Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10105549" target="_blank" >RIV/00216208:11310/11:10105549 - isvavai.cz</a>

Výsledek na webu

<a href="http://mbe.oxfordjournals.org/content/early/2011/02/03/molbev.msr032.full.pdf+html" target="_blank" >http://mbe.oxfordjournals.org/content/early/2011/02/03/molbev.msr032.full.pdf+html</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/molbev/msr032" target="_blank" >10.1093/molbev/msr032</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute

Popis výsledku v původním jazyce

Most of the major groups of eukaryotes have microbial representatives that thrive in low oxygen conditions. Those that have been studied in detail generate ATP via pathways involving anaerobically functioning enzymes of pyruvate catabolism that are typically absent in aerobic eukaryotes and whose origins remain controversial. Pyruvate formate lyase (Pfl) catalyzes the non-oxidative generation of formate and acetyl-Coenzyme A (CoA) from pyruvate and CoA and is activated by Pfl activating enzyme (Pfla). To clarify the origins of this pathway, we have comprehensively searched for homologs of Pfl and Pfla in publicly available large-scale eukaryotic genomic and cDNA sequencing data, including our own from the anaerobic amoebozoan Mastigamoeba balamuthi. Surprisingly, we find that these enzymes are widely distributed, and are present in diverse facultative or obligate anaerobic eukaryotic representatives of the archaeplastidan, metazoan, amoebozoan, and haptophyte lineages. Using maximum li

Název v anglickém jazyce

Eukaryotic pyruvate formate lyase and its activating enzyme were acquired laterally from a firmicute

Popis výsledku anglicky

Most of the major groups of eukaryotes have microbial representatives that thrive in low oxygen conditions. Those that have been studied in detail generate ATP via pathways involving anaerobically functioning enzymes of pyruvate catabolism that are typically absent in aerobic eukaryotes and whose origins remain controversial. Pyruvate formate lyase (Pfl) catalyzes the non-oxidative generation of formate and acetyl-Coenzyme A (CoA) from pyruvate and CoA and is activated by Pfl activating enzyme (Pfla). To clarify the origins of this pathway, we have comprehensively searched for homologs of Pfl and Pfla in publicly available large-scale eukaryotic genomic and cDNA sequencing data, including our own from the anaerobic amoebozoan Mastigamoeba balamuthi. Surprisingly, we find that these enzymes are widely distributed, and are present in diverse facultative or obligate anaerobic eukaryotic representatives of the archaeplastidan, metazoan, amoebozoan, and haptophyte lineages. Using maximum li

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

—

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Biology and Evolution

ISSN

0737-4038

e-ISSN

—

Svazek periodika

28

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

2087-2099

Kód UT WoS článku

000291756400013

EID výsledku v databázi Scopus

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