دورية أكاديمية
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Biophysical and biochemical studies support TP0094 as a phosphotransacetylase in an acetogenic energy-conservation pathway in Treponema pallidum.

التفاصيل البيبلوغرافية
العنوان: Biophysical and biochemical studies support TP0094 as a phosphotransacetylase in an acetogenic energy-conservation pathway in Treponema pallidum.
المؤلفون: Brautigam CA; Department of Biophysics, UT Southwestern Medical Center, Dallas, Texas, United States of America.; Department of Microbiology, UT Southwestern Medical Center, Dallas, Texas, United States of America., Deka RK; Department of Microbiology, UT Southwestern Medical Center, Dallas, Texas, United States of America., Tso SC; Department of Biophysics, UT Southwestern Medical Center, Dallas, Texas, United States of America., Liu WZ; Department of Microbiology, UT Southwestern Medical Center, Dallas, Texas, United States of America., Norgard MV; Department of Microbiology, UT Southwestern Medical Center, Dallas, Texas, United States of America.
المصدر: PloS one [PLoS One] 2023 May 18; Vol. 18 (5), pp. e0283952. Date of Electronic Publication: 2023 May 18 (Print Publication: 2023).
نوع المنشور: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Treponema pallidum*/genetics , Syphilis*/microbiology, Humans ; Phosphate Acetyltransferase/metabolism ; Bacterial Proteins/metabolism ; Treponema/genetics
مستخلص: The mechanisms of energy generation and carbon-source utilization in the syphilis spirochete Treponema pallidum have remained enigmatic despite complete genomic sequence information. Whereas the bacterium harbors enzymes for glycolysis, the apparatus for more efficient use of glucose catabolites, namely the citric-acid cycle, is apparently not present. Yet, the organism's energy needs likely exceed the modest output from glycolysis alone. Recently, building on our structure-function studies of T. pallidum lipoproteins, we proposed a "flavin-centric" metabolic lifestyle for the organism that partially resolves this conundrum. As a part of the hypothesis, we have proposed that T. pallidum contains an acetogenic energy-conservation pathway that catabolizes D-lactate, yielding acetate, reducing equivalents for the generation and maintenance of chemiosmotic potential, and ATP. We already have confirmed the D-lactate dehydrogenase activity in T. pallidum necessary for this pathway to operate. In the current study, we focused on another enzyme ostensibly involved in treponemal acetogenesis, phosphotransacetylase (Pta). This enzyme is putatively identified as TP0094 and, in this study, we determined a high-resolution (1.95 Å) X-ray crystal structure of the protein, finding that its fold comports with other known Pta enzymes. Further studies on its solution behavior and enzyme activity confirmed that it has the properties of a Pta. These results are consistent with the proposed acetogenesis pathway in T. pallidum, and we propose that the protein be referred to henceforth as TpPta.
Competing Interests: The authors have declared that no competing interests exist.
(Copyright: © 2023 Brautigam et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)
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معلومات مُعتمدة: R01 AI056305 United States AI NIAID NIH HHS; S10 OD030312 United States OD NIH HHS
المشرفين على المادة: EC 2.3.1.8 (Phosphate Acetyltransferase)
0 (Bacterial Proteins)
تواريخ الأحداث: Date Created: 20230518 Date Completed: 20230522 Latest Revision: 20230920
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC10194888
DOI: 10.1371/journal.pone.0283952
PMID: 37200262
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0283952