Patrick A. Frantom, Ph.D.

Affiliations: 
2005 Texas A & M University, College Station, TX, United States 
Area:
catalytic and regulatory mechanisms of enzymes
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"Patrick Frantom"
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Paul F. Fitzpatrick grad student 2005 Texas A & M
 (Studies of the chemical and regulatory mechanisms of tyrosine hydroxylase.)
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Publications

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Kumar G, Johnson JL, Frantom PA. (2016) Improving functional annotation in the DRE-TIM metallolyase superfamily through identification of active site fingerprints. Biochemistry
Scalfani VF, Frantom PA, Woski SA. (2016) Replacing the Traditional Graduate Chemistry Literature Seminar with a Chemical Research Literacy Course Journal of Chemical Education. 93: 482-487
Dai Y, Kim D, Dong G, et al. (2015) SufE D74R Substitution Alters Active Site Loop Dynamics To Further Enhance SufE Interaction with the SufS Cysteine Desulfurase. Biochemistry. 54: 4824-33
Kumar G, Guan S, Frantom PA. (2014) Biochemical characterization of the retaining glycosyltransferase glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis. Archives of Biochemistry and Biophysics. 564: 120-7
Frantom PA, Birman Y, Hays BN, et al. (2014) An evolutionarily conserved alternate metal ligand is important for activity in α-isopropylmalate synthase from Mycobacterium tuberculosis. Biochimica Et Biophysica Acta. 1844: 1784-9
Kumar G, Frantom PA. (2014) Evolutionarily distinct versions of the multidomain enzyme α-isopropylmalate synthase share discrete mechanisms of V-type allosteric regulation. Biochemistry. 53: 4847-56
Casey AK, Hicks MA, Johnson JL, et al. (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. Biochemistry. 53: 2915-25
Casey AK, Schwalm EL, Hays BN, et al. (2013) 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
Casey AK, Baugh J, Frantom PA. (2012) The slow-onset nature of allosteric inhibition in α-isopropylmalate synthase from Mycobacterium tuberculosis is mediated by a flexible loop. Biochemistry. 51: 4773-5
Frantom PA. (2012) 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
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