EFI - Training Resources: Training and Publications

This web resource is supported by a Research Resource from the National Institute of General Medical Sciences (R24GM141196-01).
The tools are available without charge or license to both academic and commercial users.
RadicalSAM.org, our resource for investigating sequence-function space in the radical SAM superfamily, has been updated with sequences from the UniProt Release 2024_01 and InterPro Release 98 databases (January 24, 2024) !!

https://radicalsam.org

1063 Journal Articles

1.
Wichelecki, D. J., Balthazor, B. M., Chau, A. C., Vetting, M. W., Fedorov, A. A., Fedorov, E. V., Lukk, T., Patskovsky, Y. V., Stead, M. B., Hillerich, B. S., Seidel, R. D., Almo, S. C., Gerlt, J. A., Discovery of function in the enolase superfamily: D-mannonate and d-gluconate dehydratases in the D-mannonate dehydratase subgroup. Biochemistry, 2014. 53(16): p. 2722-31. http://doi.org/10.1021/bi500264p
2.
Wichelecki, D. J., Graff, D. C., Al-Obaidi, N., Almo, S. C., Gerlt, J. A., Identification of the in vivo function of the high-efficiency D-mannonate dehydratase in Caulobacter crescentus NA1000 from the enolase superfamily. Biochemistry, 2014. 53(25): p. 4087-9. http://doi.org/10.1021/bi500683x
3.
Dunbar, K. L., Chekan, J. R., Cox, C. L., Burkhart, B. J., Nair, S. K., Mitchell, D. A., Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Nat Chem Biol, 2014. 10(10): p. 823-9. http://doi.org/10.1038/nchembio.1608
4.
Vetting, M. W., Al-Obaidi, N., Zhao, S., San Francisco, B., Kim, J., Wichelecki, D. J., Bouvier, J. T., Solbiati, J. O., Vu, H., Zhang, X., Rodionov, D. A., Love, J. D., Hillerich, B. S., Seidel, R. D., Quinn, R. J., Osterman, A. L., Cronan, J. E., Jacobson, M. P., Gerlt, J. A., Almo, S. C., Experimental strategies for functional annotation and metabolism discovery: targeted screening of solute binding proteins and unbiased panning of metabolomes. Biochemistry, 2015. 54(3): p. 909-31. http://doi.org/10.1021/bi501388y
5.
Rao, G., O'Dowd, B., Li, J., Wang, K., Oldfield, E., IspH–RPS1 and IspH–UbiA:“Rosetta stone” proteins. Chemical science, 2015. 6(12): p. 6813-6822. http://doi.org/10.1039/C5SC02600H
6.
Roche, D., Brackenridge, D., McGuffin, L., Proteins and their interacting partners: An introduction to protein–ligand binding site prediction methods. International journal of molecular sciences, 2015. 16(12): p. 29829-29842. http://doi.org/10.3390/ijms161226202
7.
San Francisco, B., Zhang, X., Whalen, K., Gerlt, J., A Novel Pathway for Bacterial Ethanolamine Metabolism. The FASEB Journal, 2015. 29(1_supplement): p. 573.45.
8.
Anders, K., Essen, L., The family of phytochrome-like photoreceptors: diverse, complex and multi-colored, but very useful. Current Opinion in Structural Biology, 2015. 35: p. 7-16. http://doi.org/10.1016/j.sbi.2015.07.005
9.
Zhang, X., Kumar, R., Vetting, M. W., Zhao, S., Jacobson, M. P., Almo, S. C., Gerlt, J. A., A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily. J Am Chem Soc, 2015. 137(4): p. 1388-91. http://doi.org/10.1021/ja5103986
10.
Celis, A. I., DuBois, J. L., Substrate, product, and cofactor: The extraordinarily flexible relationship between the CDE superfamily and heme. Arch Biochem Biophys, 2015. 574: p. 3-17. http://doi.org/10.1016/j.abb.2015.03.004
11.
Latham, J. A., Iavarone, A. T., Barr, I., Juthani, P. V., Klinman, J. P., PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. J Biol Chem, 2015. 290(20): p. 12908-18. http://doi.org/10.1074/jbc.M115.646521
12.
Liu, F., Geng, J., Gumpper, R. H., Barman, A., Davis, I., Ozarowski, A., Hamelberg, D., Liu, A., An Iron Reservoir to the Catalytic Metal: THE RUBREDOXIN IRON IN AN EXTRADIOL DIOXYGENASE. J Biol Chem, 2015. 290(25): p. 15621-34. http://doi.org/10.1074/jbc.M115.650259
13.
Burkhart, B. J., Hudson, G. A., Dunbar, K. L., Mitchell, D. A., A prevalent peptide-binding domain guides ribosomal natural product biosynthesis. Nat Chem Biol, 2015. 11(8): p. 564-70. http://doi.org/10.1038/nchembio.1856
14.
Cox, C. L., Doroghazi, J. R., Mitchell, D. A., The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles. BMC Genomics, 2015. 16(1): p. 778. http://doi.org/10.1186/s12864-015-2008-0
15.
Wichelecki, D. J., Vetting, M. W., Chou, L., Al-Obaidi, N., Bouvier, J. T., Almo, S. C., Gerlt, J. A., ATP-binding Cassette (ABC) Transport System Solute-binding Protein-guided Identification of Novel d-Altritol and Galactitol Catabolic Pathways in Agrobacterium tumefaciens C58. J Biol Chem, 2015. 290(48): p. 28963-76. http://doi.org/10.1074/jbc.M115.686857
16.
Petronikolou, N., Nair, S. K., Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel. Chem Biol, 2015. 22(11): p. 1480-1490. http://doi.org/10.1016/j.chembiol.2015.09.011
17.
Huang, H., Carter, M. S., Vetting, M. W., Al-Obaidi, N., Patskovsky, Y., Almo, S. C., Gerlt, J. A., A General Strategy for the Discovery of Metabolic Pathways: d-Threitol, l-Threitol, and Erythritol Utilization in Mycobacterium smegmatis. J Am Chem Soc, 2015. 137(46): p. 14570-3. http://doi.org/10.1021/jacs.5b08968
18.
Colin, P. Y., Kintses, B., Gielen, F., Miton, C. M., Fischer, G., Mohamed, M. F., Hyvonen, M., Morgavi, D. P., Janssen, D. B., Hollfelder, F., Ultrahigh-throughput discovery of promiscuous enzymes by picodroplet functional metagenomics. Nat Commun, 2015. 6: p. 10008. http://doi.org/10.1038/ncomms10008
19.
Molloy, E. M., Tietz, J. I., Blair, P. M., Mitchell, D. A., Biological characterization of the hygrobafilomycin antibiotic JBIR-100 and bioinformatic insights into the hygrolide family of natural products. Bioorganic & medicinal chemistry, 2016. 24(24): p. 6276-6290. http://doi.org/10.1016/j.bmc.2016.05.021
20.
Plach, M. G., Reisinger, B., Sterner, R., Merkl, R., Long-term persistence of bi-functionality contributes to the robustness of microbial life through exaptation. PLoS genetics, 2016. 12(1): p. e1005836. http://doi.org/10.1371/journal.pgen.1005836
21.
Thotsaporn, K., Tinikul, R., Maenpuen, S., Phonbuppha, J., Watthaisong, P., Chenprakhon, P., Chaiyen, P., Enzymes in the p-hydroxyphenylacetate degradation pathway of Acinetobacter baumannii. Journal of Molecular Catalysis B: Enzymatic, 2016. 134: p. 353-366. http://doi.org/10.1016/j.molcatb.2016.09.003
22.
Kumar, G., Johnson, J. L., Frantom, P. A., Improving functional annotation in the DRE-TIM metallolyase superfamily through identification of active site fingerprints. Biochemistry, 2016. 55(12): p. 1863-1872. http://doi.org/10.1021/acs.biochem.5b01193
23.
Ahmed, F. H., Mohamed, A. E., Carr, P. D., Lee, B. M., Condic‐Jurkic, K., O'Mara, M. L., Jackson, C. J., Rv2074 is a novel F420H2‐dependent biliverdin reductase in Mycobacterium tuberculosis. Protein Science, 2016. 25(9): p. 1692-1709. http://doi.org/10.1002/pro.2975
24.
Atkinson, J. T., Campbell, I., Bennett, G. N., Silberg, J. J., Cellular assays for ferredoxins: a strategy for understanding electron flow through protein carriers that link metabolic pathways. Biochemistry, 2016. 55(51): p. 7047-7064. http://doi.org/10.1021/acs.biochem.6b00831
25.
Ji, X., Li, Y., Xie, L., Lu, H., Ding, W., Zhang, Q., Expanding radical SAM chemistry by using radical addition reactions and SAM analogues. Angewandte Chemie International Edition, 2016. 55(39): p. 11845-11848. http://doi.org/10.1002/anie.201605917
26.
Zhang, X., Carter, M. S., Vetting, M. W., San Francisco, B., Zhao, S., Al-Obaidi, N. F., Solbiati, J. O., Thiaville, J. J., de Crécy-Lagard, V., Jacobson, M. P., Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proceedings of the National Academy of Sciences, 2016. 113(29): p. E4161-E4169. http://doi.org/10.1073/pnas.1605546113
27.
Tietz, J.I., Mitchell, D.A., Using genomics for natural product structure elucidation. Current topics in medicinal chemistry, 2016. 16(15): p. 1645-1694. http://doi.org/10.2174/1568026616666151012111439
28.
Prunetti, L., El Y. B., Schiavon, C. R., Kirkpatrick, E., Huang, L., Bailly, M., El B. M., Harrison, K., Gregory 3rd, J. F., Fiehn, O., Evidence that COG0325 proteins are involved in PLP homeostasis. Microbiology, 2016. 162(4): p. 694-706. http://doi.org/10.1099/mic.0.000255
29.
Gerlt, J. A., Tools and strategies for discovering novel enzymes and metabolic pathways. Perspectives in science, 2016. 9: p. 24-32. http://doi.org/10.1016/j.pisc.2016.07.001
30.
Colabroy, K. L., Tearing down to build up: Metalloenzymes in the biosynthesis lincomycin, hormaomycin and the pyrrolo [1,4]benzodiazepines. Biochim Biophys Acta, 2016. 1864(6): p. 724-737. http://doi.org/10.1016/j.bbapap.2016.03.001
31.
Ding, W., Li, Q., Jia, Y., Ji, X., Qianzhu, H., Zhang, Q., Emerging Diversity of the Cobalamin-Dependent Methyltransferases Involving Radical-Based Mechanisms. Chembiochem, 2016. 17(13): p. 1191-7. http://doi.org/10.1002/cbic.201600107
32.
Ghodge, S. V., Biernat, K. A., Bassett, S. J., Redinbo, M. R., Bowers, A. A., Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A. J Am Chem Soc, 2016. 138(17): p. 5487-90. http://doi.org/10.1021/jacs.5b13529
33.
Machovina, M. M., Usselman, R. J., DuBois, J. L., Monooxygenase Substrates Mimic Flavin to Catalyze Cofactorless Oxygenations. J Biol Chem, 2016. 291(34): p. 17816-28. http://doi.org/10.1074/jbc.M116.730051
34.
Rao, G., Oldfield, E., Structure and Function of Four Classes of the 4Fe-4S Protein, IspH. Biochemistry, 2016. 55(29): p. 4119-29. http://doi.org/10.1021/acs.biochem.6b00474
35.
Desai, J., Liu, Y. L., Wei, H., Liu, W., Ko, T. P., Guo, R. T., Oldfield, E., Structure, Function, and Inhibition of Staphylococcus aureus Heptaprenyl Diphosphate Synthase. ChemMedChem, 2016. 11(17): p. 1915-23. http://doi.org/10.1002/cmdc.201600311
36.
Ji, X., Liu, W. Q., Yuan, S., Yin, Y., Ding, W., Zhang, Q., Mechanistic study of the radical SAM-dependent amine dehydrogenation reactions. Chem Commun (Camb), 2016. 52(69): p. 10555-8. http://doi.org/10.1039/c6cc05661j
37.
Zallot, R., Harrison, K. J., Kolaczkowski, B., de Crecy-Lagard, V., Functional Annotations of Paralogs: A Blessing and a Curse. Life (Basel), 2016. 6(3): p. 39. http://doi.org/10.3390/life6030039
38.
Li, D., Moorman, R., Vanhercke, T., Petrie, J., Singh, S., Jackson, C. J., Classification and substrate head-group specificity of membrane fatty acid desaturases. Comput Struct Biotechnol J, 2016. 14: p. 341-349. http://doi.org/10.1016/j.csbj.2016.08.003
39.
Davey, L., Halperin, S. A., Lee, S. F., Thiol-Disulfide Exchange in Gram-Positive Firmicutes. Trends Microbiol, 2016. 24(11): p. 902-915. http://doi.org/10.1016/j.tim.2016.06.010
40.
Maxson, T., Tietz, J. I., Hudson, G. A., Guo, X. R., Tai, H. C., Mitchell, D. A., Targeting Reactive Carbonyls for Identifying Natural Products and Their Biosynthetic Origins. J Am Chem Soc, 2016. 138(46): p. 15157-15166. http://doi.org/10.1021/jacs.6b06848
41.
Baier, F., Copp, J. N., Tokuriki, N., Evolution of Enzyme Superfamilies: Comprehensive Exploration of Sequence-Function Relationships. Biochemistry, 2016. 55(46): p. 6375-6388. http://doi.org/10.1021/acs.biochem.6b00723
42.
Dassama, L. M., Kenney, G. E., Ro, S. Y., Zielazinski, E. L., Rosenzweig, A. C., Methanobactin transport machinery. Proc Natl Acad Sci U S A, 2016. 113(46): p. 13027-13032. http://doi.org/10.1073/pnas.1603578113
43.
Hao, Y., Pierce, E., Roe, D., Morita, M., McIntosh, J. A., Agarwal, V., Cheatham, T. E., 3rd, Schmidt, E. W., Nair, S. K., Molecular basis for the broad substrate selectivity of a peptide prenyltransferase. Proc Natl Acad Sci U S A, 2016. 113(49): p. 14037-14042. http://doi.org/10.1073/pnas.1609869113
44.
Jia, B., Jia, X., Kim, K. H., Jeon, C. O., Integrative view of 2-oxoglutarate/Fe(II)-dependent oxygenase diversity and functions in bacteria. Biochim Biophys Acta Gen Subj, 2017. 1861(2): p. 323-334. http://doi.org/10.1016/j.bbagen.2016.12.001
45.
Chekan, J. R., Koos, J. D., Zong, C., Maksimov, M. O., Link, A. J., Nair, S. K., Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates. J Am Chem Soc, 2016. 138(50): p. 16452-16458. http://doi.org/10.1021/jacs.6b10389
46.
Bhandari, D. M., Fedoseyenko, D., Begley, T. P., Tryptophan Lyase (NosL): A Cornucopia of 5'-Deoxyadenosyl Radical Mediated Transformations. J Am Chem Soc, 2016. 138(50): p. 16184-16187. http://doi.org/10.1021/jacs.6b06139
47.
Ortega, M. A., Cogan, D. P., Mukherjee, S., Garg, N., Li, B., Thibodeaux, G. N., Maffioli, S. I., Donadio, S., Sosio, M., Escano, J., Smith, L., Nair, S. K., van der Donk, W. A., Two Flavoenzymes Catalyze the Post-Translational Generation of 5-Chlorotryptophan and 2-Aminovinyl-Cysteine during NAI-107 Biosynthesis. ACS Chem Biol, 2017. 12(2): p. 548-557. http://doi.org/10.1021/acschembio.6b01031
48.
McFarland, B. J., Online Tools for Teaching Large Laboratory Courses: How the GENI Website Facilitates Authentic Research. Teaching and the Internet: The Application of Web Apps, Networking, and Online Tech for Chemistry Education, 2017. http://doi.org/10.1021/bk-2017-1270.ch008
49.
Hopkins, D. H., Fraser, N. J., Mabbitt, P. D., Carr, P. D., Oakeshott, J. G., Jackson, C. J., Structure of an insecticide sequestering carboxylesterase from the disease vector Culex quinquefasciatus: what makes an enzyme a good insecticide sponge?. Biochemistry, 2017. 56(41): p. 5512-5525. http://doi.org/10.1021/acs.biochem.7b00774
50.
Holliday, G. L., Brown, S. D., Akiva, E., Mischel, D., Hicks, M. A., Morris, J. H., Huang, C. C., Meng, E. C., Pegg, S. C., Ferrin, T. E., Biocuration in the structure–function linkage database: the anatomy of a superfamily. Database, 2017. 2017. http://doi.org/10.1093/database/bax045
51.
Wang, H., Chen, X., Li, C., Liu, Y., Yang, F., Wang, C., Sequence-based prediction of cysteine reactivity using machine learning. Biochemistry, 2017. 57(4): p. 451-460. http://doi.org/10.1021/acs.biochem.7b00897
52.
Lohans, C. T., Wang, D. Y., Wang, J., Hamed, R. B., Schofield, C. J., Crotonases: nature’s exceedingly convertible catalysts. ACS Catalysis, 2017. 7(10): p. 6587-6599. http://doi.org/10.1021/acscatal.7b01699
53.
Orth, C., Niemann, N., Hennig, L., Essen, L., Batschauer, A., Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site. Journal of Biological Chemistry, 2017. 292(31): p. 12906-12920. http://doi.org/10.1074/jbc.M117.788869
54.
Holliday, G. L., Davidson, R., Akiva, E., Babbitt, P. C., Evaluating functional annotations of enzymes using the gene ontology. The Gene Ontology Handbook, 2017. http://doi.org/10.1007/978-1-4939-3743-1_9
55.
Wang, M., Moynié, L., Harrison, P. J., Kelly, V., Piper, A., Naismith, J. H., Campopiano, D. J., Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Nature chemical biology, 2017. 13(6): p. 660. http://doi.org/10.1038/nchembio.2361
56.
Bearne, S. L., The interdigitating loop of the enolase superfamily as a specificity binding determinant or ‘flying buttress’. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 2017. 1865(5): p. 619-630. http://doi.org/10.1016/j.bbapap.2017.02.006
57.
Zallot, R., Yuan, Y., de Crécy-Lagard, V., The Escherichia coli COG1738 member YhhQ is involved in 7-cyanodeazaguanine (preQ0) transport. Biomolecules, 2017. 7(1): p. 12. http://doi.org/10.3390/biom7010012
58.
Ney, B., Ahmed, F. H., Carere, C. R., Biswas, A., Warden, A. C., Morales, S. E., Pandey, G., Watt, S. J., Oakeshott, J. G., Taylor, M. C., The methanogenic redox cofactor F 420 is widely synthesized by aerobic soil bacteria. The ISME journal, 2017. 11(1): p. 125. http://doi.org/10.1038/ismej.2016.100
59.
Cogan, D. P., Hudson, G. A., Zhang, Z., Pogorelov, T. V., van der Donk, W. A., Mitchell, D. A., Nair, S. K., Structural insights into enzymatic [4+ 2] aza-cycloaddition in thiopeptide antibiotic biosynthesis. Proceedings of the National Academy of Sciences, 2017. 114(49): p. 12928-12933. http://doi.org/10.1073/pnas.1716035114
60.
Macaisne, N., Liu, F., Scornet, D., Peters, A. F., Lipinska, A., Perrineau, M. M., Henry, A., Strittmatter, M., Coelho, S. M., Cock, J. M., The Ectocarpus IMMEDIATE UPRIGHT gene encodes a member of a novel family of cysteine-rich proteins with an unusual distribution across the eukaryotes. Development, 2017. 144(3): p. 409-418. http://doi.org/10.1242/dev.141523
61.
Repka, L. M., Chekan, J. R., Nair, S. K., van der Donk, W. A., Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes. Chem Rev, 2017. 117(8): p. 5457-5520. http://doi.org/10.1021/acs.chemrev.6b00591
62.
Pimviriyakul, P., Thotsaporn, K., Sucharitakul, J., Chaiyen, P., Kinetic Mechanism of the Dechlorinating Flavin-dependent Monooxygenase HadA. J Biol Chem, 2017. 292(12): p. 4818-4832. http://doi.org/10.1074/jbc.M116.774448
63.
Erb, T. J., Jones, P. R., Bar-Even, A., Synthetic metabolism: metabolic engineering meets enzyme design. Curr Opin Chem Biol, 2017. 37: p. 56-62. http://doi.org/10.1016/j.cbpa.2016.12.023
64.
Pornsuwan, S., Maenpuen, S., Kamutira, P., Watthaisong, P., Thotsaporn, K., Tongsook, C., Juttulapa, M., Nijvipakul, S., Chaiyen, P., 3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Pseudomonas aeruginosa: An Fe(II)-containing enzyme with fast turnover. PLoS One, 2017. 12(2): p. e0171135. http://doi.org/10.1371/journal.pone.0171135
65.
Glasner, M. E., Finding enzymes in the gut metagenome. Science, 2017. 355(6325): p. 577-578. http://doi.org/10.1126/science.aam7446
66.
Levin, B. J., Huang, Y. Y., Peck, S. C., Wei, Y., Martinez-Del C. A., Marks, J. A., Franzosa, E. A., Huttenhower, C., Balskus, E. P., A prominent glycyl radical enzyme in human gut microbiomes metabolizes trans-4-hydroxy-l-proline. Science, 2017. 355(6325): p. eaai8386. http://doi.org/10.1126/science.aai8386
67.
Jia, B., Jia, X., Hyun K. K., Ji P. Z., Kang, M. S., Ok J. C., Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway. Sci Rep, 2017. 7: p. 43489. http://doi.org/10.1038/srep43489
68.
Tietz, J. I., Schwalen, C. J., Patel, P. S., Maxson, T., Blair, P. M., Tai, H. C., Zakai, U. I., Mitchell, D. A., A new genome-mining tool redefines the lasso peptide biosynthetic landscape. Nat Chem Biol, 2017. 13(5): p. 470-478. http://doi.org/10.1038/nchembio.2319
69.
Giessen, T. W., Silver, P. A., Widespread distribution of encapsulin nanocompartments reveals functional diversity. Nat Microbiol, 2017. 2(6): p. 17029. http://doi.org/10.1038/nmicrobiol.2017.29
70.
Hetrick, K. J., van der Donk, W. A., Ribosomally synthesized and post-translationally modified peptide natural product discovery in the genomic era. Curr Opin Chem Biol, 2017. 38: p. 36-44. http://doi.org/10.1016/j.cbpa.2017.02.005
71.
Schwalen, C. J., Feng, X., Liu, W., O. D. B., Ko, T. P., Shin, C. J., Guo, R. T., Mitchell, D. A., Oldfield, E., Head-to-Head Prenyl Synthases in Pathogenic Bacteria. Chembiochem, 2017. 18(11): p. 985-991. http://doi.org/10.1002/cbic.201700099
72.
Ahmed, M. N., Reyna-Gonzalez, E., Schmid, B., Wiebach, V., Sussmuth, R. D., Dittmann, E., Fewer, D. P., Phylogenomic Analysis of the Microviridin Biosynthetic Pathway Coupled with Targeted Chemo-Enzymatic Synthesis Yields Potent Protease Inhibitors. ACS Chem Biol, 2017. 12(6): p. 1538-1546. http://doi.org/10.1021/acschembio.7b00124
73.
Estrada, P., Manandhar, M., Dong, S. H., Deveryshetty, J., Agarwal, V., Cronan, J. E., Nair, S. K., The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes. Nat Chem Biol, 2017. 13(6): p. 668-674. http://doi.org/10.1038/nchembio.2359
74.
Haase, E. M., Kou, Y., Sabharwal, A., Liao, Y. C., Lan, T., Lindqvist, C., Scannapieco, F. A., Comparative genomics and evolution of the amylase-binding proteins of oral streptococci. BMC Microbiol, 2017. 17(1): p. 94. http://doi.org/10.1186/s12866-017-1005-7
75.
Blin, K., Wolf, T., Chevrette, M. G., Lu, X., Schwalen, C. J., Kautsar, S. A., Suarez D. H. G., de Los Santos, E. L. C., Kim, H. U., Nave, M., Dickschat, J. S., Mitchell, D. A., Shelest, E., Breitling, R., Takano, E., Lee, S. Y., Weber, T., Medema, M. H., antiSMASH 4.0-improvements in chemistry prediction and gene cluster boundary identification. Nucleic Acids Res, 2017. 45(W1): p. W36-W41. http://doi.org/10.1093/nar/gkx319
76.
Kandlinger, F., Plach, M. G., Merkl, R., AGeNNT: annotation of enzyme families by means of refined neighborhood networks. BMC Bioinformatics, 2017. 18(1): p. 274. http://doi.org/10.1186/s12859-017-1689-6
77.
Wagner, D. T., Zeng, J., Bailey, C. B., Gay, D. C., Yuan, F., Manion, H. R., Keatinge-Clay, A. T., Structural and Functional Trends in Dehydrating Bimodules from trans-Acyltransferase Polyketide Synthases. Structure, 2017. 25(7): p. 1045-1055 e2. http://doi.org/10.1016/j.str.2017.05.011
78.
Benjdia, A., Guillot, A., Ruffie, P., Leprince, J., Berteau, O., Post-translational modification of ribosomally synthesized peptides by a radical SAM epimerase in Bacillus subtilis. Nat Chem, 2017. 9(7): p. 698-707. http://doi.org/10.1038/nchem.2714
79.
Koppel, N., Maini R. V., Balskus, E. P., Chemical transformation of xenobiotics by the human gut microbiota. Science, 2017. 356(6344): p. eaag2770. http://doi.org/10.1126/science.aag2770
80.
Zhong, G., Zhao, Q., Zhang, Q., Liu, W., 4-alkyl-L-(Dehydro)proline biosynthesis in actinobacteria involves N-terminal nucleophile-hydrolase activity of gamma-glutamyltranspeptidase homolog for C-C bond cleavage. Nat Commun, 2017. 8: p. 16109. http://doi.org/10.1038/ncomms16109
81.
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