PEPCK-M recoups tumor cell anabolic potential in a PKC-ζ-dependent manner [PDF]
, 2021 Background: Mitochondrial phosphoenolpyruvate carboxykinase (PEPCK-M; PCK2) is expressed in all cancer types examined and in neuroprogenitor cells. The gene is upregulated by amino acid limitation and ER-stress in an ATF4- dependent manner, and its ...
Aragó, Marc +9 more
core +2 more sources
Food Science &Nutrition, Volume 13, Issue 1, January 2025.Camellia seed oil is rich in bioactive compounds, which could promote the in vitro proliferation of Akkermansia muciniphila by reducing the oxidation–reduction potential of the media and activating the metabolism pathways involving energy and nucleic acid metabolism, protein synthesis, and environmental adaptation, thereby facilitating the nutrient ...
Xi Chen +3 more
wiley +1 more source
Roles of Asp75, Asp78, and Glu83 of GTP-dependent Phosphoenolpyruvate Carboxykinase from Mycobacterium smegmatis [PDF]
Journal of Biological Chemistry, 2006 The roles of Asp(75), Asp(78), and Glu(83) of the (75)DPSDVARVE(83) element of Mycobacterium smegmatis GTP-dependent phosphoenolpyruvate (PEP) carboxykinase (GTP-PEPCK) were investigated. Asp(78) and Glu(83) are fully conserved in GTP-PEP-CKs. The human PEPCK crystal structure suggests that Asp(78) influences Tyr(220); Tyr(220) helps to position bound ...
Biswarup Mukhopadhyay +3 more
openaire +3 more sources
PROTEOMICS – Clinical Applications, Volume 18, Issue 6, November 2024.ABSTRACT Background: Human macrophages generate antimicrobial reactive nitrogen species in response to infection by Mycobacterium tuberculosis (Mtb). Exposure to these redox‐reactive compounds induces stress response in Mtb, which can affect posttranslational modifications (PTM). Methods: Here, we present the global analysis of the PTM acylation of Mtb
Alemayehu Godana Birhanu +3 more
wiley +1 more source
Conformational Entropy in PEPCK Catalysis: Dynamic Motions Critical to Function [PDF]
, 2011 Enzymes increase the rate at which chemical reactions occur. How they achieve this rate increase has been an area of intense research for many years.
Johnson, Troy A.
core
Effect of hyperosmotic shock on phosphoenolpyruvate carboxykinase gene expression and gluconeogenic activity in the crab muscle [PDF]
, 2004 Chasmagnathus granulata phosphoenolpyruvate carboxykinase (PEPCK) cDNA from jaw muscle was cloned and sequenced, showing a specific domain to bind phosphoenolpyruvate in addition to the kinase-1 and kinase-2 motifs to bind guanosine triphosphate (GTP ...
Da Silva, Roselis S.M +5 more
core +1 more source
Plant Direct, Volume 8, Issue 6, June 2024.Abstract The coordination of assimilation pathways for all the elements that make up cellular components is a vital task for every organism. Integrating the assimilation and use of carbon (C) and nitrogen (N) is of particular importance because of the high cellular abundance of these elements.
Lisa Scholtysek +3 more
wiley +1 more source
The PEP—pyruvate—oxaloacetate node as the switch point for carbon flux distribution in bacteria: We dedicate this paper to Rudolf K. Thauer, Director of the Max-Planck-Institute for Terrestrial Microbiology in Marburg, Germany, on the occasion of his 65th birthday [PDF]
, 2017 In many organisms, metabolite interconversion at the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node involves a structurally entangled set of reactions that interconnects the major pathways of carbon metabolism and thus, is responsible for the ...
Eikmanns, Bernhard J., Sauer, Uwe
core
Propionate induces gluconeogenesis in dairy cattle through direct activation of the bovine cytosolic phosphoenolpyruvate carboxykinase gene promoter [PDF]
, 2015 Phosphoenolpyruvate carboxykinase (PCK, GTP; EC4.1.1.32) catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), a critical reaction for gluconeogenesis. The two isoforms of PCK, namely cytosolic PCK (PCK1), and the mitochondrial PCK
Zhang, Qian
core +1 more source
Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase [PDF]
, 2020 Guanylate binding proteins (GBPs) are soluble dynamin-like proteins with structured domains that undergo a conformational transition for GTP-controlled oligomerization to exert their function as part of the innate immune system of mammalian cells - attacking intra-cellular parasites by disrupting their membranes.
arxiv +1 more source