Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Krista A, Shisler"'
Autor:
Krista A. Shisler, William M. Kincannon, Jenna R. Mattice, James Larson, Adam Valaydon-Pillay, Florence Mus, Tamara Flusche, Arnab Kumar Nath, Sebastian A. Stoian, Simone Raugei, Brian Bothner, Jennifer L. DuBois, John W. Peters
Publikováno v:
mBio, Vol 15, Iss 2 (2024)
ABSTRACT Acetone carboxylases (ACs) catalyze the metal- and ATP-dependent conversion of acetone and bicarbonate to form acetoacetate. Interestingly, two homologous ACs that have been biochemically characterized have been reported to have different me
Externí odkaz:
https://doaj.org/article/7a957b0e440a4b67b606f1f3d09be52c
Publikováno v:
The Journal of biological chemistry. 298(5)
2-Ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) is a member of the flavin and cysteine disulfide containing oxidoreductase family (DSOR) that catalyzes the unique reaction between atmospheric CO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::54ae88fe0a913b0daea03ae6c0e9cecc
https://pubmed.ncbi.nlm.nih.gov/35367206
https://pubmed.ncbi.nlm.nih.gov/35367206
Publikováno v:
Journal of Biological Chemistry. 298:101884
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbaf09215d4b7738aa7dc74b5bfc1229
https://doi.org/10.1016/j.jbc.2022.101884
https://doi.org/10.1016/j.jbc.2022.101884
Autor:
Krista A. Shisler, Alexander B. Alleman, Jennifer L. DuBois, Brian Bothner, Hsin-Hua Wu, Oleg A. Zadvornyy, John W. Peters, Florence Mus
Publikováno v:
The Biochemical journal. 477(11)
Alkenes and ketones are two classes of ubiquitous, toxic organic compounds in natural environments produced in several biological and anthropogenic processes. In spite of their toxicity, these compounds are utilized as primary carbon and energy sourc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a64374c92086e4e5532c3ea852c8f404
https://pubmed.ncbi.nlm.nih.gov/32497192
https://pubmed.ncbi.nlm.nih.gov/32497192
Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b
Autor:
Bennett R. Streit, Eric M. Shepard, Jennifer L. DuBois, Garrett C. Moraski, Krista A. Shisler, Arianna I. Celis, Gudrun S. Lukat-Rodgers, Kenton R. Rodgers
Publikováno v:
Journal of Biological Chemistry. 293:3989-3999
The H(2)O(2)-dependent oxidative decarboxylation of coproheme III is the final step in the biosynthesis of heme b in many microbes. However, the coproheme decarboxylase reaction mechanism is unclear. The structure of the decarboxylase in complex with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c42815c79da13cf982a00d8af850d579
https://doi.org/10.1074/jbc.ra117.000830
https://doi.org/10.1074/jbc.ra117.000830
Autor:
Krista A. Shisler, Gregory A. Prussia, Bennett R. Streit, John W. Peters, Oleg A. Zadvornyy, Jennifer L. DuBois
Publikováno v:
The Journal of Biological Chemistry
The 2-ketopropyl-coenzyme M oxidoreductase/carboxylase (2-KPCC) enzyme is the only member of the disulfide oxidoreductase (DSOR) family of enzymes, which are important for reductively cleaving S-S bonds, to have carboxylation activity. 2-KPCC catalyz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05bc6975d06f195964f6e1d4420aaa73
https://doi.org/10.1016/j.jbc.2021.100961
https://doi.org/10.1016/j.jbc.2021.100961
Autor:
Robert J. Usselman, Joan B. Broderick, Krista A. Shisler, Eric M. Shepard, Jeremiah N. Betz, Priyanka Aggarwal, Gareth R. Eaton, Amanda S. Byer, Anna G. Scott, Sandra S. Eaton
Publikováno v:
Biochemistry
Nature utilizes [FeFe]-hydrogenase enzymes to catalyze the interconversion between H2 and protons and electrons. Catalysis occurs at the H-cluster, a carbon monoxide-, cyanide-, and dithiomethylamine-coordinated 2Fe subcluster bridged via a cysteine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebec9820ca6ef2b9b3a2f1a97b65f9b8
https://doi.org/10.1021/acs.biochem.7b00169
https://doi.org/10.1021/acs.biochem.7b00169
Autor:
Gudrun S. Lukat-Rodgers, Bennett R. Streit, George H. Gauss, Kenton R. Rodgers, Krista A. Shisler, Arianna I. Celis, John W. Peters, Garrett C. Moraski, Jennifer L. DuBois
Publikováno v:
Journal of the American Chemical Society. 139:1900-1911
Coproheme decarboxylase catalyzes two sequential oxidative decarboxylations with H2O2 as the oxidant, coproheme III as substrate and cofactor, and heme b as the product. Each reaction breaks a C-C bond and results in net loss of hydride, via steps th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01e09b5196c8627155c54d69c336ffe5
https://doi.org/10.1021/jacs.6b11324
https://doi.org/10.1021/jacs.6b11324
Autor:
Jennifer L. DuBois, Krista A. Shisler, Bennett R. Streit, Gudrun S. Lukat-Rodgers, Kenton R. Rodgers, Arianna I. Celis
Publikováno v:
Biochemistry. 56:189-201
A recently discovered pathway for the biosynthesis of heme b ends in an unusual reaction catalyzed by coproheme decarboxylase (HemQ), where the Fe(II)-containing coproheme acts as both substrate and cofactor. Because both O2 and H2O2 are available as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::859e379c32ac7789603737202ee41e0d
https://doi.org/10.1021/acs.biochem.6b00958
https://doi.org/10.1021/acs.biochem.6b00958
Autor:
Masaki Horitani, Eric M. Shepard, Ashley Rasmussen, Kaitlin S. Duschene, Adam V. Crain, Rachel U. Hutcheson, Catherine L. Drennan, Amanda S. Byer, Jessica L. Vey, Jian Yang, Krista A. Shisler, William E. Broderick, Joan B. Broderick, Brian M. Hoffman
Publikováno v:
Journal of the American Chemical Society
Pyruvate formate-lyase activating enzyme (PFL-AE) is a radical S-adenosyl-l-methionine (SAM) enzyme that installs a catalytically essential glycyl radical on pyruvate formate-lyase. We show that PFL-AE binds a catalytically essential monovalent catio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b35972665d1be1e7c7864bfea1c212fd
https://pubmed.ncbi.nlm.nih.gov/28768413
https://pubmed.ncbi.nlm.nih.gov/28768413