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Authors: Pallavi Subhraveti Peter D Karp Ingrid Keseler An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Anamika Kothari Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000308495Cyc: Nocardia brevicatena NBRC 12119 Cellular Overview Connections between pathways are omitted for legibility.

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Auxiliary Iron–Sulfur Cofactors in Radical SAM Enzymes☆
Biochimica et Biophysica Acta 1853 (2015) 1316–1334 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbamcr Review Auxiliary iron–sulfur cofactors in radical SAM enzymes☆ Nicholas D. Lanz a, Squire J. Booker a,b,⁎ a Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, United States b Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, United States article info abstract Article history: A vast number of enzymes are now known to belong to a superfamily known as radical SAM, which all contain a Received 19 September 2014 [4Fe–4S] cluster ligated by three cysteine residues. The remaining, unligated, iron ion of the cluster binds in Received in revised form 15 December 2014 contact with the α-amino and α-carboxylate groups of S-adenosyl-L-methionine (SAM). This binding mode Accepted 6 January 2015 facilitates inner-sphere electron transfer from the reduced form of the cluster into the sulfur atom of SAM, Available online 15 January 2015 resulting in a reductive cleavage of SAM to methionine and a 5′-deoxyadenosyl radical. The 5′-deoxyadenosyl Keywords: radical then abstracts a target substrate hydrogen atom, initiating a wide variety of radical-based transforma- – Radical SAM tions. A subset of radical SAM enzymes contains one or more additional iron sulfur clusters that are required Iron–sulfur cluster for the reactions they catalyze. However, outside of a subset of sulfur insertion reactions, very little is known S-adenosylmethionine about the roles of these additional clusters. This review will highlight the most recent advances in the identiﬁca- Cofactor maturation tion and characterization of radical SAM enzymes that harbor auxiliary iron–sulfur clusters.
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Changes in Soil Microbial Communities After Long-Term Warming Exposure" (2019)
University of Massachusetts Amherst ScholarWorks@UMass Amherst Doctoral Dissertations Dissertations and Theses October 2019 CHANGES IN SOIL MICROBIAL COMMUNITIES AFTER LONG- TERM WARMING EXPOSURE William G. Rodríguez-Reillo University of Massachusetts Amherst Follow this and additional works at: https://scholarworks.umass.edu/dissertations_2 Part of the Environmental Microbiology and Microbial Ecology Commons Recommended Citation Rodríguez-Reillo, William G., "CHANGES IN SOIL MICROBIAL COMMUNITIES AFTER LONG-TERM WARMING EXPOSURE" (2019). Doctoral Dissertations. 1757. https://doi.org/10.7275/15007293 https://scholarworks.umass.edu/dissertations_2/1757 This Open Access Dissertation is brought to you for free and open access by the Dissertations and Theses at ScholarWorks@UMass Amherst. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of ScholarWorks@UMass Amherst. For more information, please contact [email protected]. CHANGES IN SOIL MICROBIAL COMMUNITIES AFTER LONG-TERM WARMING EXPOSURE A Dissertation Presented by WILLIAM GABRIEL RODRÍGUEZ-REILLO Submitted to the Graduate School of the University of Massachusetts Amherst in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY SEPTEMBER 2019 Organismic and Evolutionary Biology © Copyright by William Gabriel Rodríguez-Reillo 2019 All Rights Reserved CHANGES IN SOIL MICROBIAL COMMUNITIES AFTER LONG-TERM WARMING EXPOSURE A Dissertation Presented by WILLIAM GABRIEL RODRÍGUEZ-REILLO Approved as to style and content by: _________________________________________ Jeffrey L. Blanchard, Chair _________________________________________ Courtney Babbitt, Member _________________________________________ David Sela, Member _________________________________________ Kristina Stinson, Member ______________________________________ Paige Warren, Graduate Program Director Organismic and Evolutionary Biology DEDICATION To my parents, William Rodriguez Arce and Carmen L. Reillo Batista. A quienes aún en la distancia me mantuvieron en sus oraciones.
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Metabolic Functions of the Human Gut Microbiota: the Role of Metalloenzymes Cite This: DOI: 10.1039/C8np00074c Lauren J
Natural Product Reports View Article Online REVIEW View Journal Metabolic functions of the human gut microbiota: the role of metalloenzymes Cite this: DOI: 10.1039/c8np00074c Lauren J. Rajakovich and Emily P. Balskus * Covering: up to the end of 2017 The human body is composed of an equal number of human and microbial cells. While the microbial community inhabiting the human gastrointestinal tract plays an essential role in host health, these organisms have also been connected to various diseases. Yet, the gut microbial functions that modulate host biology are not well established. In this review, we describe metabolic functions of the human gut microbiota that involve metalloenzymes. These activities enable gut microbial colonization, mediate interactions with the host, and impact human health and disease. We highlight cases in which enzyme characterization has advanced our understanding of the gut microbiota and examples that illustrate the diverse ways in which Received 14th August 2018 Creative Commons Attribution 3.0 Unported Licence. metalloenzymes facilitate both essential and unique functions of this community. Finally, we analyze Human DOI: 10.1039/c8np00074c Microbiome Project sequencing datasets to assess the distribution of a prominent family of metalloenzymes rsc.li/npr in human-associated microbial communities, guiding future enzyme characterization eﬀorts. 1 Introduction our gut from infancy and plays a critical role in the development 2 Commensal colonization of the human gut: tness and and maintenance of healthy human physiology. It aids in adaptation developing the innate and adaptive immune systems,1,2 2.1 Glycan sulfation provides nutrients and vitamins,3 and protects against path- 4 This article is licensed under a 2.2 Glycan fucosylation ogen invasion.
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2018 Summer Symposium Program
Ofce of UNDERGRADUATE RESEARCH ® THE UNIVERSITY OF UTAH 2018 Summer Symposium THURSDAY, AUGUST 2, 2018 9:00AM - 12:00PM CROCKER SCIENCE CENTER UNIVERSITY OF UTAH 2018 SUMMER SYMPOSIUM Thursday, August 2, 2018 9:00 AM – 12:00 PM Crocker Science Center University of Utah The Office of Undergraduate Research is grateful for the generous support of the Office of the Vice President for Research. We are also thankful for the development of the Summer Research Program Partnership, which is a new collaboration among the Chemistry Research Experience for Undergraduates (REU), the Huntsman Cancer Institute’s PathMaker Cancer Research Program, the Native American Summer Research Internship (NARI), the Physics & Astronomy REU and Summer Undergraduate Research Program, and the Summer Program for Undergraduate Research (SPUR). Together, these programs are serving more than 90 undergraduate researchers in Summer 2018. Finally, we would like to express our utmost pride and congratulations to the students, graduate students, and faculty mentors without whose efforts and dedication this event would not be possible. PROGRAM SCHEDULE NOTE: All student presenters MUST check-in Snacks available at 10:15 AM in Room 205/206 8:30 – 9:00 AM CHECK-IN & POSTER SET-UP 9:00 – 10:30 AM POSTER SESSION I (ODD POSTERS) 10:30 AM – 12:00 PM POSTER SESSION II (EVEN POSTERS) 12:00 – 12:15 PM POSTER TAKE-DOWN 2 SCHEDULE OF PRESENTATIONS POSTER SESSION I 9:00 – 10:30 AM Poster 1 Presenter: Sara Alektiar (University of Michigan) Mentor: Matthew Sigman (Chemistry) Electrocatalytic Bis(bipyidine)ruthenium Hydroxylation of Tertiary and Benzylic C-H Bonds The Sigman and Du Bois labs recently reported a methodology that employs a bis(bipyridine)Ru catalyst operating in acidic water to achieve oxidation of tertiary and benzylic C-H bonds in the presence of basic amines.
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Generated by SRI International Pathway Tools Version 25.0 on Mon
Authors: Pallavi Subhraveti Ron Caspi Peter Midford Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_000716605Cyc: Streptomyces sp. NRRL F-525 NRRL F-525 Cellular Overview Connections between pathways are omitted for legibility. Anamika Kothari an amino an amino an amino an amino an amino an amino an amino an amino phosphate phosphate acid acid acid acid acid acid acid acid molybdate an amino an amino H + a dipeptide phosphate phosphate phosphate acid an amino acid an amino H + phosphate phosphate glycine betaine glycine betaine glycine betaine leu pro pro pro acid acid predicted predicted predicted predicted predicted predicted predicted predicted predicted predicted predicted predicted ABC ABC ABC ABC ABC ABC ABC ABC ABC ABC ABC F0F1 ATP ABC RS16420 RS10685 RS06340 RS46495 RS16425 ProP RS28920 RS26410 LeuE RS27350 RS38790 RS13800 transporter transporter transporter RS41005 transporter transporter transporter transporter transporter CoxB transporter transporter transporter synthase transporter of an of an of an of an of an of an of an of an of molybdate of phosphate of phosphate of a dipeptide amino acid
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Supplementary Material
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Genome Properties Documentation Release 0.1B
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Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-Translationally Modified Peptides (Ripps)
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