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Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase
Open accessAbstract
Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alphabetabetaalpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.
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“the terminal cysteine Cys1 of BlBSH is predicted to be the primary catalytic residue, although other active site residues (for example, Thr2, Trp21, Thr171, Asn172 and Arg225) may also be important for BSH activity or substrate specificity24.”
From Bile Acids Are Substrates for Amine N-Acyl Transferase Activity by Bile Salt Hydrolase (2022) · cites this paper as [24]
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
Self-citationConformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,950
Lehrer, S. S. (1971) · Biochemistry · doi:10.1021/bi00793a015 · Cited by 1,782
Holm, L., & Sander, C. (1996) · Science · doi:10.1126/science.273.5275.595 · Cited by 1,497
Eftink, M. R., & Ghiron, C. A. (1976) · Biochemistry · doi:10.1021/bi00648a035 · Cited by 1,035
An improved colorimetric determination of amino acids with the use of ninhydrin
Lee, Y. P., & Takahashi, T. (1966) · Analytical Biochemistry · doi:10.1016/0003-2697(66)90057-1 · Cited by 838
An approach to multi-copy search in molecular replacement
Vagin, A. A., & Teplyakov, A. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900013780 · Cited by 702
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
Self-citationARP/wARP and molecular replacement
Anastassis Perrakis, A., Harkiolaki, M., Wilson, K. S., & Lamzin, V. S. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444901014007 · Cited by 457
Hofmann, A. F., & Roda, A. (1984) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34421-7 · Cited by 384
Dussurget, O., Cabanes, D., Dehoux, P., Lecuit, M., Buchrieser, C., Glaser, P., & Cossart, P. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03080.x · Cited by 356
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
Screening of Lactic Acid Bacteria for Bile Salt Hydrolase Activity
Tanaka, H., Doesburg, K. K., Iwasaki, T., & Mierau, I. (1999) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(99)75506-2 · Cited by 283
Structural comparison of Ntn‐hydrolases
Oinonen, C., & Rouvinen, J. (2000) · Protein Science · doi:10.1110/ps.9.12.2329 · Cited by 261
Potential of using lactic acid bacteria for therapy and immunomodulation in man
Marteau, P. R., & Rambaud, J. (1993) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1993.tb00019.x · Cited by 260
Kaufmann, P., Pfefferkorn, A., Teuber, M., & Meile, L. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.4.1268-1273.1997 · Cited by 236
Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity
Smet, I. D., Boever, P. D., & Verstraete, W. (1998) · British Journal Of Nutrition · doi:10.1079/bjn19980030 · Cited by 182
Lactobacilli and bile salt hydrolase in the murine intestinal tract
Tannock, G. W., Dashkevicz, M. P., & Feighner, S. D. (1989) · Applied and Environmental Microbiology · doi:10.1128/aem.55.7.1848-1851.1989 · Cited by 166
Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis
Stellwag, E. J., & Hylemon, P. B. (1976) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(76)90068-1 · Cited by 145
Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens
Coleman, J. P., & Hudson, L. L. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.7.2514-2520.1995 · Cited by 140
Rossocha, M., Schultz‐Heienbrok, R., von Moeller, H., Coleman, J. P., & Saenger, W. (2005) · Biochemistry · doi:10.1021/bi0473206 · Cited by 138
A fast method to sample real protein conformational space
Feldman, H. J., & Hogue, C. W. V. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(20000501)39:2 · Cited by 134
Christiaens, H., Leer, R. J., Pouwels, P. H., & Verstraete, W. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.12.3792-3798.1992 · Cited by 128
Side chain conjugation prevents bacterial 7-dehydroxylation of bile acids.
Batta, A. K., Salen, G., Arora, R., Shefer, S., Batta, M., & Person, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38535-7 · Cited by 116
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
Self-citationThomas, L. A., Veysey, M. J., Bathgate, T., King, A., French, G. L., Smeeton, N., Murphy, G. M., & Dowling, R. H. (2000) · Gastroenterology · doi:10.1053/gast.2000.16495 · Cited by 111
Knarreborg, A., Engberg, R. M., Jensen, S. K., & Jensen, B. B. (2002) · Applied and Environmental Microbiology · doi:10.1128/aem.68.12.6425-6428.2002 · Cited by 109
Grill, J., Schneider, F., Crociani, J., & Ballongue, J. (1995) · Applied and Environmental Microbiology · doi:10.1128/aem.61.7.2577-2582.1995 · Cited by 105
Deconjugation of bile acids by human intestinal bacteria implanted in germ‐free rats
Chikai, T., Nakao, H., & Uchida, K. (1987) · Lipids · doi:10.1007/bf02533948 · Cited by 101
Isolation of cholesterol-lowering lactic acid bacteria from human intestine for probiotic use
Lim, H. J., Kim, S. Y., & Lee, W. K. (2004) · Journal of Veterinary Science · doi:10.4142/jvs.2004.5.4.391 · Cited by 94
Jones, M. L., Chen, H., Ouyang, W., Metz, T., & Prakash, S. (2004) · BioMed Research International · doi:10.1155/s1110724304307011 · Cited by 86
Incorporation of Cholesterol into the Cellular Membrane of Bifidobacterium longum
Dambekodi, P. C., & Gilliland, S. E. (1998) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(98)75751-0 · Cited by 83
Bile salt deconjugation by Lactobacillus plantarum 80 and its implication for bacterial toxicity
Boever, P. D., & Verstraete, W. (1999) · Journal of Applied Microbiology · doi:10.1046/j.1365-2672.1999.00019.x · Cited by 83
Bahar, R., & Stolz, A. (1999) · Gastroenterology Clinics of North America · doi:10.1016/s0889-8553(05)70042-x · Cited by 80
Substrate specificity of cholylglycine hydrolase for the hydrolysis of bile acid conjugates.
Batta, A. K., Salen, G., & Shefer, S. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42510-5 · Cited by 64
Differential modulation of cellular death and survival pathways by conjugated bile acids
Torchia, E. C., Stolz, A., & Agellon, L. B. (2001) · BMC Biochemistry · doi:10.1186/1471-2091-2-11 · Cited by 42
Chandra, P. M., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Turkenburg, J. P., Dodson, G. G., & Suresh, C. G. (2004) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309104031227 · Cited by 12
Self-citationCoulter, L., & Amadò, R. (1993) · LWT · doi:10.1006/fstl.1993.1059 · Cited by 12
Evaluation of parameters in nonlinear models by the least squares method
Lisý, J. M., & Šimon, P. (1998) · Computers & Chemistry · doi:10.1016/s0097-8485(98)00014-x · Cited by 9
Kumar, R., Brannigan, J. A., Pundle, A. V., Prabhune, A. A., Dodson, G. G., & Suresh, C. G. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904017561 · Cited by 9
Self-citation
Research works printed but not linked: 1
- Hofmann, 1999, News Physiol. Sci., 14, 24
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Ridlon, J. M., Harris, S. C., Bhowmik, S., Kang, D.-J., & Hylemon, P. B. (2016) · Gut Microbes · doi:10.1080/19490976.2015.1127483 · Cited by 1,128
Jones, 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
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Guzior, D. V., & Quinn, R. A. (2021) · Microbiome · doi:10.1186/s40168-021-01101-1 · Cited by 795
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Ruiz, L., Margolles, A., & Sánchez, B. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00396 · Cited by 548
Metadata
- Authors
- Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G.
- Affiliations
- National Chemical Laboratory (IN)
- University of York (GB)
- Corresponding author
- Brannigan, James A.
- Suresh, C.G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-10
- Volume
- 281
- Issue
- 43
- Pages
- 32516-32525
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1998273216
- Cited by
- 143
- References
- 43
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 10 · 2023: 9 · 2022: 12 · 2021: 13 · 2020: 12 · 2019: 10 · 2018: 11 · 2017: 6 · 2016: 8 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 3
- FWCI
- 3.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Council of Scientific and Industrial Research, India
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- bile salt hydrolase, Bifidobacterium longum, penicillin V acylase, enzyme crystal structure, zymogen activation, substrate specificity, enzyme kinetics, enzyme evolution, Clostridium perfringens, Bacillus sphaericus, gut microbiota, bile acid deconjugation
- MeSH terms
- Amidohydrolases, Amino Acid Sequence, Bifidobacterium, Binding Sites, Clostridium perfringens, Hydrogen Bonding, Kinetics, Models, Molecular, Molecular Sequence Data, Penicillin Amidase, Protein Binding, Protein Conformation, Spectrometry, Fluorescence, Substrate Specificity, Molecular Structure, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Secondary, Crystallography, X-Ray, Evolution, Molecular, Dimerization, Protein Structure, Quaternary, Static Electricity, Hydrophobic and Hydrophilic Interactions
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