Výsledky vyhledávání - "Molly J. McBride"

Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States

Autor: Jeffrey W. Slater, Monica E. Neugebauer, Molly J. McBride, Debangsu Sil, Chi-Yun Lin, Bryce J. Katch, Amie K. Boal, Michelle C.Y. Chang, Alexey Silakov, Carsten Krebs, J. Martin Bollinger

Publikováno v: bioRxiv

An aliphatic halogenase requires four substrates: 2-oxoglutarate (2OG), halide (Cl−or Br−), the halogenation target (“prime substrate”), and dioxygen. In well-studied cases, the three non-gaseous substrates must bind to activate the enzyme’

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14b9fbd5470ea79412bbe4a20efb2a5d
https://doi.org/10.1101/2023.05.02.539147

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Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro-l-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate

Autor: Molly J. McBride, Mrutyunjay A. Nair, Debangsu Sil, Jeffrey W. Slater, Monica E. Neugebauer, Michelle C. Y. Chang, Amie K. Boal, Carsten Krebs, J. Martin Bollinger

Publikováno v: Biochemistry

The enzyme BesC from the β-ethynyl-L-serine biosynthetic pathway in Streptomyces cattleya fragments 4-chloro-L-lysine (produced from L-Lysine by BesD) to ammonia, formaldehyde, and 4-chloro-L-allylglycine and can analogously fragment L-Lys itself. B

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76f6540199357ff8469be639a7484ad9
https://doi.org/10.1021/acs.biochem.1c00774

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A Peroxodiiron(III/III) Intermediate Mediating Both N-Hydroxylation Steps in Biosynthesis of the N-Nitrosourea Pharmacophore of Streptozotocin by the Multi-domain Metalloenzyme SznF

Autor: Grace E. Kenney, Molly J. McBride, Tai L. Ng, Bo Zhang, J. Martin Bollinger, Anne Marie Crooke, Christina Tysoe, Carsten Krebs, Debangsu Sil, Emily P. Balskus, Amie K. Boal

Publikováno v: Journal of the American Chemical Society. 142:11818-11828

The alkylating warhead of the pancreatic cancer drug streptozotocin (SZN) contains an N-nitrosourea moiety constructed from Nω-methyl-l-arginine (l-NMA) by the multi-domain metalloenzyme SznF. The enzyme's central heme-oxygenase-like (HO-like) domai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::da8d74a99f1201a56f8a0eae42686a46
https://doi.org/10.1021/jacs.0c03431

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Biochemical and Structural Characterization of XoxG and XoxJ and Their Roles in Lanthanide‐Dependent Methanol Dehydrogenase Activity

Autor: Emily R. Featherston, Molly J. McBride, Ellison M. Taylor, Amie K. Boal, Hannah R. Rose, Joseph A. Cotruvo

Publikováno v: Chembiochem

Lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have recently been shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems contain two other proteins, XoxG (a c-type cytochrome) and XoxJ (a per

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c93a9b5aeedd66d7eaf4a524cac8308
https://doi.org/10.1002/cbic.201900184

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Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of the

Autor: Molly J, McBride, Sarah R, Pope, Kai, Hu, C Denise, Okafor, Emily P, Balskus, J Martin, Bollinger, Amie K, Boal

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance The enzyme SznF assembles the N-nitrosourea pharmacophore of the drug streptozotocin. Its N-oxygenase domain resembles heme-oxygenase (HO) and belongs to an emerging superfamily of HO-like diiron enzymes (HDOs) with unstable metallocofac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7956bcb6ea8e2c60f40ad5703206003d
https://pubmed.ncbi.nlm.nih.gov/33468680

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Structure and assembly of the diiron cofactor in the heme-oxygenase–like domain of the N -nitrosourea–producing enzyme SznF

Autor: Emily P. Balskus, Amie K. Boal, Sarah R. Pope, C. Denise Okafor, Molly J. McBride, Kai Hu, J. Martin Bollinger

Publikováno v: Proceedings of the National Academy of Sciences. 118

In biosynthesis of the pancreatic cancer drug streptozotocin, the tridomain nonheme-iron oxygenase SznF hydroxylates Nδ and Nω′ of Nω-methyl-l-arginine before oxidatively rearranging the triply modified guanidine to the N-methyl-N-nitrosourea ph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b49d8140ce9ad76bf73b55fe0113e841
https://doi.org/10.1073/pnas.2015931118

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Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of theN-nitrosourea-producing enzyme SznF

Autor: Molly J. McBride, Emily P. Balskus, C. Denise Okafor, Jeffrey W. Slater, Kai Hu, J. Martin Bollinger, Amie K. Boal, Sarah R. Pope

In biosynthesis of the pancreatic cancer drug streptozotocin, the tri-domain nonheme-iron oxygenase, SznF, hydroxylatesNδandNω’ ofNω-methyl-L-arginine before oxidatively rearranging the triply modified guanidine to theN-methyl-N-nitrosourea phar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0de0983cd72b6c2dfb5c5e7398f76854
https://doi.org/10.1101/2020.07.29.227702

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