Cyclopropane derivatives as potential human serine racemase inhibitors: unveiling novel insights into a difficult target

References

• Hashimoto A, Nishikawa T, Hayashi T, et al. The presence of free d-serine in rat brain. FEBS Lett 1992;296:33–6
   PubMed Web of Science ®Google Scholar
• Hashimoto A, Oka T. Free d-aspartate and d-serine in the mammalian brain and periphery. Prog Neurobiol 1997;52:325–53
   PubMed Web of Science ®Google Scholar
• Soglia JR, Contillo LG, Kalgutkar AS, et al. A semiquantitative method for the determination of reactive metabolite conjugate levels in vitro utilizing liquid chromatography – tandem mass spectrometry and novel quaternary ammonium glutathione analogues. Chem Res Toxicol 2006;19:480–90
   PubMed Web of Science ®Google Scholar
• Conti P, Tamborini L, Pinto A, et al. Drug discovery targeting amino acid racemases. Chem Rev 2011;111:6919–46
   PubMed Web of Science ®Google Scholar
• Matsui TA, Sekiguchi M, Hashimoto A, et al. Functional comparison of d-serine and glycine in rodents: the effect on cloned NMDA receptors and the extracellular concentration. J Neurochem 1995;65:454–8
   PubMed Web of Science ®Google Scholar
• Mothet JP, Parent AT, Wolosker H, et al. d-serine is an endogenous ligand for the glycine site of the N-methyl-d-aspartate receptor. Proc Natl Acad Sci 2000;97:4926–31
   PubMed Web of Science ®Google Scholar
• Wolosker H, Blackshaw S, Snyder SH. Serine racemase: a glial enzyme synthesizing d-serine to regulate glutamate-N-methyl-d-aspartate neurotransmission. Proc Natl Acad Sci 1999;96:13409–14
   PubMed Web of Science ®Google Scholar
• Santangelo RM, Acker TM, Zimmerman SS, et al. Novel NMDA receptor modulators: an update. Expert Opin Thera Pat 2012;22:1337–52
   PubMed Web of Science ®Google Scholar
• Van-Horn MR, Sild M, Ruthazer ES. d-Serine as a gliotransmitter and its roles in brain development and disease. Front Cell Neurosci 2013;7:39. doi: 10.3389/fncel.2013.00039
   Google Scholar
• Amadasi A, Bertoldi M, Contestabile R, et al. Pyridoxal 5′-phosphate enzymes as targets for therapeutic agents. Curr Med Chem 2007;14:1291–324
   PubMed Web of Science ®Google Scholar
• Marchetti M, Bruno S, Campanini B, et al. Regulation of human serine racemase activity and dynamics by halides, ATP and malonate. Amino Acids 2015;47:163–73
   PubMed Web of Science ®Google Scholar
• Wolosker H. NMDA receptor regulation by d-serine: new findings and perspectives. Mol Neurobiol 2007;36:152–64
   PubMed Web of Science ®Google Scholar
• Campanini B, Spyrakis F, Peracchi A, Mozzarelli A. Serine racemase: a key player in neuron activity and in neuropathologies. Front Biosci 2013;18:1112–28
   Web of Science ®Google Scholar
• Campanini B, Pieroni M, Raboni S, et al. Inhibitors of the sulfur assimilation pathway in bacterial pathogens as enhancers of antibiotic therapy. Curr Med Chem 2015;22:187–213
   PubMed Web of Science ®Google Scholar
• De Miranda J, Panizzutti R, Foltyn VN, Wolosker H. Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-d-aspartate (NMDA) receptor coagonist d-serine. Proc Natl Acad Sci 2002;99:14542–7
   PubMed Web of Science ®Google Scholar
• Verrall L, Walker M, Rawlings N, et al. d-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia. Eur J Neurosci 2007;26:1657–69
   PubMed Web of Science ®Google Scholar
• Xia M, Liu Y, Figueroa DJ, et al. Characterization and localization of a human serine racemase. Mol Brain Res 2004;125:96–104
   PubMedGoogle Scholar
• Wolosker H, Mori H. Serine racemase: an unconventional enzyme for an unconventional transmitter. Amino Acids 2012;43:1895–904
   PubMed Web of Science ®Google Scholar
• Stříšovský K, Jirásková J, Bařinka C, et al. Mouse brain serine racemase catalyzes specific elimination of l-serine to pyruvate. FEBS Lett 2003;535:44–8
   PubMed Web of Science ®Google Scholar
• Smith MA, Mack V, Ebneth A, et al. The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem 2010;285:12873–81
   PubMed Web of Science ®Google Scholar
• Goto M, Yamaouchi T, Kamiya N, et al. Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem 2009;284:25944–52
   PubMed Web of Science ®Google Scholar
• Yamauchi T, Goto M, Wu HY, et al. Serine racemase with catalytically active lysinoalanyl residue. J Biochem 2009;145:421–4
   PubMed Web of Science ®Google Scholar
• Jirásková-Vaníčková J, Ettrich R, Vorlová B, et al. Inhibition of human serine racemase, an emerging target for medicinal chemistry. Curr Drug Targets 2011;12:1037–55
   PubMed Web of Science ®Google Scholar
• Mori H, Wada R, Li J, et al. In silico and pharmacological screenings identify novel serine racemase inhibitors. Bioorg Med Chem Lett 2014;24:3732–5
   PubMed Web of Science ®Google Scholar
• Vorlová B, Nachtigallová D, Jirásková-Vaníčková J, et al. Malonate-based inhibitors of mammalian serine racemase: kinetic characterization and structure-based computational study. Eur J Med Chem 2015;89:189–97
   PubMed Web of Science ®Google Scholar
• Harty M, Nagar M, Atkinson L, et al. Inhibition of serine and proline racemases by substrate-product analogues. Bioorg Med Chem Lett 2014;24:390–3
   PubMed Web of Science ®Google Scholar
• Oprea TI, Davis AM, Teague SJ, Leeson PD. Is there a difference between leads and drugs? A historical perspective. J Chem Inf Comput Sci 2001;41:1308–15
   PubMedGoogle Scholar
• Amori L, Katkevica S, Bruno A, et al. Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase. MedChemCommun 2012;3:1111–16
   Web of Science ®Google Scholar
• Pieroni M, Annunziato G, Azzali E, et al. Further insights on the SAR of 1-substituted cyclopropylamine derivatives as inhibitors of histone demethylase KDM1A. Eur J Med Chem 2015;92:377–86
   PubMed Web of Science ®Google Scholar
• McCoy LL. Three-membered rings. The preparation of some 1,2-cyclopropanedicarboxylic acids. J Am Chem Soc 1959;80:6568–72
   Web of Science ®Google Scholar
• Zhao Q, Wong HNC. Synthetic studies toward plakortide E: application of the Feldman oxygenation to synthesis of highly substituted 1,2-dioxolanes. Tetrahedron 2007;63:6296–305
   Web of Science ®Google Scholar
• Marchetti M, Bruno S, Campanini B, et al. ATP binding to human serine racemase is cooperative and modulated by glycine. FEBS J 2013;280:5853–63
   PubMed Web of Science ®Google Scholar
• Bruno A, Amori L, Costantino G. Addressing the conformational flexibility of serine racemase by combining targeted molecular dynamics, conformational sampling and docking studies. Mol Inf 2011;30:317–28
   PubMed Web of Science ®Google Scholar
• LigPrep, version 2.8. New York, NY: Schrödinger, LLC; 2013
   Google Scholar
• Cleland WW, Frey PA, Gerlt JA. The low barrier hydrogen bond in enzymatic catalysis. J Biol Chem 1998;273:25529–32
   PubMed Web of Science ®Google Scholar
• Friesner RA, Banks JL, Murphy RB, et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 2004;47:1739–49
   PubMed Web of Science ®Google Scholar
• Halgren TA, Murphy RB, Friesner RA, et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem 2004;47:1750–9
   PubMed Web of Science ®Google Scholar
• Morris GM, Ruth H, Lindstrom W, et al. Software news and updates AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J Comput Chem 2009;30:2785–91
   PubMed Web of Science ®Google Scholar
• Korb O, Stützle T, Exner TE. PLANTS: application of ant colony optimization to structure-based drug design. Lecture Notes Comput Sci. 2006;4150:247–58
   Google Scholar
• Strisovsky K, Jiráskova J, Mikulová A, et al. Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the β-eliminase activity. Biochemistry 2005;44:13091–100
   PubMed Web of Science ®Google Scholar
• Hoffman HE, Jirásková J, Cígler P, et al. Hydroxamic acids as a novel family of serine racemase inhibitors: mechanistic analysis reveals different modes of interaction with the pyridoxal-5′-phosphate cofactor. J Med Chem 2009;52:6032–41
   PubMed Web of Science ®Google Scholar
• Cook SP, Galve-Roperh I, Del Pozo AM, Rodríguez-Crespo I. Direct calcium binding results in activation of brain serine racemase. J Biol Chem 2002;277:27782–92
   PubMed Web of Science ®Google Scholar
• Dixon SM, Li P, Liu R, et al. Slow-binding human serine racemase inhibitors from high-throughput screening of combinatorial libraries. J Med Chem 2006;49:2388–97
   PubMed Web of Science ®Google Scholar
• Major DT, Nam K, Gao J. Transition state stabilization and α-amino carbon acidity in alanine racemase. J Am Chem Soc 2006;128:8114–15
   PubMed Web of Science ®Google Scholar
• Major DT, Gao J. A combined quantum mechanical and molecular mechanical study of the reaction mechanism and α-amino acidity in alanine racemase. J Am Chem Soc 2006;128:16345–57
   PubMed Web of Science ®Google Scholar