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Patrick A. Frantom, Ph.D. - Publications

Affiliations: 
Chemistry The University of Alabama, Tuscaloosa, AL 
 2005 Texas A & M University, College Station, TX, United States 
Area:
catalytic and regulatory mechanisms of enzymes
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29 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Travis S, Green KD, Thamban Chandrika N, Pang AH, Frantom PA, Tsodikov OV, Garneau-Tsodikova S, Thompson MK. Identification and analysis of small molecule inhibitors of FosB from . Rsc Medicinal Chemistry. 14: 947-956. PMID 37252104 DOI: 10.1039/d3md00113j  0.338
2023 Gogar RK, Carroll F, Conte JV, Nasef M, Dunkle JA, Frantom PA. The β-latch structural element of the SufS cysteine desulfurase mediates active site accessibility and SufE transpersulfurase positioning. The Journal of Biological Chemistry. 102966. PMID 36736428 DOI: 10.1016/j.jbc.2023.102966  0.355
2021 Wiltsie V, Travis S, Shay MR, Simmons Z, Frantom P, Thompson MK. Structural and Functional Characterization of Fosfomycin Resistance Conferred by FosB from Enterococcus faecium. Protein Science : a Publication of the Protein Society. PMID 34882867 DOI: 10.1002/pro.4253  0.359
2020 Conte JV, Frantom PA. Biochemical characterization of 2-phosphinomethylmalate synthase from Streptomyces hygroscopicus: A member of the DRE-TIM metallolyase superfamily. Archives of Biochemistry and Biophysics. 108489. PMID 32697946 DOI: 10.1016/j.abb.2020.108489  0.449
2019 Travis S, Shay MR, Manabe S, Gilbert NC, Frantom PA, Thompson MK. Characterization of the genomically encoded fosfomycin resistance enzyme from . Medchemcomm. 10: 1948-1957. PMID 32952996 DOI: 10.1039/c9md00372j  0.361
2019 Blahut M, Wise CE, Bruno MR, Dong G, Makris TM, Frantom PA, Dunkle JA, Outten FW. Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues. The Journal of Biological Chemistry. PMID 31248989 DOI: 10.2210/Pdb6O11/Pdb  0.351
2019 Chen W, Frantom PA. Distinct mechanisms of substrate selectivity in the DRE-TIM metallolyase superfamily: A role for the LeuA dimer regulatory domain. Archives of Biochemistry and Biophysics. PMID 30668939 DOI: 10.1016/j.abb.2019.01.021  0.348
2018 Kim D, Singh H, Dai Y, Dong G, Busenlehner LS, Outten FW, Frantom PA. Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems. Biochemistry. PMID 29589903 DOI: 10.1021/Acs.Biochem.7B01275  0.357
2016 Kumar G, Johnson JL, Frantom PA. Improving functional annotation in the DRE-TIM metallolyase superfamily through identification of active site fingerprints. Biochemistry. PMID 26935545 DOI: 10.1021/acs.biochem.5b01193  0.388
2014 Kumar G, Guan S, Frantom PA. Biochemical characterization of the retaining glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis. Archives of Biochemistry and Biophysics. 564: 120-7. PMID 25317963 DOI: 10.1016/j.abb.2014.10.002  0.517
2014 Frantom PA, Birman Y, Hays BN, Casey AK. An evolutionarily conserved alternate metal ligand is important for activity in α-isopropylmalate synthase from Mycobacterium tuberculosis. Biochimica Et Biophysica Acta. 1844: 1784-9. PMID 25064783 DOI: 10.1016/j.bbapap.2014.07.013  0.739
2014 Kumar G, Frantom PA. Evolutionarily distinct versions of the multidomain enzyme α-isopropylmalate synthase share discrete mechanisms of V-type allosteric regulation. Biochemistry. 53: 4847-56. PMID 24991690 DOI: 10.1021/Bi500702U  0.563
2014 Casey AK, Hicks MA, Johnson JL, Babbitt PC, Frantom PA. Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily. Biochemistry. 53: 2915-25. PMID 24720347 DOI: 10.1021/Bi500246Z  0.719
2013 Casey AK, Schwalm EL, Hays BN, Frantom PA. V-type allosteric inhibition is described by a shift in the rate-determining step for α-isopropylmalate synthase from Mycobacterium tuberculosis. Biochemistry. 52: 6737-9. PMID 24033269 DOI: 10.1021/Bi401186V  0.713
2012 Casey AK, Baugh J, Frantom PA. The slow-onset nature of allosteric inhibition in α-isopropylmalate synthase from Mycobacterium tuberculosis is mediated by a flexible loop. Biochemistry. 51: 4773-5. PMID 22662746 DOI: 10.1021/Bi300671U  0.731
2012 Frantom PA. Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily. Archives of Biochemistry and Biophysics. 519: 202-9. PMID 22033339 DOI: 10.1016/j.abb.2011.10.009  0.412
2010 Frantom PA, Coward JK, Blanchard JS. UDP-(5F)-GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase. Journal of the American Chemical Society. 132: 6626-7. PMID 20411981 DOI: 10.1021/Ja101231A  0.628
2010 Frantom PA, Blanchard JS. Bisubstrate analog inhibitors Comprehensive Natural Products Ii: Chemistry and Biology. 8: 689-717.  0.473
2009 Fan F, Vetting MW, Frantom PA, Blanchard JS. Structures and mechanisms of the mycothiol biosynthetic enzymes. Current Opinion in Chemical Biology. 13: 451-9. PMID 19699138 DOI: 10.1016/J.Cbpa.2009.07.018  0.593
2009 Frantom PA, Zhang HM, Emmett MR, Marshall AG, Blanchard JS. Mapping of the allosteric network in the regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: solution-phase H/D exchange monitored by FT-ICR mass spectrometry. Biochemistry. 48: 7457-64. PMID 19606873 DOI: 10.1021/Bi900851Q  0.594
2009 De Carvalho LPS, Frantom PA, Argyrou A, Blanchard JS. Kinetic evidence for interdomain communication in the allosteric regulation of α-isopropylmalate synthase from Mycobacterium tuberculosis Biochemistry. 48: 1996-2004. PMID 19166329 DOI: 10.1021/Bi801707T  0.643
2009 Fan F, Vetting MW, Frantom PA, Blanchard JS. Structures and mechanisms of the mycothiol biosynthetic enzymes Current Opinion in Chemical Biology. 13: 444-452. DOI: 10.1016/j.cbpa.2009.07.018  0.583
2008 Vetting MW, Frantom PA, Blanchard JS. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: Substrate-assisted catalysis Journal of Biological Chemistry. 283: 15834-15844. PMID 18390549 DOI: 10.1074/Jbc.M801017200  0.541
2007 Eser BE, Barr EW, Frantom PA, Saleh L, Bollinger JM, Krebs C, Fitzpatrick PF. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. Journal of the American Chemical Society. 129: 11334-5. PMID 17715926 DOI: 10.1021/Ja074446S  0.548
2006 Frantom PA, Seravalli J, Ragsdale SW, Fitzpatrick PF. Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity. Biochemistry. 45: 2372-9. PMID 16475826 DOI: 10.1021/Bi052283J  0.667
2006 Frantom PA, Seravalli J, Ragsdale SW, Fitzpatrick PF. Erratum: Reduction and oxidation of the active site iron in tyrosine hydroxylase: Kinetics and specificity (Biochemistry (February 21, 2006) 45, 7 (2372-2379)) Biochemistry. 45. DOI: 10.1021/Bi0680072  0.565
2003 Frantom PA, Fitzpatrick PF. Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps. Journal of the American Chemical Society. 125: 16190-1. PMID 14692751 DOI: 10.1021/Ja0383165  0.633
2002 Frantom PA, Pongdee R, Sulikowski GA, Fitzpatrick PF. Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase. Journal of the American Chemical Society. 124: 4202-3. PMID 11960436 DOI: 10.1021/Ja025602S  0.596
1999 Blanchard CZ, Lee YM, Frantom PA, Waldrop GL. Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin Biochemistry. 38: 3393-3400. PMID 10079084 DOI: 10.1021/Bi982660A  0.5
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