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  1. Article ; Online: Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase.

    Drago, Victoria N / Devos, Juliette M / Blakeley, Matthew P / Forsyth, V Trevor / Parks, Jerry M / Kovalevsky, Andrey / Mueser, Timothy C

    Cell reports. Physical science

    2024  Volume 5, Issue 2

    Abstract: Pyridoxal 5'-phosphate (PLP), the biologically active form of vitamin ... ...

    Abstract Pyridoxal 5'-phosphate (PLP), the biologically active form of vitamin B
    Language English
    Publishing date 2024-02-12
    Publishing country United States
    Document type Journal Article
    ISSN 2666-3864
    ISSN (online) 2666-3864
    DOI 10.1016/j.xcrp.2024.101827
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography.

    Drago, Victoria N / Campos, Claudia / Hooper, Mattea / Collins, Aliyah / Gerlits, Oksana / Weiss, Kevin L / Blakeley, Matthew P / Phillips, Robert S / Kovalevsky, Andrey

    Communications chemistry

    2023  Volume 6, Issue 1, Page(s) 162

    Abstract: Pyridoxal 5'-phosphate (PLP)-dependent enzymes utilize a vitamin ... ...

    Abstract Pyridoxal 5'-phosphate (PLP)-dependent enzymes utilize a vitamin B
    Language English
    Publishing date 2023-08-03
    Publishing country England
    Document type Journal Article
    ZDB-ID 2929562-2
    ISSN 2399-3669 ; 2399-3669
    ISSN (online) 2399-3669
    ISSN 2399-3669
    DOI 10.1038/s42004-023-00964-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Microgravity crystallization of perdeuterated tryptophan synthase for neutron diffraction.

    Drago, Victoria N / Devos, Juliette M / Blakeley, Matthew P / Forsyth, V Trevor / Kovalevsky, Andrey Y / Schall, Constance A / Mueser, Timothy C

    NPJ microgravity

    2022  Volume 8, Issue 1, Page(s) 13

    Abstract: Biologically active vitamin ... ...

    Abstract Biologically active vitamin B
    Language English
    Publishing date 2022-05-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2823626-9
    ISSN 2373-8065
    ISSN 2373-8065
    DOI 10.1038/s41526-022-00199-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: 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 / Blakeley, Matthew P / Keen, David A / Coquelle, Nicolas / Weiss, Kevin L / Gerlits, Oksana / Kovalevsky, Andrey / Mueser, Timothy C

    Chemical science

    2022  Volume 13, Issue 34, Page(s) 10057–10065

    Abstract: Pyridoxal 5'-phosphate (PLP)-dependent enzymes have been extensively studied for their ability to fine-tune PLP cofactor electronics to promote a wide array of chemistries. Neutron crystallography offers a straightforward approach to studying the ... ...

    Abstract Pyridoxal 5'-phosphate (PLP)-dependent enzymes have been extensively studied for their ability to fine-tune PLP cofactor electronics to promote a wide array of chemistries. Neutron crystallography offers a straightforward approach to studying the electronic states of PLP and the electrostatics of enzyme active sites, responsible for the reaction specificities, by enabling direct visualization of hydrogen atom positions. Here we report a room-temperature joint X-ray/neutron structure of aspartate aminotransferase (AAT) with pyridoxamine 5'-phosphate (PMP), the cofactor product of the first half reaction catalyzed by the enzyme. Between PMP N
    Language English
    Publishing date 2022-08-17
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d2sc02285k
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Synthesis and in Vitro Characterization of Trehalose-Based Inhibitors of Mycobacterial Trehalose 6-Phosphate Phosphatases.

    Kapil, Sunayana / Petit, Cecile / Drago, Victoria N / Ronning, Donald R / Sucheck, Steven J

    Chembiochem : a European journal of chemical biology

    2018  Volume 20, Issue 2, Page(s) 260–269

    Abstract: α,α'-Trehalose plays roles in the synthesis of several cell wall components involved in pathogenic mycobacteria virulence. Its absence in mammalian biochemistry makes trehalose-related biochemical processes potential targets for chemotherapy. The ... ...

    Abstract α,α'-Trehalose plays roles in the synthesis of several cell wall components involved in pathogenic mycobacteria virulence. Its absence in mammalian biochemistry makes trehalose-related biochemical processes potential targets for chemotherapy. The trehalose 6-phosphate synthase (TPS)/trehalose 6-phosphate phosphatase (TPP) pathway, also known as the OtsA/OtsB2 pathway, is the major pathway involved in the production of trehalose in Mycobacterium tuberculosis (Mtb). In addition, TPP is essential for Mtb survival. We describe the synthesis of α,α'-trehalose derivatives in the forms of the 6-phosphonic acid 4 (TMP), the 6-methylenephosphonic acid 5 (TEP), and the 6-N-phosphonamide 6 (TNP). These non-hydrolyzable substrate analogues of TPP were examined as inhibitors of Mtb, Mycobacterium lentiflavum (Mlt), and Mycobacterium triplex (Mtx) TPP. In all cases the compounds were most effective in inhibiting Mtx TPP, with TMP [IC
    MeSH term(s) Carbohydrate Conformation ; Dose-Response Relationship, Drug ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Glucosyltransferases/antagonists & inhibitors ; Glucosyltransferases/metabolism ; Mycobacterium tuberculosis/enzymology ; Phosphoric Monoester Hydrolases/antagonists & inhibitors ; Phosphoric Monoester Hydrolases/metabolism ; Structure-Activity Relationship ; Trehalose/chemical synthesis ; Trehalose/chemistry ; Trehalose/pharmacology
    Chemical Substances Enzyme Inhibitors ; Trehalose (B8WCK70T7I) ; Glucosyltransferases (EC 2.4.1.-) ; trehalose-6-phosphate synthase (EC 2.4.1.15) ; trehalose-phosphatase (EC 3.1.3.12) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2)
    Language English
    Publishing date 2018-12-20
    Publishing country Germany
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.201800551
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate.

    Holmes, Jacob B / Liu, Viktoriia / Caulkins, Bethany G / Hilario, Eduardo / Ghosh, Rittik K / Drago, Victoria N / Young, Robert P / Romero, Jennifer A / Gill, Adam D / Bogie, Paul M / Paulino, Joana / Wang, Xiaoling / Riviere, Gwladys / Bosken, Yuliana K / Struppe, Jochem / Hassan, Alia / Guidoulianov, Jevgeni / Perrone, Barbara / Mentink-Vigier, Frederic /
    Chang, Chia-En A / Long, Joanna R / Hooley, Richard J / Mueser, Timothy C / Dunn, Michael F / Mueller, Leonard J

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 2

    Abstract: NMR-assisted crystallography-the integrated application of solid-state NMR, X-ray crystallography, and first-principles computational chemistry-holds significant promise for mechanistic enzymology: by providing atomic-resolution characterization of ... ...

    Abstract NMR-assisted crystallography-the integrated application of solid-state NMR, X-ray crystallography, and first-principles computational chemistry-holds significant promise for mechanistic enzymology: by providing atomic-resolution characterization of stable intermediates in enzyme active sites, including hydrogen atom locations and tautomeric equilibria, NMR crystallography offers insight into both structure and chemical dynamics. Here, this integrated approach is used to characterize the tryptophan synthase α-aminoacrylate intermediate, a defining species for pyridoxal-5'-phosphate-dependent enzymes that catalyze β-elimination and replacement reactions. For this intermediate, NMR-assisted crystallography is able to identify the protonation states of the ionizable sites on the cofactor, substrate, and catalytic side chains as well as the location and orientation of crystallographic waters within the active site. Most notable is the water molecule immediately adjacent to the substrate β-carbon, which serves as a hydrogen bond donor to the ε-amino group of the acid-base catalytic residue βLys87. From this analysis, a detailed three-dimensional picture of structure and reactivity emerges, highlighting the fate of the L-serine hydroxyl leaving group and the reaction pathway back to the preceding transition state. Reaction of the α-aminoacrylate intermediate with benzimidazole, an isostere of the natural substrate indole, shows benzimidazole bound in the active site and poised for, but unable to initiate, the subsequent bond formation step. When modeled into the benzimidazole position, indole is positioned with C3 in contact with the α-aminoacrylate C
    MeSH term(s) Alanine/analogs & derivatives ; Catalysis ; Catalytic Domain ; Crystallography, X-Ray/methods ; Indoles ; Magnetic Resonance Imaging ; Magnetic Resonance Spectroscopy/methods ; Nuclear Magnetic Resonance, Biomolecular ; Pyridoxal Phosphate/metabolism ; Tryptophan Synthase/chemistry ; Tryptophan Synthase/metabolism
    Chemical Substances Indoles ; Pyridoxal Phosphate (5V5IOJ8338) ; indole (8724FJW4M5) ; dehydroalanine (98RA387EKY) ; Tryptophan Synthase (EC 4.2.1.20) ; Alanine (OF5P57N2ZX)
    Language English
    Publishing date 2022-01-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2109235119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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