Neutron diffraction reveals protonation states in pyridoxal‐5′‐phosphate‐free and glycine external aldimine‐bound serine hydroxymethyltransferase

Drago, Victoria N.; Blakeley, Matthew P.; Phillips, Robert S.; Kovalevsky, Andrey Y.

doi:10.1111/febs.70260

Neutron diffraction reveals protonation states in pyridoxal‐5′‐phosphate‐free and glycine external aldimine‐bound serine hydroxymethyltransferase

Journal Article · Sun Sep 07 00:00:00 EDT 2025 · Federation of European Biochemical Societies (FEBS) Journal

DOI:https://doi.org/10.1111/febs.70260· OSTI ID:3018167

Drago, Victoria N. ^[1]; ^[2]; ^[3]; ^[1]

Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Inst. Laue-Langevin (ILL), Grenoble (France)
Univ. of Georgia, Athens, GA (United States)

Serine hydroxymethyltransferase (SHMT) is a critical enzyme in the one-carbon (1C) metabolism pathway catalyzing the reversible conversion of L-Ser into Gly and concurrent transfer of 1C unit to tetrahydrofolate (THF) to give 5,10-methylene-THF (5,10-MTHF), which is used in the downstream syntheses of biomolecules critical for cell proliferation. The cellular 1C metabolism is hijacked by many cancer types to support cancer cell proliferation, making SHMT a promising target for the design and development of novel small-molecule antimetabolite chemotherapies. To advance structure-assisted drug design, knowledge of SHMT catalysis is crucial, but can only be fully realized when the atomic details of each reaction step governed by the acid–base catalysis are elucidated by visualizing active site hydrogen atoms. Here, we used room-temperature neutron crystallography to directly determine protonation states in Thermus thermophilus SHMT (TthSHMT), capturing protomer A in the apo form lacking the coenzyme pyridoxal 5′-phosphate (PLP), and protomer B as a ternary complex with PLP–Gly-external aldimine and (6S)-5-methyltetrahydrofolate (5MTHF). We observed protonation of the Schiff base nitrogen in PLP–Gly and neutrality of the catalytic Lys226 side chain in the ternary complex, whereas Lys226 is protonated and positively charged in the apo-active site. Furthermore, we obtained an X-ray structure of TthSHMT in complex with the substrate THF, which binds identically as 5MTHF at the peripheral binding site. In conclusion, the unique structural and functional information provided by neutron crystallography, in combination with X-ray structures, can be employed in the rational design of SHMT inhibitors.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities (SUF); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC05-00OR22725

Other Award/Contract Number:: R01GM137008

OSTI ID:: 3018167

Journal Information:: Federation of European Biochemical Societies (FEBS) Journal, Journal Name: Federation of European Biochemical Societies (FEBS) Journal Journal Issue: 2 Vol. 293; ISSN 1742-464X; ISSN 1742-4658

Publisher:: Federation of European Biochemical SocietiesCopyright Statement

Country of Publication:: United States

Language:: English

References (70)

Structural basis of inhibition of the human serine hydroxymethyltransferase SHMT 2 by antifolate drugs Scaletti, Emma; Jemth, Ann‐Sofie; Helleday, Thomas FEBS Letters, Vol. 593, Issue 14 https://doi.org/10.1002/1873-3468.13455	journal	June 2019
Current developments in Coot for macromolecular model building of Electron Cryo‐microscopy and Crystallographic Data Casañal, Ana; Lohkamp, Bernhard; Emsley, Paul Protein Science, Vol. 29, Issue 4 https://doi.org/10.1002/pro.3791	journal	March 2020
Conformational transitions driven by pyridoxal-5′-phosphate uptake in the psychrophilic serine hydroxymethyltransferase from P sychromonas ingrahamii : Psychrophilic SHMT Conformational Transitions Angelaccio, Sebastiana; Dworkowski, Florian; Di Bello, Angela Proteins: Structure, Function, and Bioinformatics, Vol. 82, Issue 10 https://doi.org/10.1002/prot.24646	journal	August 2014
Serine hydroxymethyltransferase 2: a novel target for human cancer therapy Xie, Min; Pei, Dong-Sheng Investigational New Drugs, Vol. 39, Issue 6 https://doi.org/10.1007/s10637-021-01144-z	journal	July 2021
Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase — a potential target for cancer chemotherapy Appaji Rao, N.; Talwar, Rashmi; Savithri, H. S. The International Journal of Biochemistry & Cell Biology, Vol. 32, Issue 4 https://doi.org/10.1016/S1357-2725(99)00126-0	journal	April 2000
Structure–function relationship in serine hydroxymethyltransferase Appaji Rao, N.; Ambili, M.; Jala, Venkatakrishna R. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1647, Issue 1-2 https://doi.org/10.1016/S1570-9639(03)00043-8	journal	April 2003
IMAGINE: The neutron protein crystallography beamline at the high flux isotope reactor Meilleur, Flora; Kovalevsky, Andrey; Myles, Dean A. A. Methods in Enzymology https://doi.org/10.1016/bs.mie.2019.11.016	book	February 2020
Binding of a potential antibacterial drug, mangiferin, to serine hydroxymethyltransferase from Enterococcus faecium Hayashi, Hironori; Hasegawa, Kazuya; Saijo, Erika Biochemical and Biophysical Research Communications, Vol. 743 https://doi.org/10.1016/j.bbrc.2024.151177	journal	January 2025
Serine hydroxymethyltransferase revisited Schirch, Verne; Szebenyi, Doletha ME Current Opinion in Chemical Biology, Vol. 9, Issue 5 https://doi.org/10.1016/j.cbpa.2005.08.017	journal	October 2005
Hallmarks of Cancer: The Next Generation Hanahan, Douglas; Weinberg, Robert A. Cell, Vol. 144, Issue 5 https://doi.org/10.1016/j.cell.2011.02.013	journal	March 2011
Folate-mediated one-carbon metabolism: a targeting strategy in cancer therapy Yang, Chengcan; Zhang, Jifa; Liao, Minru Drug Discovery Today, Vol. 26, Issue 3 https://doi.org/10.1016/j.drudis.2020.12.006	journal	March 2021
Regulatory mechanisms of one-carbon metabolism enzymes Petrova, Boryana; Maynard, Adam G.; Wang, Peng Journal of Biological Chemistry, Vol. 299, Issue 12 https://doi.org/10.1016/j.jbc.2023.105457	journal	December 2023
Structural, Electronic, and Electrostatic Determinants for Inhibitor Binding to Subsites S1 and S2 in SARS-CoV-2 Main Protease Kneller, Daniel W.; Li, Hui; Galanie, Stephanie Journal of Medicinal Chemistry, Vol. 64, Issue 23 https://doi.org/10.1021/acs.jmedchem.1c01475	journal	October 2021
Structure-Based Design of Transport-Specific Multitargeted One-Carbon Metabolism Inhibitors in Cytosol and Mitochondria Nayeen, Md. Junayed; Katinas, Jade M.; Magdum, Tejashree Journal of Medicinal Chemistry, Vol. 66, Issue 16 https://doi.org/10.1021/acs.jmedchem.3c00763	journal	August 2023
Neutron Crystallography of a Semiquinone Radical Intermediate of Copper Amine Oxidase Reveals a Substrate-Assisted Conformational Change of the Peptidyl Quinone Cofactor Murakawa, Takeshi; Kurihara, Kazuo; Shoji, Mitsuo ACS Catalysis, Vol. 13, Issue 18 https://doi.org/10.1021/acscatal.3c02629	journal	September 2023
Catalytic Mechanism of the Serine Hydroxymethyltransferase: A Computational ONIOM QM/MM Study Fernandes, Henrique S.; Ramos, Maria João; Cerqueira, Nuno M. F. S. A. ACS Catalysis, Vol. 8, Issue 11 https://doi.org/10.1021/acscatal.8b02321	journal	September 2018
A Review of Small-Molecule Inhibitors of One-Carbon Enzymes: SHMT2 and MTHFD2 in the Spotlight Cuthbertson, Christine R.; Arabzada, Zahra; Bankhead, Armand ACS Pharmacology & Translational Science, Vol. 4, Issue 2 https://doi.org/10.1021/acsptsci.0c00223	journal	March 2021
Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D- and L-alanine Shostak, Keith; Schirch, Verne Biochemistry, Vol. 27, Issue 21 https://doi.org/10.1021/bi00421a006	journal	October 1988
Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism ^† Szebenyi, Doletha M. E.; Musayev, Faik N.; di Salvo, Martino L. Biochemistry, Vol. 43, Issue 22 https://doi.org/10.1021/bi049791y	journal	June 2004
Providing one-carbon units for biological methylations: mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase Matthews, Rowena G.; Drummond, James T. Chemical Reviews, Vol. 90, Issue 7 https://doi.org/10.1021/cr00105a010	journal	November 1990
One-carbon metabolism in cancer Newman, Alice C.; Maddocks, Oliver D. K. British Journal of Cancer, Vol. 116, Issue 12 https://doi.org/10.1038/bjc.2017.118	journal	May 2017
SHMT inhibition is effective and synergizes with methotrexate in T-cell acute lymphoblastic leukemia García-Cañaveras, Juan C.; Lancho, Olga; Ducker, Gregory S. Leukemia, Vol. 35, Issue 2 https://doi.org/10.1038/s41375-020-0845-6	journal	May 2020
Targeting serine hydroxymethyltransferases 1 and 2 for T-cell acute lymphoblastic leukemia therapy Pikman, Yana; Ocasio-Martinez, Nicole; Alexe, Gabriela Leukemia, Vol. 36, Issue 2 https://doi.org/10.1038/s41375-021-01361-8	journal	August 2021
Direct visualization of critical hydrogen atoms in a pyridoxal 5′-phosphate enzyme Dajnowicz, Steven; Johnston, Ryne C.; Parks, Jerry M. Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/s41467-017-01060-y	journal	October 2017
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease Kneller, Daniel W.; Li, Hui; Phillips, Gwyndalyn Nature Communications, Vol. 13, Issue 1 https://doi.org/10.1038/s41467-022-29915-z	journal	April 2022
Unraveling the role of the mitochondrial one-carbon pathway in undifferentiated thyroid cancer by multi-omics analyses Lee, Seong Eun; Park, Seongyeol; Yi, Shinae Nature Communications, Vol. 15, Issue 1 https://doi.org/10.1038/s41467-024-45366-0	journal	February 2024
Targeting cancer metabolism in the era of precision oncology Stine, Zachary E.; Schug, Zachary T.; Salvino, Joseph M. Nature Reviews Drug Discovery, Vol. 21, Issue 2 https://doi.org/10.1038/s41573-021-00339-6	journal	December 2021
Metabolic control of BRISC–SHMT2 assembly regulates immune signalling Walden, Miriam; Tian, Lei; Ross, Rebecca L. Nature, Vol. 570, Issue 7760 https://doi.org/10.1038/s41586-019-1232-1	journal	May 2019
Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models Ruszkowski, Milosz; Sekula, Bartosz; Ruszkowska, Agnieszka Scientific Reports, Vol. 9, Issue 1 https://doi.org/10.1038/s41598-019-56043-4	journal	December 2019
Serine hydroxymethyltransferase as a potential target of antibacterial agents acting synergistically with one-carbon metabolism-related inhibitors Makino, Yuko; Oe, Chihiro; Iwama, Kazuya Communications Biology, Vol. 5, Issue 1 https://doi.org/10.1038/s42003-022-03555-x	journal	June 2022
Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography Drago, Victoria N.; Campos, Claudia; Hooper, Mattea Communications Chemistry, Vol. 6, Issue 1 https://doi.org/10.1038/s42004-023-00964-9	journal	August 2023
A genomic overview of pyridoxal-phosphate-dependent enzymes Percudani, Riccardo; Peracchi, Alessio EMBO reports, Vol. 4, Issue 9 https://doi.org/10.1038/sj.embor.embor914	journal	September 2003
An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction Drago, Victoria N.; Dajnowicz, Steven; Parks, Jerry M. Chemical Science, Vol. 13, Issue 34 https://doi.org/10.1039/D2SC02285K	journal	January 2022
Universality of critical active site glutamate as an acid–base catalyst in serine hydroxymethyltransferase function Drago, Victoria N.; Phillips, Robert S.; Kovalevsky, Andrey Chemical Science, Vol. 15, Issue 32 https://doi.org/10.1039/D4SC03187C	journal	January 2024
Neutron macromolecular crystallography Blakeley, Matthew P.; Podjarny, Alberto D. Emerging Topics in Life Sciences, Vol. 2, Issue 1 https://doi.org/10.1042/ETLS20170083	journal	February 2018
A suite-level review of the neutron single-crystal diffraction instruments at Oak Ridge National Laboratory Coates, L.; Cao, H. B.; Chakoumakos, B. C. Review of Scientific Instruments, Vol. 89, Issue 9 https://doi.org/10.1063/1.5030896	journal	September 2018
Human SHMT inhibitors reveal defective glycine import as a targetable metabolic vulnerability of diffuse large B-cell lymphoma Ducker, Gregory S.; Ghergurovich, Jonathan M.; Mainolfi, Nello Proceedings of the National Academy of Sciences, Vol. 114, Issue 43 https://doi.org/10.1073/pnas.1706617114	journal	October 2017
A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus Bolton, Rachel; Machelett, Moritz M.; Stubbs, Jack Proceedings of the National Academy of Sciences, Vol. 121, Issue 12 https://doi.org/10.1073/pnas.2308478121	journal	March 2024
Crystal Structure of Binary and Ternary Complexes of Serine Hydroxymethyltransferase from Bacillus stearothermophilus: INSIGHTS INTO THE CATALYTIC MECHANISM Trivedi, V.; Gupta, A.; Jala, V. R. Journal of Biological Chemistry, Vol. 277, Issue 19 https://doi.org/10.1074/jbc.M111976200	journal	May 2002
Cytoplasmic Serine Hydroxymethyltransferase Mediates Competition between Folate-dependent Deoxyribonucleotide andS-Adenosylmethionine Biosyntheses Herbig, Katherine; Chiang, En-Pei; Lee, Ling-Ru Journal of Biological Chemistry, Vol. 277, Issue 41 https://doi.org/10.1074/jbc.M205000200	journal	October 2002
Global indicators of X-ray data quality Weiss, Manfred S. Journal of Applied Crystallography, Vol. 34, Issue 2 https://doi.org/10.1107/S0021889800018227	journal	April 2001
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
LAUEGEN , an X-windows-based program for the processing of Laue diffraction data Campbell, J. W. Journal of Applied Crystallography, Vol. 28, Issue 2 https://doi.org/10.1107/S002188989400991X	journal	April 1995
LAUEGEN version 6.0 and INTLDM Campbell, J. W.; Hao, Q.; Harding, M. M. Journal of Applied Crystallography, Vol. 31, Issue 3 https://doi.org/10.1107/S0021889897016683	journal	June 1998
LSCALE – the new normalization, scaling and absorption correction program in the Daresbury Laue software suite Arzt, Steffi; Campbell, John W.; Harding, Marjorie M. Journal of Applied Crystallography, Vol. 32, Issue 3 https://doi.org/10.1107/S0021889898015350	journal	June 1999
Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules Adams, Paul D.; Mustyakimov, Marat; Afonine, Pavel V. Acta Crystallographica Section D Biological Crystallography, Vol. 65, Issue 6 https://doi.org/10.1107/S0907444909011548	journal	May 2009
electronic Ligand Builder and Optimization Workbench ( eLBOW ): a tool for ligand coordinate and restraint generation Moriarty, Nigel W.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Acta Crystallographica Section D Biological Crystallography, Vol. 65, Issue 10 https://doi.org/10.1107/S0907444909029436	journal	September 2009
PHENIX: a comprehensive Python-based system for macromolecular structure solution Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221 https://doi.org/10.1107/S0907444909052925	journal	January 2010
Neutron macromolecular crystallography with LADI-III Blakeley, Matthew P.; Teixeira, Susana C. M.; Petit-Haertlein, Isabelle Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 11 https://doi.org/10.1107/S0907444910019797	journal	October 2010
Overview of the CCP 4 suite and current developments Winn, Martyn D.; Ballard, Charles C.; Cowtan, Kevin D. Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4 https://doi.org/10.1107/S0907444910045749	journal	March 2011
How good are my data and what is the resolution? Evans, Philip R.; Murshudov, Garib N. Acta Crystallographica Section D Biological Crystallography, Vol. 69, Issue 7 https://doi.org/10.1107/S0907444913000061	journal	June 2013
The IMAGINE instrument: first neutron protein structure and new capabilities for neutron macromolecular crystallography Meilleur, Flora; Munshi, Parthapratim; Robertson, Lee Acta Crystallographica Section D Biological Crystallography, Vol. 69, Issue 10 https://doi.org/10.1107/S0907444913019604	journal	September 2013
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Brünger, A. T.; Adams, P. D.; Clore, G. M. Acta Crystallographica Section D Biological Crystallography, Vol. 54, Issue 5 https://doi.org/10.1107/S0907444998003254	journal	September 1998
Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix Liebschner, Dorothee; Afonine, Pavel V.; Baker, Matthew L. Acta Crystallographica Section D Structural Biology, Vol. 75, Issue 10 https://doi.org/10.1107/S2059798319011471	journal	October 2019
Identification of three new compounds that directly target human serine hydroxymethyltransferase 2 Han, Yanfang; He, Liping; Qi, Yifei Chemical Biology & Drug Design, Vol. 97, Issue 2 https://doi.org/10.1111/cbdd.13774	journal	September 2020
Mechanism for folate-independent aldolase reaction catalyzed by serine hydroxymethyltransferase: Y. Chiba et al. Chiba, Yoko; Terada, Tohru; Kameya, Masafumi FEBS Journal, Vol. 279, Issue 3 https://doi.org/10.1111/j.1742-4658.2011.08443.x	journal	December 2011
Repurposing the Antidepressant Sertraline as SHMT Inhibitor to Suppress Serine/Glycine Synthesis–Addicted Breast Tumor Growth Geeraerts, Shauni Lien; Kampen, Kim Rosalie; Rinaldi, Gianmarco Molecular Cancer Therapeutics, Vol. 20, Issue 1 https://doi.org/10.1158/1535-7163.MCT-20-0480	journal	January 2021
Hallmarks of Cancer: New Dimensions Hanahan, Douglas Cancer Discovery, Vol. 12, Issue 1 https://doi.org/10.1158/2159-8290.CD-21-1059	journal	January 2022
Structural and functional insight into serine hydroxymethyltransferase from Helicobacter pylori Sodolescu, Andreea; Dian, Cyril; Terradot, Laurent PLOS ONE, Vol. 13, Issue 12 https://doi.org/10.1371/journal.pone.0208850	journal	December 2018
Induction of serine hydroxymethyltransferase 2 promotes tumorigenesis and metastasis in neuroblastoma Clark, Rachael A.; Qiao, Jingbo; Jacobson, Jillian C. Oncotarget, Vol. 13, Issue 1 https://doi.org/10.18632/oncotarget.28168	journal	January 2022
A pyrazolopyran derivative preferentially inhibits the activity of human cytosolic serine hydroxymethyltransferase and induces cell death in lung cancer cells Marani, Marina; Paone, Alessio; Fiascarelli, Alessio Oncotarget, Vol. 7, Issue 4 https://doi.org/10.18632/oncotarget.6726	journal	December 2015
Serine hydroxymethyltransferase 2 predicts unfavorable outcomes in multiple cancer: a systematic review and meta-analysis Du, Juan; Huang, Yongkang; Jing, Suxian Translational Cancer Research, Vol. 11, Issue 3 https://doi.org/10.21037/tcr-21-2485	journal	March 2022
Current status of neutron crystallography in structural biology Kono, Fumiaki; Kurihara, Kazuo; Tamada, Taro Biophysics and Physicobiology, Vol. 19, Issue 0 https://doi.org/10.2142/biophysico.bppb-v19.0009	journal	January 2022
SHMT2 is Associated with Tumor Purity, CD8+ T Immune Cells Infiltration, and a Novel Therapeutic Target in Four Different Human Cancers Usman, Muhammad; Hameed, Yasir; Ahmad, Mukhtiar Current Molecular Medicine, Vol. 23, Issue 2 https://doi.org/10.2174/1566524022666220112142409	journal	February 2023
SHMT as a Potential Therapeutic Target for Renal Cell Carcinoma Situ, Yongli; Zhang, Juying; Liao, Wenyu Frontiers in Bioscience-Landmark, Vol. 28, Issue 9 https://doi.org/10.31083/j.fbl2809196	journal	September 2023
Targeting SHMTs and MTHFDs in cancer: attractive opportunity for anti-tumor strategy Zhang, Xue; Wang, Zhenhua Frontiers in Pharmacology, Vol. 15 https://doi.org/10.3389/fphar.2024.1335785	journal	February 2024
Structural insights into binding of polyglutamylated tetrahydrofolate by serine hydroxymethyltransferase 8 from soybean Owuocha, Luckio F.; Mitchum, Melissa G.; Beamer, Lesa J. Frontiers in Plant Science, Vol. 15 https://doi.org/10.3389/fpls.2024.1451839	journal	August 2024
BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling Rabl, Julius Biomolecules, Vol. 10, Issue 11 https://doi.org/10.3390/biom10111503	journal	October 2020
Metformin Is a Pyridoxal-5′-phosphate (PLP)-Competitive Inhibitor of SHMT2 Tramonti, Angela; Cuyàs, Elisabet; Encinar, José Cancers, Vol. 13, Issue 16 https://doi.org/10.3390/cancers13164009	journal	August 2021
The Neutron Macromolecular Crystallography Instruments at Oak Ridge National Laboratory: Advances, Challenges, and Opportunities Meilleur, Flora; Coates, Leighton; Cuneo, Matthew Crystals, Vol. 8, Issue 10 https://doi.org/10.3390/cryst8100388	journal	October 2018

Similar Records

Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography

Journal Article · Wed Aug 02 20:00:00 EDT 2023 · Communications Chemistry · OSTI ID:1994657

Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models

Journal Article · Sat Nov 30 19:00:00 EST 2019 · Scientific Reports · OSTI ID:1624518

Related Subjects

X-ray crystallography
external aldimine
neutron crystallography
protonation state
serine hydroxymethyltransferase

Neutron diffraction reveals protonation states in pyridoxal‐5′‐phosphate‐free and glycine external aldimine‐bound serine hydroxymethyltransferase

Citation Formats

References (70)

Similar Records

Related Subjects