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(12)
, 1929-1942. https://doi.org/10.1021/acs.biochem.3c00143
- Karen N. Allen, Christian P. Whitman. The Birth of Genomic Enzymology: Discovery of the Mechanistically Diverse Enolase Superfamily. Biochemistry 2021, 60
(46)
, 3515-3528. https://doi.org/10.1021/acs.biochem.1c00494
- Colin D. Douglas, Lia Grandinetti, Nicole M. Easton, Oliver P. Kuehm, Joshua A. Hayden, Meghan C. Hamilton, Martin St. Maurice, Stephen L. Bearne. Slow-Onset, Potent Inhibition of Mandelate Racemase by 2-Formylphenylboronic Acid. An Unexpected Adduct Clasps the Catalytic Machinery. Biochemistry 2021, 60
(32)
, 2508-2518. https://doi.org/10.1021/acs.biochem.1c00374
- Amar Nath Sharma, Lia Grandinetti, Erin R. Johnson, Martin St. Maurice, Stephen L. Bearne. Potent Inhibition of Mandelate Racemase by Boronic Acids: Boron as a Mimic of a Carbon Acid Center. Biochemistry 2020, 59
(33)
, 3026-3037. https://doi.org/10.1021/acs.biochem.0c00478
- Marc Nadal-Ferret, Ricard Gelabert, Miquel Moreno, and José M. Lluch . Are There Really Low-Barrier Hydrogen Bonds in Proteins? The Case of Photoactive Yellow Protein. Journal of the American Chemical Society 2014, 136
(9)
, 3542-3552. https://doi.org/10.1021/ja4116617
- M. Ashley Spies, Joseph G. Reese, Dylan Dodd, Katherine L. Pankow, Steven R. Blanke and Jerome Baudry . Determinants of Catalytic Power and Ligand Binding in Glutamate Racemase. Journal of the American Chemical Society 2009, 131
(14)
, 5274-5284. https://doi.org/10.1021/ja809660g
- John F. Rakus,, Alexander A. Fedorov,, Elena V. Fedorov,, Margaret E. Glasner,, Jacob E. Vick,, Patricia C. Babbitt,, Steven C. Almo, and, John A. Gerlt. Evolution of Enzymatic Activities in the Enolase Superfamily: d-Mannonate Dehydratase from Novosphingobium aromaticivorans,. Biochemistry 2007, 46
(45)
, 12896-12908. https://doi.org/10.1021/bi701703w
- M. Ashley Spies and, Michael D. Toney. Intrinsic Primary and Secondary Hydrogen Kinetic Isotope Effects for Alanine Racemase from Global Analysis of Progress Curves. Journal of the American Chemical Society 2007, 129
(35)
, 10678-10685. https://doi.org/10.1021/ja067643k
- Tina L. Amyes and, John P. Richard. Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite Dianion. Biochemistry 2007, 46
(19)
, 5841-5854. https://doi.org/10.1021/bi700409b
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(49)
, 14582-14597. https://doi.org/10.1021/bi061687o
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(49)
, 14598-14608. https://doi.org/10.1021/bi061688g
- Xavier Prat-Resina,, Àngels González-Lafont, and, José M. Lluch. Reaction Mechanism of the Mandelate Anion Racemization Catalyzed by Mandelate Racemase Enzyme: A QM/MM Molecular Dynamics Free Energy Study. The Journal of Physical Chemistry B 2005, 109
(44)
, 21089-21101. https://doi.org/10.1021/jp052239d
- C. Li,, Y. Xia,, X. Gao, and, P. D. Gershon. Mechanism of RNA 2‘-O-Methylation: Evidence that the Catalytic Lysine Acts To Steer Rather than Deprotonate the Target Nucleophile. Biochemistry 2004, 43
(19)
, 5680-5687. https://doi.org/10.1021/bi0359980
- Zhenlin Zhong,, Timothy S. Snowden,, Michael D. Best, and, Eric V. Anslyn. Rate of Enolate Formation Is Not Very Sensitive to the Hydrogen Bonding Ability of Donors to Carboxyl Oxygen Lone Pair Acceptors; A Ramification of the Principle of Non-Perfect Synchronization for General-Base-Catalyzed Enolate Formation. Journal of the American Chemical Society 2004, 126
(11)
, 3488-3495. https://doi.org/10.1021/ja0306011
- Luis F. Pacios. Topological Descriptors of the Electron Density and the Electron Localization Function in Hydrogen Bond Dimers at Short Intermonomer Distances. The Journal of Physical Chemistry A 2004, 108
(7)
, 1177-1188. https://doi.org/10.1021/jp030978t
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(1)
, 224-229. https://doi.org/10.1021/bi035815+
- Maite Roca,, Sergio Martí,, Juan Andrés,, Vicent Moliner,, Iñaki Tuñón,, Juan Bertrán, and, Ian H. Williams. Theoretical Modeling of Enzyme Catalytic Power: Analysis of “Cratic” and Electrostatic Factors in Catechol O-Methyltransferase. Journal of the American Chemical Society 2003, 125
(25)
, 7726-7737. https://doi.org/10.1021/ja0299497
- Martin E. Tanner. Understanding Nature's Strategies for Enzyme-Catalyzed Racemization and Epimerization. Accounts of Chemical Research 2002, 35
(4)
, 237-246. https://doi.org/10.1021/ar000056y
- Robert D. Bach,, Olga Dmitrenko, and, Mikhail N. Glukhovtsev. A Theoretical Study of the Effect of a Tetraalkylammonium Counterion on the Hydrogen Bond Strength in Z-Hydrogen Maleate. Journal of the American Chemical Society 2001, 123
(29)
, 7134-7145. https://doi.org/10.1021/ja010362m
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(11)
, 2478-2486. https://doi.org/10.1021/ja0009121
- Mary Jo Ondrechen,, James M. Briggs, and, J. Andrew McCammon. A Model for Enzyme−Substrate Interaction in Alanine Racemase. Journal of the American Chemical Society 2001, 123
(12)
, 2830-2834. https://doi.org/10.1021/ja0029679
- Mireia Garcia-Viloca,, Àngels González-Lafont, and, José M. Lluch. A QM/MM Study of the Racemization of Vinylglycolate Catalyzed by Mandelate Racemase Enzyme. Journal of the American Chemical Society 2001, 123
(4)
, 709-721. https://doi.org/10.1021/ja002879o
- Robert D. Bach,, Carlo Canepa, and, Mikhail N. Glukhovtsev. Influence of Electrostatic Effects on Activation Barriers in Enzymatic Reactions: Pyridoxal 5‘-Phosphate-Dependent Decarboxylation of α-Amino Acids. Journal of the American Chemical Society 1999, 121
(28)
, 6542-6555. https://doi.org/10.1021/ja9907616
- Mireia Garcia-Viloca,, Ricard Gelabert,, Àngels González-Lafont,, Miquel Moreno, and, José M. Lluch. Temperature Dependence of Proton NMR Chemical Shift As a Criterion To Identify Low-Barrier Hydrogen Bonds. Journal of the American Chemical Society 1998, 120
(39)
, 10203-10209. https://doi.org/10.1021/ja9742141
- David C. Hawkinson,, Jeffrey M. Feiock,, John B. Nevy, and, Yue-Zhong Wu. Enolization and Hydrolysis of 7-Nitroisochroman-3-one in Aqueous Solution: Generation of a Relatively Stable Lactone Enolate. The Journal of Organic Chemistry 1998, 63
(16)
, 5345-5349. https://doi.org/10.1021/jo980032t
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(7)
, 1623-1624. https://doi.org/10.1021/ja973140q
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(46)
, 8727-8733. https://doi.org/10.1021/jp972335h
- Y. Chiang,, A. J. Kresge,, V. V. Popik, and, N. P. Schepp. The Mandelic Acid Keto−Enol System in Aqueous Solution. Generation of the Enol by Hydration of Phenylhydroxyketene and Phenylcarboxycarbene. Journal of the American Chemical Society 1997, 119
(42)
, 10203-10212. https://doi.org/10.1021/ja971774r
- Mireia Garcia-Viloca,, Angels González-Lafont, and, José M. Lluch. On pKa Matching as a Requirement To Form a Low-Barrier Hydrogen Bond. A Theoretical Study in Gas Phase. The Journal of Physical Chemistry A 1997, 101
(21)
, 3880-3886. https://doi.org/10.1021/jp964031l
- Mireia Garcia-Viloca,, Angels González-Lafont, and, José M. Lluch. Theoretical Study of the Low-Barrier Hydrogen Bond in the Hydrogen Maleate Anion in the Gas Phase. Comparison with Normal Hydrogen Bonds. Journal of the American Chemical Society 1997, 119
(5)
, 1081-1086. https://doi.org/10.1021/ja962662n
- Patricia C. Babbitt,, Miriam S. Hasson,, Joseph E. Wedekind,, David R. J. Palmer,, William C. Barrett,, George H. Reed,, Ivan Rayment,, Dagmar Ringe,, George L. Kenyon, and, John A. Gerlt. The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids. Biochemistry 1996, 35
(51)
, 16489-16501. https://doi.org/10.1021/bi9616413
- Tina L. Amyes and, John P. Richard. Determination of the pKa of Ethyl Acetate: Brønsted Correlation for Deprotonation of a Simple Oxygen Ester in Aqueous Solution. Journal of the American Chemical Society 1996, 118
(13)
, 3129-3141. https://doi.org/10.1021/ja953664v
- David R. J. Palmer and, John A. Gerlt. Evolution of Enzymatic Activities: Multiple Pathways for Generating and Partitioning a Common Enolic Intermediate by Glucarate Dehydratase from Pseudomonas putida. Journal of the American Chemical Society 1996, 118
(42)
, 10323-10324. https://doi.org/10.1021/ja962126v
- Stephen L. Bearne. Capturing the free energy of transition state stabilization: insights from the inhibition of mandelate racemase. Philosophical Transactions of the Royal Society B: Biological Sciences 2023, 378
(1871)
https://doi.org/10.1098/rstb.2022.0041
- Stephen L. Bearne, Joshua A. Hayden. Application of circular dichroism-based assays to racemases and epimerases: Recognition and catalysis of reactions of chiral substrates by mandelate racemase. 2023, 127-169. https://doi.org/10.1016/bs.mie.2023.03.014
- Mitesh Nagar, Joshua A. Hayden, Einat Sagey, George Worthen, Mika Park, Amar Nath Sharma, Christopher M. Fetter, Oliver P. Kuehm, Stephen L. Bearne. Altering the binding determinant on the interdigitating loop of mandelate racemase shifts specificity towards that of d-tartrate dehydratase. Archives of Biochemistry and Biophysics 2022, 718 , 109119. https://doi.org/10.1016/j.abb.2022.109119
- . Organic Synthesis with Isomerases. 2022, 221-320. https://doi.org/10.1002/9781118995167.ch6
- José M. Saa, Antonio Frontera. On the Role of Water as a Catalyst in Prebiotic Chemistry. ChemPhysChem 2020, 21
(4)
, 313-320. https://doi.org/10.1002/cphc.201901069
- Stephen L. Bearne. The role of Brønsted base basicity in estimating carbon acidity at enzyme active sites: a caveat. Organic & Biomolecular Chemistry 2019, 17
(30)
, 7161-7165. https://doi.org/10.1039/C9OB00863B
- Matthew L Harty, Amar Nath Sharma, Stephen L Bearne. Catalytic properties of the metal ion variants of mandelate racemase reveal alterations in the apparent electrophilicity of the metal cofactor. Metallomics 2019, 11
(3)
, 707-723. https://doi.org/10.1039/c8mt00330k
- Mitesh Nagar, Himank Kumar, Stephen L Bearne. A platform for chemical modification of mandelate racemase: characterization of the C92S/C264S and γ-thialysine 166 variants. Protein Engineering, Design and Selection 2018, 31
(4)
, 135-145. https://doi.org/10.1093/protein/gzy011
- Stephen L. Bearne, Martin St. Maurice. A Paradigm for C H Bond Cleavage: Structural and Functional Aspects of Transition State Stabilization by Mandelate Racemase. 2017, 113-160. https://doi.org/10.1016/bs.apcsb.2017.04.007
- Sun Ja Cho, Jeong Ah Kim, Sun Bok Lee. Identification and characterization of 3,6-anhydro-L-galactonate cycloisomerase belonging to theenolase superfamily. Biotechnology and Bioprocess Engineering 2015, 20
(3)
, 462-472. https://doi.org/10.1007/s12257-015-0359-7
- . Isomerases. 2012, 213-224. https://doi.org/10.1002/9781118348970.ch10
- . Enzyme Models Classified by Reaction. 2009, 61-194. https://doi.org/10.1039/9781847559784-00061
- Davide Tessaro, Gianluca Molla, Loredano Pollegioni, Stefano Servi. Chemo‐Enzymatic Deracemization Methods. 2008, 195-228. https://doi.org/10.1002/9783527623839.ch13
- Krzysztof Okrasa, Colin Levy, Bernhard Hauer, Nina Baudendistel, David Leys, Jason Micklefield. Structure and Mechanism of an Unusual Malonate Decarboxylase and Related Racemases. Chemistry – A European Journal 2008, 14
(22)
, 6609-6613. https://doi.org/10.1002/chem.200800918
- Bettina M. Nestl, Anne Bodlenner, Rainer Stuermer, Bernhard Hauer, Wolfgang Kroutil, Kurt Faber. Biocatalytic racemization of synthetically important functionalized α-hydroxyketones using microbial cells. Tetrahedron: Asymmetry 2007, 18
(12)
, 1465-1474. https://doi.org/10.1016/j.tetasy.2007.06.005
- Tracey L. Thaler, Phillip R. Gibbs, Rick P. Trebino, Andreas S. Bommarius. Search for Extraterrestrial Life Using Chiral Molecules: Mandelate Racemase as a Test Case. Astrobiology 2006, 6
(6)
, 901-910. https://doi.org/10.1089/ast.2006.6.901
- John A. Gerlt. Enzymatic Catalysis of Proton Transfer at Carbon Atoms. 2006, 1107-1137. https://doi.org/10.1002/9783527611546.ch35
- M. Ashley Spies, Michael D. Toney. Multiple Hydrogen Transfers in Enzyme Action. 2006, 1139-1170. https://doi.org/10.1002/9783527611546.ch36
- Bettina M. Nestl, Silvia M. Glueck, Melanie Hall, Wolfgang Kroutil, Rainer Stuermer, Bernhard Hauer, Kurt Faber. Biocatalytic Racemization of (Hetero)Aryl‐aliphatic α‐Hydroxycarboxylic Acids by
Lactobacillus
spp. Proceeds via an Oxidation–Reduction Sequence. European Journal of Organic Chemistry 2006, 2006
(20)
, 4573-4577. https://doi.org/10.1002/ejoc.200600454
- P. Gadler, S.M. Glueck, W. Kroutil, B.M. Nestl, B. Larissegger-Schnell, B.T. Ueberbacher, S.R. Wallner, K. Faber. Biocatalytic approaches for the quantitative production of single stereoisomers from racemates. Biochemical Society Transactions 2006, 34
(2)
, 296-300. https://doi.org/10.1042/BST0340296
- Ulfried Felfer, Marian Goriup, Marion F. Koegl, Ulrike Wagner, Barbara Larissegger‐Schnell, Kurt Faber, Wolfgang Kroutil. The Substrate Spectrum of Mandelate Racemase: Minimum Structural Requirements for Substrates and Substrate Model. Advanced Synthesis & Catalysis 2005, 347
(7-8)
, 951-961. https://doi.org/10.1002/adsc.200505012
- Ralph M. Pollack. Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase. Bioorganic Chemistry 2004, 32
(5)
, 341-353. https://doi.org/10.1016/j.bioorg.2004.06.005
- Barbara Schnell, Kurt Faber, Wolfgang Kroutil. Enzymatic Racemisation and its Application to Synthetic Biotransformations. Advanced Synthesis & Catalysis 2003, 345
(6-7)
, 653-666. https://doi.org/10.1002/adsc.200303009
- A. Williams. Acid–Base Catalysis – Biological. 2002https://doi.org/10.1002/0471227617.eoc001
- David Amar, Paul North, Vanda Miskiniene, Narimantas Cénas, Florence Lederer. Hydroxamates as Substrates and Inhibitors for FMN-Dependent 2-Hydroxy Acid Dehydrogenases. Bioorganic Chemistry 2002, 30
(3)
, 145-162. https://doi.org/10.1006/bioo.2002.1237
- Xavier Prat-Resina, Mireia Garcia-Viloca, Angels González-Lafont, José M. Lluch. On the modulation of the substrate activity for the racemization catalyzed by mandelate racemase enzyme. A QM/MM study. Phys. Chem. Chem. Phys. 2002, 4
(21)
, 5365-5371. https://doi.org/10.1039/B204693H
- Ulfried Felfer, Ulrike T. Strauss, Wolfgang Kroutil, Walter M.F. Fabian, Kurt Faber. Substrate spectrum of mandelate racemase. Journal of Molecular Catalysis B: Enzymatic 2001, 15
(4-6)
, 213-222. https://doi.org/10.1016/S1381-1177(01)00035-2
- Marian Goriup, Ulrike T. Strauss, Ulfried Felfer, Wolfgang Kroutil, Kurt Faber. Substrate spectrum of mandelate racemase. Journal of Molecular Catalysis B: Enzymatic 2001, 15
(4-6)
, 207-211. https://doi.org/10.1016/S1381-1177(01)00036-4
- John A. Gerlt, Patricia C. Babbitt. Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies. Annual Review of Biochemistry 2001, 70
(1)
, 209-246. https://doi.org/10.1146/annurev.biochem.70.1.209
- Patricia C. Babbitt, John A. Gerlt. New functions from old scaffolds: How nature reengineers enzymes for new functions. 2001, 1-28. https://doi.org/10.1016/S0065-3233(01)55001-9
- Ulrike T. Strauss, Kurt Faber. Bio- and Chemo-Catalytic Deracemisation Techniques. 2000, 1-23. https://doi.org/10.1007/978-94-010-0924-9_1
- Ulrike T Strauss, Kurt Faber. Deracemization of (±)-mandelic acid using a lipase–mandelate racemase two-enzyme system. Tetrahedron: Asymmetry 1999, 10
(21)
, 4079-4081. https://doi.org/10.1016/S0957-4166(99)00436-X
- Stephen L. Bearne, Martin St. Maurice, Mark D. Vaughan. An Assay for Mandelate Racemase Using High-Performance Liquid Chromatography. Analytical Biochemistry 1999, 269
(2)
, 332-336. https://doi.org/10.1006/abio.1999.4018
- Ursula Schell, Sari Helin, Tommi Kajander, Michael Schl�mann, Adrian Goldman. Structural basis for the activity of two muconate cycloisomerase variants toward substituted muconates. Proteins: Structure, Function, and Genetics 1999, 34
(1)
, 125-136. https://doi.org/10.1002/(SICI)1097-0134(19990101)34:1<125::AID-PROT10>3.0.CO;2-Y
- John A. Gerlt. Stabilization of Reactive Intermediates and Transition States in Enzyme Active Sites by Hydrogen Bonding. 1999, 5-29. https://doi.org/10.1016/B978-0-08-091283-7.00131-4
- Christian P. Whitman. Keto–Enol Tautomerism in Enzymatic Reactions. 1999, 31-50. https://doi.org/10.1016/B978-0-08-091283-7.00132-6
- Shu-ou Shan, Daniel Herschlag. [11] Hydrogen bonding in enzymatic catalysis: Analysis of energetic contributions. 1999, 246-276. https://doi.org/10.1016/S0076-6879(99)08013-1
- A. J. Kresge. Flash photolytic generation and investigation of short-lived reaction intermediates: a case study. Journal of Physical Organic Chemistry 1998, 11
(5)
, 292-298. https://doi.org/10.1002/(SICI)1099-1395(199805)11:5<292::AID-POC996>3.0.CO;2-U
- Amy Kaufman Katz, Jenny P. Glusker. Roles of zinc and magnesium ions in enzymes. 1998, 227-279. https://doi.org/10.1016/S1087-3295(98)80008-X
- Eelco J. Ebbers, Gerry J.A. Ariaans, Joannes P.M. Houbiers, Alle Bruggink, Binne Zwanenburg. Controlled racemization of optically active organic compounds: Prospects for asymmetric transformation. Tetrahedron 1997, 53
(28)
, 9417-9476. https://doi.org/10.1016/S0040-4020(97)00324-4
- Hartmut Stecher, Ulfried Felfer, Kurt Faber. Large-scale production of Mandelate racemase by Pseudomonas putida ATCC 12633: optimization of enzyme induction and development of a stable crude enzyme preparation. Journal of Biotechnology 1997, 56
(1)
, 33-40. https://doi.org/10.1016/S0168-1656(97)00076-X
- Jerzy Cioslowski, Gernot Boche. Geometry‐Tunable Lewis Acidity of Amidinium Cations and Its Relevance to Redox Reactions of the Thauer Metal‐Free Hydrogenase: A Theoretical Study. Angewandte Chemie International Edition in English 1997, 36
(1-2)
, 107-109. https://doi.org/10.1002/anie.199701071
- Jerzy Cioslowski, Gernot Boche. Konformationsgesteuerte Lewis‐Acidität von Amidinium‐Ionen und ihre Bedeutung für die Redoxreaktionen der Thauerschen metallfreien Hydrogenase – eine theoretische Studie. Angewandte Chemie 1997, 109
(1-2)
, 165-167. https://doi.org/10.1002/ange.19971090155
- Jiali Gao. A theoretical investigation of the enol content of acetic acid and the acetate ion in aqueous solution. Journal of Molecular Structure: THEOCHEM 1996, 370
(2-3)
, 203-208. https://doi.org/10.1016/S0166-1280(96)04702-1
- Anthony J. Kirby. Enzyme Mechanisms, Models, and Mimics. Angewandte Chemie International Edition in English 1996, 35
(7)
, 706-724. https://doi.org/10.1002/anie.199607061
- Anthony J. Kirby. Enzyme — Mechanismen, Modellreaktionen und Mimetica. Angewandte Chemie 1996, 108
(7)
, 770-790. https://doi.org/10.1002/ange.19961080705
- Masha V. Sergeeva, Vihra Yomtova, Adrian Parkinson, Marjolein Overgaauw, Rikus Pomp, Arjen Schots, Anthony J. Kirby, Riet Hilhorst. Hapten Design for Antibody‐Catalyzed Decarboxylation and Ring‐Opening Reactions of Benzisoxazoles. Israel Journal of Chemistry 1996, 36
(2)
, 177-183. https://doi.org/10.1002/ijch.199600024
- Victor S Lamzin, Zbigniew Dauter, Keith S Wilson. How nature deals with stereoisomers. Current Opinion in Structural Biology 1995, 5
(6)
, 830-836. https://doi.org/10.1016/0959-440X(95)80018-2
- G. L. KENYON, J. A. GERLT, G. A. PETSKO, J. W. KOZARICH. ChemInform Abstract: Mandelate Racemase: Structure‐Function Studies of a Pseudosymmetric Enzyme. ChemInform 1995, 26
(34)
https://doi.org/10.1002/chin.199534315
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