Výsledky vyhledávání - "T.D. Panosian"

Bioretrosynthetic construction of a didanosine biosynthetic pathway

Autor: William R Birmingham, T.D. Panosian, Brian O. Bachmann, D.P. Nannemann, Tina M. Iverson, Chrystal A Starbird

Publikováno v: Nature chemical biology
Birmingham, W R, Starbird, C A, Panosian, T D, Nannemann, D P, Iverson, T M & Bachmann, B O 2014, ' Bioretrosynthetic construction of a didanosine biosynthetic pathway ', Nature chemical biology, vol. 10, no. 5, pp. 392-399 . https://doi.org/10.1038/nchembio.1494

Concatenation of engineered biocatalysts into multistep pathways dramatically increases their utility, but development of generalizable assembly methods remains a significant challenge. Herein we evaluate ‘bioretrosynthesis’, which is an applicat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e2cac0b75f16c7d88e050952c4391c
https://doi.org/10.1038/nchembio.1494

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Molecular Differences between a Mutase and a Phosphatase: Investigations of the Activation Step in Bacillus cereus Phosphopentomutase

Autor: T.D. Panosian, William R. Birmingham, Tina M. Iverson, D.P. Nannemann, Brian O. Bachmann

Publikováno v: Biochemistry. 51:1964-1975

Prokaryotic phosphopentomutases (PPMs) are di-Mn(2+) enzymes that catalyze the interconversion of α-D-ribose 5-phosphate and α-D-ribose 1-phosphate at an active site located between two independently folded domains. These prokaryotic PPMs belong to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe174b5cce43314d6b57b4fe1628a672
https://doi.org/10.1021/bi201761h

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Mechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA pore

Autor: Ilsoo Kim, Tina M. Iverson, Toby W. Allen, T.D. Panosian, Crina M. Nimigean, Ameer N. Thompson

Publikováno v: Nature Structural & Molecular Biology. 16:1317-1324

Potassium channels allow K+ ions to easily diffuse through their pores while effectively preventing smaller Na+ ions from permeation. The ability to discriminate between these two similar and abundant ions is vital for these proteins to control elect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac0c467358efca01ed8ba64ca0d52344
https://doi.org/10.1038/nsmb.1703

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Bacillus cereus Phosphopentomutase Is an Alkaline Phosphatase Family Member That Exhibits an Altered Entry Point into the Catalytic Cycle*

Autor: T.D. Panosian, Brian O. Bachmann, Brian E. Wadzinski, W. Hayes McDonald, Tina M. Iverson, Vanessa V. Phelan, Guy R. Watkins, D.P. Nannemann

Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert α-D-ribose 5-phosphate (ribose 5-phosphate) and α-D-ribose 1-phosphate (ribose 1-phosphate). We investigated the reaction mechanism of Bacillus cere

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d762cfe14a7548263d481596468dcb1
https://europepmc.org/articles/PMC3048691/

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Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus

Autor: Tina M. Iverson, Brian O. Bachmann, T.D. Panosian, D.P. Nannemann

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 66(Pt 7)

Phosphopentomutases (PPMs) interconvert D-ribose 5-phosphate and alpha-D-ribose 1-phosphate to link glucose and nucleotide metabolism. PPM from Bacillus cereus was overexpressed in Escherichia coli, purified to homogeneity and crystallized. Bacterial

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27e93df824c8f0796b9fd305ae6b29fb
https://pubmed.ncbi.nlm.nih.gov/20606280

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New Insights Into Selectivity of Potassium Channels Using Small Cation Blockers

Autor: T.D. Panosian, Ilsoo Kim, Ameer N. Thompson, Tina M. Iverson, Crina M. Nimigean, Toby W. Allen

Publikováno v: Biophysical Journal. (3):660a

KcsA channel pores are blocked by intracellular Na+ and Li+ ions. We are investigating Na+/Li+ binding locations using electrophysiology, X-ray crystallography, and molecular dynamics simulations. We found that intracellular Li+ blocks KcsA channels

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