Enzymatic Chemistry of Cyclopropane, Epoxide, and Aziridine Biosynthesis

Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

Costas, M., Mehn, M. P., Jensen, M. P., & Que, L. (2004) · Chemical Reviews · doi:10.1021/cr020628n · Cited by 2,472

Heme-Containing Oxygenases

Sono, M., Roach, M. P., Coulter, E. D., & Dawson, J. H. (1996) · Chemical Reviews · doi:10.1021/cr9500500 · Cited by 2,441

Mechanism of Oxidation Reactions Catalyzed by Cytochrome P450 Enzymes

Meunier, B., de Visser, S. P., & Shaik, S. (2004) · Chemical Reviews · doi:10.1021/cr020443g · Cited by 2,398

Ethylene in plant biology

Davies, P. J. (1993) · Cell · doi:10.1016/0092-8674(93)90043-p · Cited by 1,781

Theoretical Perspective on the Structure and Mechanism of Cytochrome P450 Enzymes

Shaik, S., Kumar, D., de Visser, S. P., Altun, A., & Thiel, W. (2005) · Chemical Reviews · doi:10.1021/cr030722j · Cited by 1,236

Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants

Degenhardt, J., Köllner, T. G., & Gershenzon, J. (2009) · Phytochemistry · doi:10.1016/j.phytochem.2009.07.030 · Cited by 1,093

P450 Enzymes: Their Structure, Reactivity, and Selectivity—Modeled by QM/MM Calculations

Shaik, S., Cohen, S., Wang, Y., Chen, H., Kumar, D., & Thiel, W. (2010) · Chemical Reviews · doi:10.1021/cr900121s · Cited by 1,083

Ethylene Biosynthesis

Kende, H. (1993) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.44.060193.001435 · Cited by 1,013

Structural Biology and Chemistry of the Terpenoid Cyclases

Christianson, D. W. (2006) · Chemical Reviews · doi:10.1021/cr050286w · Cited by 788

Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites

Que, L., & Ho, R. Y. N. (1996) · Chemical Reviews · doi:10.1021/cr960039f · Cited by 730

Epothilones, a new class of microtubule-stabilizing agents with a taxol-like mechanism of action.

Bollag, D. M., McQueney, P. A., Zhu, J., Hensens, O. D., Koupal, L. R., Liesch, J. M., Goetz, M., Lazarides, E., & Woods, C. M. (1995) · PubMed · Cited by 685

A Novel Mycolic Acid Cyclopropane Synthetase Is Required for Cording, Persistence, and Virulence of Mycobacterium tuberculosis

Glickman, M. S., Cox, J. S., & Jacobs, W. R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80250-6 · Cited by 655

Biosynthesis and Metabolism of Cyclopropane Rings in Natural Compounds

Wessjohann, L. A., Brandt, W., & Thiemann, T. (2003) · Chemical Reviews · doi:10.1021/cr0100188 · Cited by 640

Cyclopropane ring formation in membrane lipids of bacteria.

Grogan, D. W., & Cronan, J. E. (1997) · Microbiology and molecular biology reviews : MMBR · doi:10.1128/.61.4.429-441.1997 · Cited by 610

DNA Cross-Linking Agents as Antitumor Drugs

Rajski, S. R., & Williams, R. M. (1998) · Chemical Reviews · doi:10.1021/cr9800199 · Cited by 592

Biosynthesis and catabolism of monoterpenoids

Croteau, R. (1987) · Chemical Reviews · doi:10.1021/cr00081a004 · Cited by 590

Mycolic acids: structure, biosynthesis and physiological functions

Barry, C. E., Lee, R. E., Mdluli, K., Sampson, A. E., Schroeder, B. G., Slayden, R. A., & Yuan, Y. (1998) · Progress in Lipid Research · doi:10.1016/s0163-7827(98)00008-3 · Cited by 565

Biosynthesis of isoprenoid compounds

(1982) · Comparative Biochemistry and Physiology Part A: Physiology · doi:10.1016/0300-9629(82)90284-5 · Cited by 552

Epothilone A and B—Novel 16‐Membered Macrolides with Cytotoxic Activity: Isolation, Crystal Structure, and Conformation in Solution

Höfle, G., Bedorf, N., Steinmetz, H., Schomburg, D., Gerth, K., & Reichenbach, H. (1996) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199615671 · Cited by 515

Activities of the Microtubule-stabilizing Agents Epothilones A and B with Purified Tubulin and in Cells Resistant to Paclitaxel (Taxol®)

Kowalski, R. J., Giannakakou, P., & Hamel, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2534 · Cited by 511

Chemical and Pharmacological Research of the Plants in Genus Euphorbia

Shi, Q.-W., Su, X.-H., & Kiyota, H. (2008) · Chemical Reviews · doi:10.1021/cr078350s · Cited by 496

5-Lipoxygenase: regulation of expression and enzyme activity

Rådmark, O., Werz, O., Steinhilber, D., & Samuelsson, B. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.06.002 · Cited by 471

Isolation and Structure of a Covalent Cross-Link Adduct Between Mitomycin C and DNA

Tomasz, M., Lipman, R., Chowdary, D., Pawlak, J., Verdine, G. L., & Nakanishi, K. (1987) · Science · doi:10.1126/science.3103215 · Cited by 452

Suicide substrates: mechanism-based enzyme inactivators

Walsh, C. (1982) · Tetrahedron · doi:10.1016/0040-4020(82)85068-0 · Cited by 447

Cloning and Heterologous Expression of the Epothilone Gene Cluster

Tang, L., Shah, S., Chung, L., Carney, J., Katz, L., Khosla, C., & Julien, B. (2000) · Science · doi:10.1126/science.287.5453.640 · Cited by 424

Synthesis of epothilones A and B in solid and solution phase

Nicolaou, K. C., Winssinger, N., Pastor, J., Ninkovic, S., Sarabia, F., He, Y., Vourloumis, D., Yang, Z., Li, T., Giannakakou, P., et al. (1997) · Nature · doi:10.1038/387268a0 · Cited by 400

Cyclopropane Derivatives and their Diverse Biological Activities

Salaün, J. (2000) · Topics in Current Chemistry · doi:10.1007/3-540-48255-5_1 · Cited by 361

Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory

Shaik, S., de Visser, S. P., Ogliaro, F., Schwarz, H., & Schröder, D. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00363-0 · Cited by 357

Acyl‐CoA dehydrogenases: A mechanistic overview

Ghisla, S., & Thorpe, C. (2004) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03946.x · Cited by 344

Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis

Köksal, M., Jin, Y., Coates, R. M., Croteau, R., & Christianson, D. W. (2011) · Nature · doi:10.1038/nature09628 · Cited by 343

Biosynthesis of Phosphonic and Phosphinic Acid Natural Products

Metcalf, W. W., & van der Donk, W. A. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.091707.100215 · Cited by 336

Prostratin: activation of latent HIV-1 expression suggests a potential inductive adjuvant therapy for HAART

Kulkosky, J., Culnan, D. M., Roman, J., Dornadula, G., Schnell, M., Boyd, M. R., & Pomerantz, R. J. (2001) · Blood · doi:10.1182/blood.v98.10.3006 · Cited by 329

Dioxygenase enzymes: catalytic mechanisms and chemical models

Bugg, T. D. H. (2003) · Tetrahedron · doi:10.1016/s0040-4020(03)00944-x · Cited by 329

Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis

Vaillancourt, F. H., Yeh, E., Vosburg, D. A., O'Connor, S. E., & Walsh, C. T. (2005) · Nature · doi:10.1038/nature03797 · Cited by 322

Bacterial dehalogenation

Fetzner, S. (1998) · Applied Microbiology and Biotechnology · doi:10.1007/s002530051346 · Cited by 318

Oxidizing species in the mechanism of cytochrome P450

Ortiz de Montellano, P. R., & De Voss, J. J. (2002) · Natural Product Reports · doi:10.1039/b101297p · Cited by 317

Dynemicin A, a novel antibiotic with the anthraquinone and 1,5-diyn-3-ene subunit.

KONISHI, M., OHKUMA, H., MATSUMOTO, K., TSUNO, T., KAMEI, H., MIYAKI, T., OKI, T., KAWAGUCHI, H., VANDUYNE, G. D., & CLARDY, J. (1989) · The Journal of Antibiotics · doi:10.7164/antibiotics.42.1449 · Cited by 301

Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes

Lee, D.-S., Nioche, P., Hamberg, M., & Raman, C. S. (2008) · Nature · doi:10.1038/nature07307 · Cited by 293

The Organic Chemistry of Drug Design and Drug Action

Cooper, M. E. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03199-x · Cited by 292

The mitomycin bioreductive antitumor agents: Cross-linking and alkylation of DNA as the molecular basis of their activity

Tomasz, M., & Palom, Y. (1997) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(97)00088-0 · Cited by 283

Hypersensitive Radical Probes and the Mechanisms of Cytochrome P450-Catalyzed Hydroxylation Reactions

Newcomb, M., & Toy, P. H. (2000) · Accounts of Chemical Research · doi:10.1021/ar960058b · Cited by 274

Rational Conversion of Substrate and Product Specificity in a Salvia Monoterpene Synthase: Structural Insights into the Evolution of Terpene Synthase Function

Kampranis, S. C., Ioannidis, D., Purvis, A., Mahrez, W., Ninga, E., Katerelos, N. A., Anssour, S., Dunwell, J. M., Degenhardt, J., Makris, A. M., et al. (2007) · The Plant Cell · doi:10.1105/tpc.106.047779 · Cited by 254

Bioactive natural products with carbon–phosphorus bonds and their biosynthesis

Seto, H., Kuzuyama, T., Seto, H., & Kuzuyama, T. (1999) · Natural Product Reports · doi:10.1039/a809398i · Cited by 253

Monoterpene Synthases from Common Sage (Salvia officinalis )

Wise, M. L., Savage, T. J., Katahira, E., & Croteau, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.14891 · Cited by 245

Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.

Kim, J. J., Wang, M., & Paschke, R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7523 · Cited by 241

Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen.

Corey, E. J., Matsuda, S. P., & Bartel, B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.11628 · Cited by 240

Crystal Structure of Human Squalene Synthase

Pandit, J., Danley, D. E., Schulte, G. K., Mazzalupo, S., Pauly, T. A., Hayward, C. M., Hamanaka, E. S., Thompson, J. F., & Harwood, H. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004132200 · Cited by 238

Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule

Rao, V., Fujiwara, N., Porcelli, S. A., & Glickman, M. S. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20041668 · Cited by 238

Multi-State Epoxidation of Ethene by Cytochrome P450: A Quantum Chemical Study

de Visser, S. P., Ogliaro, F., Harris, N., & Shaik, S. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003544+ · Cited by 236

Volatile leaf oil analysis in chemosystematic studies of North American conifers

von Rudloff, E. (1975) · Biochemical Systematics and Ecology · doi:10.1016/0305-1978(75)90055-1 · Cited by 230

Molecular cloning of hyoscyamine 6 beta-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger

Matsuda, J., Okabe, S., Hashimoto, T., & Yamada, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92843-7 · Cited by 220

Chain elongation in the isoprenoid biosynthetic pathway

Kellogg, B. A., & Poulter, C. D. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80054-3 · Cited by 215

Practical Synthesis of Prostratin, DPP, and Their Analogs, Adjuvant Leads Against Latent HIV

Wender, P. A., Kee, J., & Warrington, J. M. (2008) · Science · doi:10.1126/science.1154690 · Cited by 214

Traumatic resin defense in Norway spruce (Picea abies): Methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase

Fäldt, J., Martin, D., Miller, B., Rawat, S., & Bohlmann, J. (2003) · Plant Molecular Biology · doi:10.1023/a:1020714403780 · Cited by 211

Characterization of the Interaction of Ingenol 3-Angelate with Protein Kinase C

Kedei, N., Lundberg, D. J., Toth, A., Welburn, P., Garfield, S. H., & Blumberg, P. M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3403 · Cited by 209

Biochemical Characterization of StyAB from Pseudomonas sp. Strain VLB120 as a Two-Component Flavin-Diffusible Monooxygenase

Otto, K., Hofstetter, K., Röthlisberger, M., Witholt, B., & Schmid, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.16.5292-5302.2004 · Cited by 205

The Diverse Roles of Flavin CoenzymesNature's Most Versatile Thespians

Mansoorabadi, S. O., Thibodeaux, C. J., & Liu, H.-W. (2007) · The Journal of Organic Chemistry · doi:10.1021/jo0703092 · Cited by 198

Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis.

Yuan, Y., Lee, R. E., Besra, G. S., Belisle, J. T., & Barry, C. E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6630 · Cited by 197

Duocarmycin A, a new antitumor antibiotic from Streptomyces.

TAKAHASHI, I., TAKAHASHI, K.-I., ICHIMURA, M., MORIMOTO, M., ASANO, K., KAWAMOTO, I., TOMITA, F., & NAKANO, H. (1988) · The Journal of Antibiotics · doi:10.7164/antibiotics.41.1915 · Cited by 194

Chimeras of Two Isoprenoid Synthases Catalyze All Four Coupling Reactions in Isoprenoid Biosynthesis

Thulasiram, H. V., Erickson, H. K., & Poulter, C. D. (2007) · Science · doi:10.1126/science.1137786 · Cited by 191

Crystal Structures of Mycolic Acid Cyclopropane Synthases from Mycobacterium tuberculosis

Huang, C.-C., Smith, C. V., Glickman, M. S., Jacobs, W. R., & Sacchettini, J. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111698200 · Cited by 191

Isoprenoid biosynthesis: manifold chemistry catalyzed by similar enzymes

Wendt, K. U., & Schulz, G. E. (1998) · Structure · doi:10.1016/s0969-2126(98)00015-x · Cited by 187

The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism (1967 to 1999)

Prescott, A. G., & Lloyd, M. D. (2000) · Natural Product Reports · doi:10.1039/a902197c · Cited by 180

Metamorphic enzyme assembly in polyketide diversification

Gu, L., Wang, B., Kulkarni, A., Geders, T. W., Grindberg, R. V., Gerwick, L. G., Håkansson, K., Wipf, P., Smith, J. L., Gerwick, W. H., et al. (2009) · Nature · doi:10.1038/nature07870 · Cited by 176

Molecular characterization and analysis of the biosynthetic gene cluster for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL 2564

Mao, Y., Varoglu, M., & Sherman, D. H. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80040-4 · Cited by 175

The Biosynthesis of Cyclopropanated Mycolic Acids in Mycobacterium tuberculosis

George, K. M., Yuan, Y., Sherman, D. R., & Barry, C. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27292 · Cited by 173

Stereospecific Biocatalytic Epoxidation: The First Example of Direct Regeneration of a FAD-Dependent Monooxygenase for Catalysis

Hollmann, F., Lin, P.-C., Witholt, B., & Schmid, A. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034119u · Cited by 172

Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides

Schirmer, A., Kennedy, J., Murli, S., Reid, R., & Santi, D. V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600445103 · Cited by 169

A Gene Cluster from a Marine Streptomyces Encoding the Biosynthesis of the Aromatic Spiroketal Polyketide Griseorhodin A

Li, A., & Piel, J. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00223-5 · Cited by 159

Solubilization and partial characterization of rat liver squalene epoxidase

Ono, T., & Bloch, K. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41847-4 · Cited by 157

Two‐step epoxidation of hyoscyamine to scopolamine is catalyzed by bifunctional hyoscyamine 6β‐hydroxylase

Hashimoto, T., Matsuda, J., & Yamada, Y. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80187-y · Cited by 154

Carbocyclic fatty acids in plants: Biochemical and molecular genetic characterization of cyclopropane fatty acid synthesis of Sterculia foetida

Bao, X., Katz, S., Pollard, M., & Ohlrogge, J. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092152999 · Cited by 149

Purification and characterization of hyoscyamine 6β‐hydroxylase from root cultures of Hyoscyamus niger L.

Hashimoto, T., & Yamada, Y. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11055.x · Cited by 147

Kinetics, Stoichiometry, and Identification of the Reactive Thiolate in the Inactivation of UDP-GlcNAc Enolpyruvoyl Transferase by the Antibiotic Fosfomycin

Marquardt, J. L., Brown, E. D., Lane, W. S., Haley, T. M., Ichikawa, Y., Wong, C., & Walsh, C. T. (1994) · Biochemistry · doi:10.1021/bi00201a011 · Cited by 145

Monoterpene Biosynthesis

Wise, M. L., & Croteau, R. (1999) · Elsevier eBooks · doi:10.1016/b978-0-08-091283-7.00038-2 · Cited by 144

Vitamin K and Energy Transduction: A Base Strength Amplification Mechanism

Dowd, P., Hershline, R., Ham, S. W., et al. (1995) · Science · doi:10.1126/science.7569894 · Cited by 142

Cloning of casbene synthase cDNA: evidence for conserved structural features among terpenoid cyclases in plants.

Mau, C. J. D., & West, C. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8497 · Cited by 139

Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short‐chain dehydrogenase/reductase fold without an NAD(P)H binding site

de Jong, R. M., Tiesinga, J. J. W., Rozeboom, H. J., Kalk, K. H., Tang, L., Janssen, D. B., & Dijkstra, B. W. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg479 · Cited by 129

A Complete Gene Cluster from Streptomyces nanchangensis NS3226 Encoding Biosynthesis of the Polyether Ionophore Nanchangmycin

Sun, Y., Zhou, X., Dong, H. F., Guo-quan, T., Wang, M., Wang, B., & Deng, Z. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00092-9 · Cited by 127

Formation of oxylipins by CYP74 enzymes

Stumpe, M., & Feußner, I. (2006) · Phytochemistry Reviews · doi:10.1007/s11101-006-9038-9 · Cited by 126

Insights into Polyether Biosynthesis from Analysis of the Nigericin Biosynthetic Gene Cluster in Streptomyces sp. DSM4137

Harvey, B. M., Mironenko, T., Sun, Y., Hong, H., Deng, Z., Leadlay, P. F., Weissman, K. J., & Haydock, S. F. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.05.011 · Cited by 124

Substrate activation by iron superoxo intermediates

van der Donk, W. A., Krebs, C., & Bollinger, J. M., Jr. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.005 · Cited by 121

Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene 1 1Edited by R. Huber

Capitani, G., Hohenester, E., Feng, L., Storici, P., Kirsch, J. F., & Jansonius, J. N. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3255 · Cited by 121

Identification of a Naturally Occurring Peroxidase-Lipoxygenase Fusion Protein

Koljak, R., Boutaud, O. G., Shieh, B., et al. (1997) · Science · doi:10.1126/science.277.5334.1994 · Cited by 120

Novel interstrand cross-links induced by the antitumor antibiotic carzinophilin/azinomycin B

Armstrong, R. W., Salvati, M., & Nguyen, M. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00034a074 · Cited by 120

Reactivity patterns of cytochrome P450 enzymes: multifunctionality of the active species, and the two states–two oxidants conundrum

Shaik, S. S., Hirao, H., & Kumar, D. (2007) · Natural Product Reports · doi:10.1039/b604192m · Cited by 120

Flavin-Dependent Enzymes

Fagan, R. L., & Palfey, B. A. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00135-0 · Cited by 116

A novel antifungal antibiotic, FR-900848. I. Production, isolation, physico-chemical and biological properties.

Yoshida, M., Ezaki, M., Hashimoto, M., Yamashita, M., Shigematsu, N., OKUHARA, M., KOHSAKA, M., & Horikoshi, K. (1990) · The Journal of Antibiotics · doi:10.7164/antibiotics.43.748 · Cited by 112

Revisiting Heme Mechanisms. A Perspective on the Mechanisms of Nitric Oxide Synthase (NOS), Heme Oxygenase (HO), and Cytochrome P450s (CYP450s)

Zhu, Y., & Silverman, R. B. (2008) · Biochemistry · doi:10.1021/bi7023817 · Cited by 112

Molecular cloning, characterization, and overexpression of ERG7, the Saccharomyces cerevisiae gene encoding lanosterol synthase.

Corey, E. J., Matsuda, S., & Bartel, B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2211 · Cited by 111

Cloning of casbene and neocembrene synthases from Euphorbiaceae plants and expression in Saccharomyces cerevisiae

Kirby, J., Nishimoto, M., Park, J. G., Withers, S. T., Nowroozi, F. F., Behrendt, D., Rutledge, E. J. G., Fortman, J. L., Johnson, H. E., Anderson, J. V., et al. (2010) · Phytochemistry · doi:10.1016/j.phytochem.2010.06.001 · Cited by 108

Biosynthesis of pentalenene and pentalenolactone

Cane, D. E., Oliver, J. S., Harrison, P. H. M., Abell, C., Hubbard, B. R., Kane, C. T. J., & Lattman, R. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00167a059 · Cited by 106

Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase

Kantz, A., Chin, F., Nallamothu, N., Nguyen, T., & Gassner, G. T. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.020 · Cited by 102

A Multifunctional Lipoxygenase with Fatty Acid Hydroperoxide Cleaving Activity from the Moss Physcomitrella patens

Senger, T., Wichard, T., Kunze, S., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411738200 · Cited by 101

The Hedamycin Locus Implicates a Novel Aromatic PKS Priming Mechanism

Bililign, T., Hyun, C., Williams, J. S., Czisny, A. M., & Thorson, J. S. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.04.016 · Cited by 101

Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon–halogen bond

de Jong, R. M., & Dijkstra, B. W. (2003) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.10.009 · Cited by 97

Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.

Shi, Z., Buntel, C. J., & Griffin, J. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7370 · Cited by 97

The manumycin-group metabolites

Sattler, I., Thiericke, R., & Zeeck, A. (1998) · Natural Product Reports · doi:10.1039/a815221y · Cited by 95

Catalysis of the CC-1065 and duocarmycin DNA alkylation reaction: DNA binding induced conformational change in the agent results in activation

Boger, D. L., & Garbaccio, R. M. (1997) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(96)00238-6 · Cited by 88

The biosynthesis of polyketide-derived polycyclic ethers

Gallimore, A. R. (2008) · Natural Product Reports · doi:10.1039/b807902c · Cited by 88

Functional Analysis of MycCI and MycG, Cytochrome P450 Enzymes Involved in Biosynthesis of Mycinamicin Macrolide Antibiotics

Anzai, Y., Li, S., Chaulagain, M. R., Kinoshita, K., Kato, F., Montgomery, J., & Sherman, D. H. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.07.014 · Cited by 88

Biosynthesis of non-head-to-tail terpenes. Formation of 1'-1 and 1'-3 linkages

Poulter, C. (1990) · Accounts of Chemical Research · doi:10.1021/ar00171a003 · Cited by 87

The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide

Oldham, M. L., BRASH, A. R., & Newcomer, M. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406352102 · Cited by 86

Analysis of the Tetronomycin Gene Cluster: Insights into the Biosynthesis of a Polyether Tetronate Antibiotic

Demydchuk, Y. A., Sun, Y., Hong, H., Staunton, J., Spencer, J. B., & Leadlay, P. F. (2008) · ChemBioChem · doi:10.1002/cbic.200700715 · Cited by 82

Crystal Structures of Epothilone D-bound, Epothilone B-bound, and Substrate-free Forms of Cytochrome P450epoK

Nagano, S., Li, H., Shimizu, H., Nishida, C. R., Ogura, H., de Montellano, P. R. O., & Poulos, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308115200 · Cited by 82

Structure and Ligand Binding Properties of the Epoxidase Component of Styrene Monooxygenase,

Ukaegbu, U. E., Kantz, A., Beaton, M., Gassner, G. T., & Rosenzweig, A. C. (2010) · Biochemistry · doi:10.1021/bi901693u · Cited by 80

Isolation and characterization of the duocarmycin-adenine DNA adduct

Boger, D. L., Ishizaki, T., & Zarrinmayeh, H. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00017a042 · Cited by 80

Biosynthetic studies of marine lipids. 41. Sponge sterols: origin and biosynthesis

Djerassi, C., & Silva, C. J. (1991) · Accounts of Chemical Research · doi:10.1021/ar00012a003 · Cited by 77

The biosynthetic genes encoding for the production of the dynemicin enediyne core inMicromonospora chersinaATCC53710

Gao, Q., & Thorson, J. S. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01112.x · Cited by 76

Genome Mining in Streptomyces. Elucidation of the Role of Baeyer−Villiger Monooxygenases and Non-Heme Iron-Dependent Dehydrogenase/Oxygenases in the Final Steps of the Biosynthesis of Pentalenolactone and Neopentalenolactone

Seo, M., Zhu, D., Endo, S., Ikeda, H., & Cane, D. E. (2011) · Biochemistry · doi:10.1021/bi1019786 · Cited by 73

Further Insight into S-Adenosylmethionine-dependent Methyltransferases

Boissier, F., Bardou, F., Guillet, V., Uttenweiler‐Joseph, S., Daffé, M., Quémard, A., & Mourey, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510250200 · Cited by 73

Biosynthesis of the Diterpene Phytoalexin Casbene

Dueber, M. T., Adolf, W., & West, C. A. (1978) · PLANT PHYSIOLOGY · doi:10.1104/pp.62.4.598 · Cited by 69

Biochemical and Genetic Insights into Asukamycin Biosynthesis

Rui, Z., Petřı́čková, K., Škanta, F., Pospíšil, S., Yang, Y., Chen, C., Tsai, S., Floss, H. G., Petřı́ček, M., & Yu, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.128850 · Cited by 67

Prostacyclin and Thromboxane Synthase: New Aspects of Hemethiolate Catalysis

Ullrich, V., & Brugger, R. (1994) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199419111 · Cited by 67

Enzyme Redesign: Two Mutations Cooperate to Convert Cycloartenol Synthase into an Accurate Lanosterol Synthase

Lodeiro, S., Schulz‐Gasch, T., & Matsuda, S. P. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja053791j · Cited by 66

Stereochemical Course of Enzymatic Enolpyruvyl Transfer and Catalytic Conformation of the Active Site Revealed by the Crystal Structure of the Fluorinated Analogue of the Reaction Tetrahedral Intermediate Bound to the Active Site of the C115A Mutant of MurA

Skarzynski, T. J., Kim, D. H., Lees, W. J., Walsh, C. T., & Duncan, K. (1998) · Biochemistry · doi:10.1021/bi9722608 · Cited by 64

Studies on the biosynthesis of cyclopropane fatty acids in Escherichia coli

Cronan, J. E., Nunn, W. D., & Batchelor, J. G. (1974) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(74)90093-9 · Cited by 62

18O Kinetic Isotope Effects in Non-Heme Iron Enzymes: Probing the Nature of Fe/O2 Intermediates

Mirica, L. M., McCusker, K. P., Munos, J. W., Liu, H., & Klinman, J. P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja800265s · Cited by 62

Saccharomyces cerevisiae oxidosqualene‐lanosterol cyclase: A chemistry–biology interdisciplinary study of the protein's structure–function–reaction mechanism relationships

Wu, T., Chang, C.-H., Liu, Y., & Wang, T.-T. (2008) · The Chemical Record · doi:10.1002/tcr.20157 · Cited by 56

Elucidation of enzyme mechanisms using fluorinated substrate analogues

Pongdee, R., & Liu, H. (2004) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2004.06.012 · Cited by 54

Characterization of the Aminocarboxycyclopropane-Forming Enzyme CmaC

Kelly, W. L., Boyne, M. T., Yeh, E., Vosburg, D. A., Galonić, D. P., Kelleher, N. L., & Walsh, C. T. (2006) · Biochemistry · doi:10.1021/bi061930j · Cited by 47

RÖMPP Encyclopedia Natural Products

Steglich, W., Fugmann, B., Lang-Fugmann, S., et al. (2000) · Thieme eBooks · doi:10.1055/b-003-125715 · Cited by 44

Monoterpene biosynthesis: Demonstration of a geranyl pyrophosphate: Sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis)

Hallahan, T., & Croteau, R. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90328-1 · Cited by 44

Biosynthesis of the mitomycin antibiotics from 3-amino-5-hydroxybenzoic acid

Anderson, M. G., Kibby, J. J., Rickards, R. W., & Rothschild, J. M. (1980) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39800001277 · Cited by 44

The Nonribosomal Peptide Synthetase Enzyme DdaD Tethers Nβ-Fumaramoyl- l -2,3-diaminopropionate for Fe(II)/α-Ketoglutarate-Dependent Epoxidation by DdaC during Dapdiamide Antibiotic Biosynthesis

Hollenhorst, M. A., Bumpus, S. B., Matthews, M. L., Bollinger, J. M., Jr., Kelleher, N. L., & Walsh, C. T. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1072367 · Cited by 43

Cloning and Characterization of the Biosynthetic Gene Cluster of 16‐Membered Macrolide Antibiotic FD‐891: Involvement of a Dual Functional Cytochrome P450 Monooxygenase Catalyzing Epoxidation and Hydroxylation

Kudo, F., Motegi, A., Mizoue, K., & Eguchi, T. (2010) · ChemBioChem · doi:10.1002/cbic.201000214 · Cited by 42

Structural Basis of Regiospecificity of a Mononuclear Iron Enzyme in Antibiotic Fosfomycin Biosynthesis

Yun, D., Dey, M., Higgins, L., Feng, Y. F., Liu, H., & Drennan, C. L. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2025728 · Cited by 41

Covalent Structure of the DNA-DNA Interstrand Cross-Link Formed by Reductively Activated FR66979 in Synthetic DNA Duplexes

Huang, H., Pratum, T. K., & Hopkins, P. B. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00086a002 · Cited by 39

Squalene Epoxidase and Oxidosqualene : Lanosterol Cyclase—Key Enzymes in Cholesterol Biosynthesis

Abe, I., & Prestwich, G. D. (1999) · Elsevier eBooks · doi:10.1016/b978-0-08-091283-7.00045-x · Cited by 39

Escherichia coli Cyclopropane Fatty Acid Synthase: Is a Bound Bicarbonate Ion the Active-Site Base?

Courtois, F., & Ploux, O. (2005) · Biochemistry · doi:10.1021/bi051159x · Cited by 38

Thoughts on thiolate tethering. Tribute and thanks to a teacher

Ullrich, V. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00410-1 · Cited by 33

Determination of the Substrate Binding Mode to the Active Site Iron of (S)-2-Hydroxypropylphosphonic Acid Epoxidase Using 17O-Enriched Substrates and Substrate Analogues

Feng, Y. F., Moon, S.-J., Liu, P., Zhao, Z. K., Lipscomb, J. D., Liu, A., & Liu, H. (2007) · Biochemistry · doi:10.1021/bi701370e · Cited by 32

On the identity and reactivity patterns of the “second oxidant” of the T252A mutant of cytochrome P450cam in the oxidation of 5-methylenenylcamphor

Hirao, H., Kumar, D., & Shaik, S. S. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.09.001 · Cited by 30

Biosynthesis of Fosfomycin, Re-Examination and Re-Confirmation of a Unique Fe(II)- and NAD(P)H-Dependent Epoxidation Reaction

Feng, Y. F., Munos, J. W., Liu, P., & Liu, H. (2006) · Biochemistry · doi:10.1021/bi060839c · Cited by 29

A cDNA clone for 3-carene synthase from Salvia stenophylla☆☆The nucleotide sequence reported in this article has been deposited with the GenBank/EMBL Database under accession number AF527416.

Hoelscher, D. J., Williams, D. C., Wildung, M. R., & Croteau, R. (2003) · Phytochemistry · doi:10.1016/s0031-9422(02)00674-x · Cited by 27

Epoxyquinones from 2,5-dihydroxyacetanilide: opposite facial specificity in the epoxidation by enzymes from Streptomyces LL-C10037 and Streptomyces MPP 3051

Gould, S. J., & Shen, B. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00002a052 · Cited by 25

Incorporation of Two Oxygens from 18O2 in the Epoxyquinone from the Dihydroxyacetanilide Epoxidase Reaction: Evidence for a Dioxygenase Mechanism

Gould, S. J., Kirchmeier, M. J., & LaFever, R. E. (1996) · Journal of the American Chemical Society · doi:10.1021/ja960696p · Cited by 25

Chrysanthemyl Diphosphate Synthase. The Relationship among Chain Elongation, Branching, and Cyclopropanation Reactions in the Isoprenoid Biosynthetic Pathway

Erickson, H. K., & Poulter, C. D. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034520g · Cited by 23

Mevalonate Pathway in Bacteria and Archaea

Kuzuyama, T., Hemmi, H., & Takahashi, S. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00014-9 · Cited by 21

Insight into the reaction mechanism of the Escherichia coli cyclopropane fatty acid synthase: Isotope exchange and kinetic isotope effects

Guangqi, E., Lesage, D., & Ploux, O. (2010) · Biochimie · doi:10.1016/j.biochi.2010.05.019 · Cited by 12

The biosynthesis of manumycin; origin of the oxygen and nitrogen atoms

Thiericke, R., Zeeck, A., Robinson, J. A., Beale, J. M., & Floss, H. G. (1989) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39890000402 · Cited by 12

Mycolic Acid/Cyclopropane Fatty Acid/Fatty Acid Biosynthesis and Health Relations

Kastrinsky, D. B., McBride, N. S., Backus, K. M., LeBlanc, J. J., & Barry, C. E. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00029-0 · Cited by 9

Antitumor activity of asukamycin, a secondary metabolite from the actinomycete bacterium Streptomyces nodosus subspecies asukaensis

Klegeris (2009) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000283 · Cited by 8

Prenyltransferase

Kurokawa, H., & Koyama, T. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00002-2 · Cited by 6

Bacterial Squalene Cyclase

Abe, I. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00737-1 · Cited by 2

Nonproteinogenic Amino Acid Building Blocks for Nonribosomal Peptide and Hybrid Polyketide Scaffolds

Walsh, C. T., O'Brien, R. V., & Khosla, C. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208344 · Cited by 406

Flavoenzymes: Versatile catalysts in biosynthetic pathways

Walsh, C. T., & Wencewicz, T. A. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20069d · Cited by 373

The colibactin warhead crosslinks DNA

Vizcaino, M. I., & Crawford, J. M. (2015) · Nature Chemistry · doi:10.1038/nchem.2221 · Cited by 247