16 Publications
2018
Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS.
Dunkle, Jack ABruno, MichaelOutten, Franklin Wayne and Frantom, Patrick A
Biochemistry, December 20, 2018. | Journal Article
2014
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.
Casey, Ashley KHicks, Michael AJohnson, Jordyn LBabbitt, Patsy C and Frantom, Patrick A
Biochemistry, vol. 53, (no. 18), pp. 2915-25, 2014/May/13. | Journal Article
2013
V-type allosteric inhibition is described by a shift in the rate-determining step for α-isopropylmalate synthase from Mycobacterium tuberculosis.
Casey, Ashley KSchwalm, Erica LHays, Brittani N and Frantom, Patrick A
Biochemistry, vol. 52, (no. 39), pp. 6737-9, 2013/Oct/1. | Journal Article
2012
Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily.
Frantom, Patrick A
Archives of biochemistry and biophysics, vol. 519, (no. 2), pp. 202-9, 2012/Mar/15. | Journal Article
 
The slow-onset nature of allosteric inhibition in α-isopropylmalate synthase from Mycobacterium tuberculosis is mediated by a flexible loop.
Casey, Ashley KBaugh, Joshua and Frantom, Patrick A
Biochemistry, vol. 51, (no. 24), pp. 4773-5, 2012/Jun/19. | Journal Article
2010
UDP-(5F)-GlcNAc acts as a slow-binding inhibitor of MshA, a retaining glycosyltransferase.
Frantom, Patrick ACoward, James K and Blanchard, John S
Journal of the American Chemical Society, vol. 132, (no. 19), pp. 6626-7, 2010/May/19. | Journal Article
2009
Kinetic evidence for interdomain communication in the allosteric regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.
de Carvalho, Luiz PFrantom, Patrick AArgyrou, Argyrides and Blanchard, John S
Biochemistry, vol. 48, (no. 9), pp. 1996-2004, 2009/Mar/10. | Journal Article
 
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.
Frantom, Patrick AZhang, Hui-MinEmmett, Mark RMarshall, Alan G and Blanchard, John S
Biochemistry, vol. 48, (no. 31), pp. 7457-64, 2009/Aug/11. | Journal Article
 
Structures and mechanisms of the mycothiol biosynthetic enzymes
Fan, FanVetting, M. WFrantom, Patrick A and Blanchard, John S
Current Opinion in Chemical Biology, vol. 13, (no. 4), pp. 451-459, 2009. | Journal Article
2008
Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum: SUBSTRATE-ASSISTED CATALYSIS
Vetting, M. WFrantom, Patrick A and Blanchard, John S
Journal of Biological Chemistry, vol. 283, (no. 23), pp. 15834-15844, 2008. | Journal Article
2007
Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase.
Eser, Bekir EBarr, Eric WFrantom, Patrick ASaleh, LanaBollinger, J. MKrebs, Carsten and Fitzpatrick, Paul F
Journal of the American Chemical Society, vol. 129, (no. 37), pp. 11334-5, 2007/Sep/19. | Journal Article
2006
Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity.
Frantom, Patrick ASeravalli, JavierRagsdale, Stephen W and Fitzpatrick, Paul F
Biochemistry, vol. 45, (no. 7), pp. 2372-9, 2006/Feb/21. | Journal Article
2005
Studies of the chemical and regulatory mechanisms of tyrosine hydroxylase (Dissertation)
Frantom, Patrick A (2005).
2003
Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps.
Frantom, Patrick A and Fitzpatrick, Paul F
Journal of the American Chemical Society, vol. 125, (no. 52), pp. 16190-1, 2003/Dec/31. | Journal Article
2002
Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase.
Frantom, Patrick APongdee, RongsonSulikowski, Gary A and Fitzpatrick, Paul F
Journal of the American Chemical Society, vol. 124, (no. 16), pp. 4202-3, 2002/Apr/24. | Journal Article
1999
Mutations at Four Active Site Residues of Biotin Carboxylase Abolish Substrate-Induced Synergism by Biotin
Blanchard, CZLee, YMFrantom, Patrick A and Waldrop, Grover L
Biochemistry (Washington), vol. 38, (no. 11), pp. 3393-3400, 1999. | Journal Article