citationJones, B. V., Begley, M., Hill, C., Gahan, C. G. M., & Marchesi, J. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804437105 · Cited by 1,098 · see citing works
Self-citationBile acid signaling in metabolic disease and drug therapy
Li, T., & Chiang, J. Y. L. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.008201 · Cited by 935 · see citing works
Quorum quenching: role in nature and applied developments
Grandclément, C., Tannières, M., Moréra, S., Dessaux, Y., & Faure, D. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv038 · Cited by 708 · see citing works
Li, F., Jiang, C., Krausz, K. W., Li, Y., Albert, I., Hao, H., Fabre, K. M., Mitchell, J. B., Patterson, A. D., & Gonzalez, F. J. (2013) · Nature Communications · doi:10.1038/ncomms3384 · Cited by 705 · see citing works
Intestinal microbiome is related to lifetime antibiotic use in Finnish pre-school children
Korpela, K., Salonen, A., Virta, L. J., Kekkonen, R. A., Forslund, K., Bork, P., & de Vos, W. M. (2016) · Nature Communications · doi:10.1038/ncomms10410 · Cited by 698 · see citing works
A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
Brannigan, J. A., Dodson, G. G., Duggleby, H. J., Moody, P. C. E., Smith, J. L., Tomchick, D. R., & Murzin, A. G. (1995) · Nature · doi:10.1038/378416a0 · Cited by 622 · see citing works
Regulation of host weight gain and lipid metabolism by bacterial bile acid modification in the gut
Joyce, S. A., MacSharry, J., Casey, P. G., Kinsella, M., Murphy, E. F., Shanahan, F., Hill, C., & Gahan, C. G. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323599111 · Cited by 604 · see citing works
Self-citationDiversification of host bile acids by members of the gut microbiota
Winston, J. A., & Theriot, C. M. (2019) · Gut Microbes · doi:10.1080/19490976.2019.1674124 · Cited by 583 · see citing works
Bile Acids Activated Receptors Regulate Innate Immunity
Fiorucci, S., Biagioli, M., Zampella, A., & Distrutti, E. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01853 · Cited by 569 · see citing works
Song, Z., Cai, Y., Lao, X., Wang, X., Lin, X., Cui, Y., Kalavagunta, P. K., Liao, J., Jin, L., Shang, J., et al. (2019) · Microbiome · doi:10.1186/s40168-019-0628-3 · Cited by 505 · see citing works
Interactions between gut bacteria and bile in health and disease
Long, S. L., Gahan, C. G. M., & Joyce, S. A. (2017) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2017.06.002 · Cited by 495 · see citing works
Self-citationThe bile acid TGR5 membrane receptor: from basic research to clinical application
Duboc, H., Taché, Y., & Hofmann, A. F. (2014) · Digestive and Liver Disease · doi:10.1016/j.dld.2013.10.021 · Cited by 473 · see citing works
Bile Acids as Metabolic Regulators and Nutrient Sensors
Chiang, J. Y. L., & Ferrell, J. M. (2019) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082018-124344 · Cited by 440 · see citing works
An Intestinal Microbiota–Farnesoid X Receptor Axis Modulates Metabolic Disease
Gonzalez, F. J., Jiang, C., & Patterson, A. D. (2016) · Gastroenterology · doi:10.1053/j.gastro.2016.08.057 · Cited by 377 · see citing works
Degirolamo, C., Rainaldi, S., Bovenga, F., Murzilli, S., & Moschetta, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.032 · Cited by 356 · see citing works
Bile Salt Hydrolase of Bifidobacterium longum —Biochemical and Genetic Characterization
Tanaka, H., Hashiba, H., Kok, J., & Mierau, I. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.6.2502-2512.2000 · Cited by 285 · see citing works
A selective gut bacterial bile salt hydrolase alters host metabolism
Yao, L., Seaton, S. C., Ndousse-Fetter, S., Adhikari, A. A., DiBenedetto, N., Mina, A. I., Banks, A. S., Bry, L., & Devlin, A. S. (2018) · eLife · doi:10.7554/elife.37182 · Cited by 274 · see citing works
Mullish, B. H., McDonald, J. A. K., Pechlivanis, A., Allegretti, J. R., Kao, D., Barker, G. F., Kapila, D., Petrof, E. O., Joyce, S. A., Gahan, C. G. M., et al. (2019) · Gut · doi:10.1136/gutjnl-2018-317842 · Cited by 268 · see citing works
Self-citationBegley, M., Sleator, R. D., Gahan, C. G. M., & Hill, C. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.894-904.2005 · Cited by 264 · see citing works
Self-citationStructural comparison of Ntn‐hydrolases
Oinonen, C., & Rouvinen, J. (2000) · Protein Science · doi:10.1110/ps.9.12.2329 · Cited by 261 · see citing works
The microbiome modulating activity of bile acids
Tian, Y., Gui, W., Koo, I., Smith, P. B. W., Allman, E. L., Nichols, R. G., Rimal, B., Cai, J., Liu, Q., & Patterson, A. D. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1732268 · Cited by 251 · see citing works
Joyce, S. A., & Gahan, C. G. M. (2016) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-041715-033159 · Cited by 241 · see citing works
Self-citationBustos, A. Y., Font de Valdez, G., Fadda, S., & Taranto, M. P. (2018) · Food Research International · doi:10.1016/j.foodres.2018.06.035 · Cited by 232 · see citing works
Lambert, J. M., Bongers, R. S., de Vos, W. M., & Kleerebezem, M. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.00137-08 · Cited by 212 · see citing works
Foley, M. H., O’Flaherty, S., Allen, G., Rivera, A. J., Stewart, A. K., Barrangou, R., & Theriot, C. M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017709118 · Cited by 205 · see citing works
Joyce, S. A., Kamil, A., Fleige, L. E., & Gahan, C. G. M. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00171 · Cited by 203 · see citing works
Self-citationBiotechnological applications of penicillin acylases: state-of-the-art
Arroyo, M., de la Mata, I., Acebal, C., & Castillón, M. P. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-002-1113-6 · Cited by 190 · see citing works
Dietary Glycine and Taurine on Bile Acid Conjugation in Man. Bile Acids and Steroids 75
Sjövall, J. (1959) · Experimental Biology and Medicine · doi:10.3181/00379727-100-24741 · Cited by 189 · see citing works
Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604172200 · Cited by 143 · see citing works
Elkins, C. A., Moser, S. A., & Savage, D. C. (2001) · Microbiology · doi:10.1099/00221287-147-12-3403 · Cited by 142 · see citing works
Joyce, S. A., Shanahan, F., Hill, C., & Gahan, C. G. (2014) · Gut Microbes · doi:10.4161/19490976.2014.969986 · Cited by 139 · see citing works
Self-citationRossocha, M., Schultz‐Heienbrok, R., von Moeller, H., Coleman, J. P., & Saenger, W. (2005) · Biochemistry · doi:10.1021/bi0473206 · Cited by 138 · see citing works
Jia, B., Park, D., Hahn, Y., & Jeon, C. O. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1748261 · Cited by 135 · see citing works
Guban, J., Korver, D. R., Allison, G. E., & Tannock, G. W. (2006) · Poultry Science · doi:10.1093/ps/85.12.2186 · Cited by 133 · see citing works
Genetic Analysis of Two Bile Salt Hydrolase Activities in Lactobacillus acidophilus NCFM
McAuliffe, O. E., Cano, R. J., & Klaenhammer, T. R. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.8.4925-4929.2005 · Cited by 126 · see citing works
Disease-Associated Changes in Bile Acid Profiles and Links to Altered Gut Microbiota
Joyce, S. A., & Gahan, C. G. M. (2017) · Digestive Diseases · doi:10.1159/000450907 · Cited by 123 · see citing works
Self-citationThe <i>Lactobacillus</i> Bile Salt Hydrolase Repertoire Reveals Niche-Specific Adaptation
O’Flaherty, S., Briner Crawley, A., Theriot, C. M., & Barrangou, R. (2018) · mSphere · doi:10.1128/msphere.00140-18 · Cited by 118 · see citing works
Purification and characterization of bile salt hydrolase from Clostridium perfringens.
Gopal-Srivastava, R., & Hylemon, P. B. (1988) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38464-9 · Cited by 117 · see citing works
Penicillin V acylase crystal structure reveals new Ntn-hydrolase family members.
Suresh, C. G., Brannigan, J. A., Pundle, A. V., Sivaraman, H., Rao, K. N., McVey, C. E., Verma, C. S., Dauter, Z., Dodson, E. J., & Dodson, G. G. (1999) · Nature Structural Biology · doi:10.1038/8213 · Cited by 113 · see citing works
Metabolic role of lactobacilli in weight modification in humans and animals
Drissi, F., Raoult, D., & Merhej, V. (2016) · Microbial Pathogenesis · doi:10.1016/j.micpath.2016.03.006 · Cited by 113 · see citing works
The role of penicillin amidases in nature and in industry
Valle, F., Balbás, P., Merino, E., & Bollvar, F. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90014-m · Cited by 105 · see citing works
Wang, Z., Zeng, X., Mo, Y., Smith, K., Guo, Y., & Lin, J. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.02519-12 · Cited by 99 · see citing works
Molecular features of bile salt hydrolases and relevance in human health
Chand, D., Avinash, V. S., Yadav, Y., Pundle, A. V., Suresh, C. G., & Ramasamy, S. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.024 · Cited by 95 · see citing works
Fang, F., Li, Y., Bumann, M., Raftis, E. J., Casey, P. G., Cooney, J. C., Walsh, M. A., & O’Toole, P. W. (2009) · Journal of Bacteriology · doi:10.1128/jb.00506-09 · Cited by 94 · see citing works
Bile salt hydrolases: Structure and function, substrate preference, and inhibitor development
Dong, Z., & Lee, B. H. (2018) · Protein Science · doi:10.1002/pro.3484 · Cited by 92 · see citing works
Bile Acid Biology, Pathophysiology, and Therapeutics
Chiang, J. Y. L., & Ferrell, J. M. (2020) · Clinical Liver Disease · doi:10.1002/cld.861 · Cited by 87 · see citing works
Srirangan, K., Ward, V. C. A., Akawi, L., Westbrook, A. W., Moo‐Young, M., & Chou, C.-H. P. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2013.05.006 · Cited by 86 · see citing works
Bile acid signaling and biliary functions
Jones, H. F., Alpini, G. D., & Francis, H. (2015) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2015.01.009 · Cited by 86 · see citing works
Microbiome-mediated bile acid modification: Role in intestinal drug absorption and metabolism
Enright, E. F., Griffin, B. T., Gahan, C. G. M., & Joyce, S. A. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.04.009 · Cited by 86 · see citing works
Self-citationSmet, I. D., Hoorde, L. V., Saeyer, N. D., Woestyne, M. V., & Verstraete, W. (1994) · Microbial Ecology in Health and Disease · doi:10.3109/08910609409141371 · Cited by 86 · see citing works
Lodola, A., Branduardi, D., Vivo, M. D., Capoferri, L., Mor, M., Piomelli, D., & Cavalli, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032397 · Cited by 81 · see citing works
Chae, J. P., Valeriano, V. D., Kim, G., & Kang, D. K. (2012) · Journal of Applied Microbiology · doi:10.1111/jam.12027 · Cited by 73 · see citing works
Ren, J., Sun, K., Wu, Z., Yao, J., & Guo, B. (2011) · Journal of Food Science · doi:10.1111/j.1750-3841.2011.02431.x · Cited by 70 · see citing works
Chand, D., Panigrahi, P., Varshney, N. K., Ramasamy, S., & Suresh, C. G. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.01.003 · Cited by 64 · see citing works
Current state and perspectives of penicillin G acylase-based biocatalyses
Marešová, H., Plačková, M., Grulich, M., & Kyslı́k, P. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5492-7 · Cited by 62 · see citing works
Kusada, H., Tamaki, H., Kamagata, Y., Hanada, S., & Kimura, N. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.00080-17 · Cited by 59 · see citing works
Qu, T., Yang, L., Wang, Y., Jiang, B., Shen, M., & Ren, D. (2020) · Food & Function · doi:10.1039/c9fo02478f · Cited by 58 · see citing works
Mukherji, R., Varshney, N. K., Panigrahi, P., Suresh, C. G., & Prabhune, A. A. (2013) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2013.12.010 · Cited by 55 · see citing works
Modulating bile acid pathways and TGR5 receptors for treating liver and GI diseases
Malhi, H., & Camilleri, M. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.09.008 · Cited by 54 · see citing works
Improved annotation of conjugated bile acid hydrolase superfamily members in Gram-positive bacteria
Lambert, J. M., Siezen, R. J., de Vos, W. M., & Kleerebezem, M. (2008) · Microbiology · doi:10.1099/mic.0.2008/016808-0 · Cited by 47 · see citing works
Sunder, A. V., Utari, P. D., Ramasamy, S., van Merkerk, R., Quax, W. J., & Pundle, A. V. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-8031-5 · Cited by 47 · see citing works
Rani, R. P., Anandharaj, M., & Ravindran, A. D. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01004 · Cited by 46 · see citing works
Koreishi, M., Zhang, D., Imanaka, H., Imamura, K., Adachi, S., Matsuno, R., & Nakanishi, K. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf052102k · Cited by 40 · see citing works
Xu, F., Hu, X., Singh, W., Geng, W., Tikhonova, I. G., & Lin, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-48850-6 · Cited by 40 · see citing works
Liang, L., Yi, Y., Lv, Y., Qian, J., Lei, X., & Zhang, G. (2018) · Molecules · doi:10.3390/molecules23051157 · Cited by 38 · see citing works
Crystal structure of bile salt hydrolase fromLactobacillus salivarius
Xu, F., Guo, F., Hu, X., & Lin, J. (2016) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x16005707 · Cited by 37 · see citing works
Hu, P.-L., Yuan, Y., Yue, T., & Guo, C. (2018) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-018-8742-x · Cited by 37 · see citing works
DiMarzio, M., Rusconi, B. A., Yennawar, N. H., Eppinger, M., Patterson, A. D., & Dudley, E. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0183564 · Cited by 35 · see citing works
Penicillin acylases revisited: importance beyond their industrial utility
Avinash, V. S., Pundle, A. V., Ramasamy, S., & Suresh, C. G. (2014) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2014.960359 · Cited by 33 · see citing works
Wang, Y., Li, H., Cui, X., & Zhang, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-04606-8 · Cited by 31 · see citing works
Panigrahi, P., Sule, M., Sharma, R., Ramasamy, S., & Suresh, C. G. (2014) · Microbiology · doi:10.1099/mic.0.077586-0 · Cited by 25 · see citing works
Velasco-Bucheli, R., Hormigo, D., Fernández‐Lucas, J., Torres‐Ayuso, P., Alfaro-Ureña, Y., Saborido, A., Serrano‐Aguirre, L., García, J. L., Ramón, F., Acebal, C., et al. (2020) · Catalysts · doi:10.3390/catal10070730 · Cited by 24 · see citing works
Torres‐Bacete, J., Hormigo, D., Torres‐Guzmán, R., Arroyo, M., Castillón, M. P., García, J. L., Acebal, C., & de la Mata, I. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.02352-14 · Cited by 19 · see citing works
Impaired Intestinal Farnesoid X Receptor Signaling in Cystic Fibrosis Mice
Ikpa, P. T., Doktorova, M., Meijsen, K. F., Nieuwenhuijze, N. D. A., Verkade, H. J., Jonker, J. W., de Jonge, H. R., & Bijvelds, M. J. C. (2019) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2019.08.006 · Cited by 19 · see citing works
Avinash, V. S., Ramasamy, S., Suresh, C. G., & Pundle, A. V. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.04.036 · Cited by 18 · see citing works
Pundle, A. V., & Sivaraman, H. (1997) · Current Microbiology · doi:10.1007/s002849900159 · Cited by 17 · see citing works
Kumar, R., Grover, S., Kaushik, J. K., & Batish, V. K. (2013) · Microbiological Research · doi:10.1016/j.micres.2013.10.006 · Cited by 16 · see citing works
Purification and characterization of YxeI, a penicillin acylase from Bacillus subtilis
Rathinaswamy, P., Gaikwad, S. M., Suresh, C. G., Prabhune, A. A., Brannigan, J. A., Dodson, G. G., & Pundle, A. V. (2011) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2011.09.018 · Cited by 16 · see citing works
Rathinaswamy, P., Pundle, A. V., Prabhune, A. A., SivaRaman, H., Brannigan, J. A., Dodson, G. G., & Suresh, C. G. (2005) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309105017987 · Cited by 15 · see citing works
Xu, G., Zhao, Q., Huang, B., Zhou, J., & Cao, F. (2018) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2018.08.006 · Cited by 15 · see citing works
Avinash, V. S., Panigrahi, P., Suresh, C. G., Pundle, A. V., & Ramasamy, S. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.06.109 · Cited by 13 · see citing works
Industrial and Therapeutic Enzymes
Illanes, A., & Valencia, P. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-444-63662-1.00013-0 · Cited by 13 · see citing works
Avinash, V. S., Chauhan, P. D., Gaikwad, S., & Pundle, A. V. (2016) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2016.1163580 · Cited by 12 · see citing works
Avinash, V. S., Panigrahi, P., Chand, D., Pundle, A. V., Suresh, C. G., & Ramasamy, S. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.12.008 · Cited by 10 · see citing works
Philem, P. D., Yadav, Y., Sunder, A. V., Ghosh, D., Prabhune, A. A., & Ramasamy, S. (2020) · Biochimie · doi:10.1016/j.biochi.2020.07.017 · Cited by 8 · see citing works
Öztürk, M., & Önal, C. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-04889-2 · Cited by 6 · see citing works
Flagged first, then by citations
1 of the 90 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The changing metabolic landscape of bile acids – keys to metabolism and immune regulation
Mohanty, I., Allaband, C., Mannochio-Russo, H., Abiead, Y. E., Hagey, L. R., Knight, R. D., & Dorrestein, P. C. (2024) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-024-00914-3 · Cited by 227 · see citing works
Jia, B., Zou, Y., Han, X., Bae, J., & Jeon, C. O. (2022) · Trends in Microbiology · doi:10.1016/j.tim.2022.08.003 · Cited by 220 · see citing works
The underappreciated diversity of bile acid modifications
Mohanty, I., Mannochio-Russo, H., Schweer, J. V., Abiead, Y. E., Bittremieux, W., Xing, S., Schmid, R., Zuffa, S., Vasquez, F. J. D. A., Muti, V. B., et al. (2024) · Cell · doi:10.1016/j.cell.2024.02.019 · Cited by 202 · see citing works
Interactive relationships between intestinal flora and bile acids
Guo, X., Okpara, E. S., Hu, W., Yan, C., Wang, Y., Liang, Q., Chiang, J. Y. L., & Han, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158343 · Cited by 206 · see citing works
Molecular basis of bile acid-FXR-FGF15/19 signaling axis
Katafuchi, T., & Makishima, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116046 · Cited by 193 · see citing works
Another renaissance for bile acid gastrointestinal microbiology
Ridlon, J. M., & Gaskins, H. R. (2024) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-024-00896-2 · Cited by 193 · see citing works
Bile salt hydrolase in non-enterotoxigenic Bacteroides potentiates colorectal cancer
Sun, L., Zhang, Y., Cai, J., Rimal, B., Rocha, E. R., Coleman, J. P., Zhang, C., Nichols, R. G., Luo, Y., Kim, B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36089-9 · Cited by 121 · see citing works
Physiological Role of Bile Acids Modified by the Gut Microbiome
Kiriyama, Y., & Nochi, H. (2021) · Microorganisms · doi:10.3390/microorganisms10010068 · Cited by 101 · see citing works
Kiriyama, Y., & Nochi, H. (2023) · Microorganisms · doi:10.3390/microorganisms11112730 · Cited by 75 · see citing works
O’Mahony, A. K., Álvarez‐Ordóñez, A., Filloux, A., Gahan, C. G. M., & Cotter, P. D. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1002185 · Cited by 59 · see citing works
Self-citationMorinaga, K., Kusada, H., & Tamaki, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810980 · Cited by 38 · see citing works
Gao, X., Lin, X., Yan, X., Zhu, X., Li, X., Chen, M., Huang, Z., & Guo, H. (2023) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2023.109347 · Cited by 36 · see citing works
Identifying a Novel Bile Salt Hydrolase from the Keystone Gut Bacterium Christensenella minuta
Déjean, G., Tudela, H., Bruno, L., Kissi, D., Rawadi, G., & Claus, S. P. (2021) · Microorganisms · doi:10.3390/microorganisms9061252 · Cited by 34 · see citing works
Kusada, H., Arita, M., Tohno, M., & Tamaki, H. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.858263 · Cited by 29 · see citing works
Zhang, M., Xiao, B., Chen, X., Ou, B., & Wang, S. (2023) · Acta Physiologica · doi:10.1111/apha.14065 · Cited by 26 · see citing works
Lucas, L. N., Mallikarjun, J., Cattaneo, L. E., Gangwar, B., Zhang, Q., Clay, A. P., Kerby, R. L., Stevenson, D. M., Blackwell, H. E., Rey, F. E., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68556-4 · Cited by 27 · see citing works
Gao, Y., Lin, J., Ye, C., Guo, S., & Jiang, C. (2023) · Liver Research · doi:10.1016/j.livres.2023.09.002 · Cited by 23 · see citing works
Guo, S.-J., Li, C.-C., Feng, Y.-T., Zhou, Y.-R., Liu, B., Gao, Z.-P., & Guo, C. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.103847 · Cited by 22 · see citing works
Kang, M. H., Elnar, A. G., & Kim, G.-B. (2025) · Food Science of Animal Resources · doi:10.5851/kosfa.2025.e1 · Cited by 21 · see citing works
Agolino, G., Cristofolini, M., Vaccalluzzo, A., Tagliazucchi, D., Cattivelli, A., Pino, A., Caggia, C., Solieri, L., & Randazzo, C. L. (2025) · Biomolecules · doi:10.3390/biom15010086 · Cited by 19 · see citing works
Shangpliang, H. N. J., & Tamang, J. P. (2023) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-023-10125-y · Cited by 13 · see citing works
Bravo, M., Conchillo‐Solé, O., Coves, X., García-Navarro, A., Gómez, A.-C., Márquez-Martínez, M., Ferrer‐Miralles, N., Daura, X., Gibert, I., & Yero, D. (2025) · Scientific Reports · doi:10.1038/s41598-025-92749-4 · Cited by 9 · see citing works
Microbiome manipulation by corals and other Cnidaria via quorum quenching
Mason, B. M., Hayward, D. C., Moya, A., Cooke, I., Sorenson, A. E., Brunner, R., Andrade-Rodriguez, N., Huerlimann, R., Bourne, D. G., Schaeffer, P. M., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.05.073 · Cited by 8 · see citing works
Biological Actions of Bile Acids via Cell Surface Receptors
Kiriyama, Y., Tokumaru, H., Sadamoto, H., & Nochi, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115004 · Cited by 7 · see citing works
Pleiotropic immunoregulation by bile acids in pathophysiology
Lin, B.-S., Yin, M., Xie, S.-A., Li, P., & Li, X. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1719092 · Cited by 7 · see citing works
Pheiffer, F., Schneider, Y. K.-H., Hansen, E. H., Andersen, J. H., Isaksson, J. M., Busche, T., Rückert, C., Kalinowski, J., van Zyl, L. J., & Trindade, M. (2022) · Marine Drugs · doi:10.3390/md21010002 · Cited by 7 · see citing works
Adams, C. O., Campbell, J. A., Zhang, B., Cleaver, L. M., Bier, S. B., Mayoral, J., White, R. C., Garnett, J. A., & Cianciotto, N. P. (2025) · mBio · doi:10.1128/mbio.01393-25 · Cited by 6 · see citing works
Wang, Y., Zhang, Y. L., Wang, Q., Fan, Y., Li, W., Liu, M., Zhang, X., Zhou, W., Wang, M., Jiang, S., et al. (2024) · Journal of Chromatography B · doi:10.1016/j.jchromb.2024.124218 · Cited by 5 · see citing works
Poly(vinyl alcohol) (PVA) for gene delivery: A systematic review
Santos, J. D. A., Valente, A. J. M., & Muniz, E. C. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.106149 · Cited by 3 · see citing works
Duche, R. T., Nwagu, T. N., Singh, A., Wandhare, A. G., Sihag, M. K., Panwar, H., & Ezeogu, L. I. (2022) · Indian Journal of Dairy Science · doi:10.33785/ijds.2022.v75i04.003 · Cited by 2 · see citing works
Special Issue: Microbial Impact on Cholesterol and Bile Acid Metabolism
Ridlon, J. M. (2022) · Microorganisms · doi:10.3390/microorganisms10020477 · Cited by 2 · see citing works
Agolino, G., Cristofolini, M., Ronsivalle, M. A., Cattivelli, A., Tagliazucchi, D., Caggia, C., Solieri, L., & Randazzo, C. L. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10810-0 · Cited by 1 · see citing works
“BSH and PVA are evolutionary related enzymes with high similarity in terms of the amino acid residues involved in their active site [5, 84].”
Lu, X., Wang, Y., Chang, D., Bai, F., Wen, X., Lü, M., Liu, X., Li, J., Li, X., Zhang, D., et al. (2025) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250294 · Cited by 1 · see citing works
Sevelamer inhibits the formation of cholesterol gallstones by modulating bile acid metabolism
Shen, S., Ning, M., Li, M., Qian, S., Ye, X., Zhuang, Q., Wu, S., Wan, X., & Dong, Z. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1737631 · Cited by 1 · see citing works
Keuler, T., Wolf, V., Lemke, C., Voget, R., Braune, A., & Gütschow, M. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106574 · Cited by 1 · see citing works
Jiang, L., Lu, X., Lin, X., Cao, Z., Liu, R., Mu, G., & Jiang, S. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250406
Al, K. F., Wammes, M., Warren, M., Lee, J. E., Walton, D. M., O’Connor, C. P., Cameron, L., Burton, J. P., & Osuch, E. A. (2026) · Translational Psychiatry · doi:10.1038/s41398-026-04046-x
Cagle, R., Proll, S. C., Minot, S. S., Purcell, H. J., Zhu, W., Djukovic, D., Liu, C., Fiedler, T. L., DeMeules, M. M., Mielcarek, M. B., et al. (2026) · Frontiers in Microbiology · doi:10.3389/fmicb.2026.1818647 · Cited by 1 · see citing works
Structural and Functional Siderophore Remodeling by Enzymatic Delipidation
Herzog, E., Ishida, K., Molloy, E. M., Hermenau, R., Scherlach, K., & Hertweck, C. (2026) · Angewandte Chemie · doi:10.1002/ange.2621546
Structural and Functional Siderophore Remodeling by Enzymatic Delipidation
Herzog, E., Ishida, K., Molloy, E. M., Hermenau, R., Scherlach, K., & Hertweck, C. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.2621546
- Authors
- Daly, J. W., Keely, S. J., & Gahan, C. G. M.
- Affiliations
- University College Cork (IE)
- Royal College of Surgeons in Ireland (IE)
- Corresponding author
- Gahan, Cormac G. M.
- Venue
- Microorganisms
- Publisher
- MDPI AG
- Published
- 2021-03-31
- Volume
- 9
- Issue
- 4
- Pages
- 732
- ISSN
- 2076-2607 (ISSN-L)
- PMC
- PMC8066178
- OpenAlex
- W3152258656
- Cited by
- 40
- References
- 90
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 8 · 2023: 7 · 2022: 9 · 2021: 2
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Microorganisms (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Science Foundation Ireland (16/IA/4445)
- APC Microbiome Ireland (SFI/12/RC/2273)
- Irish Department of Agriculture Food and the Marine (DAFM) under the Food Institutional Re-search Measure (FIRM) (17F244)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gut microbiota and health
- Keywords
- bile salt hydrolase, penicillin V acylase, enzyme phylogeny, functional diversity, bile acid metabolism, farnesoid X receptor, TGR5, cholesterol homeostasis, semisynthetic antibiotics, enzyme evolution, microbial enzymes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review