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Structure and Mechanism of Phosphoenolpyruvate Carboxykinase
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Distantly related sequences in the alpha‐ and beta‐subunits of ATP synthase, myosin, kinases and other ATP‐requiring enzymes and a common nucleotide binding fold.
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Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.
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Protein Structure Comparison by Alignment of Distance Matrices
inferredcites →https://doi.org/10.1006/jmbi.1996.0072openalex-snapshot
Crystal Structure ofEscherichia coliPhosphoenolpyruvate Carboxykinase: A New Structural Family with the P-loop Nucleoside Triphosphate Hydrolase Fold
inferredcites →https://doi.org/10.1007/bf00020190openalex-snapshot
Isolation and sequence analysis of cDNAs encoding phosphoenolpyruvate carboxykinase from the PCK-type C4 grass Urochloa panicoides
inferredcites →https://doi.org/10.1007/bf00193217openalex-snapshot
Phosphoenolpyruvate carboxykinase from higher plants: Purification from cucumber and evidence of rapid proteolytic cleavage in extracts from a range of plant tissues
inferredcites →https://doi.org/10.1007/bf01025041openalex-snapshot
Limited proteolysis ofSaccharomyces cerevisiae phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1007/bf01025121openalex-snapshot
Reactivity of cysteinyl, arginyl, and lysyl residues ofEscherichia coli phosphoenolpyruvate carboxykinase against group-specific chemical reagents
inferredcites →https://doi.org/10.1007/bf01886854openalex-snapshot
Woodward's reagent K reacts with histidine and cysteine residues inEscherichia coli andSaccharomyces cerevisiae phosphoenolpyruvate carboxykinases
inferredcites →https://doi.org/10.1016/0003-2697(85)90101-0openalex-snapshot
Purification of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae and its use for bicarbonate assay
inferredcites →https://doi.org/10.1016/0003-9861(87)90335-3openalex-snapshot
The phosphoenolpyruvate carboxykinase of Trypanosoma (Schizotrypanum) cruzi epimastigotes: Molecular, kinetic, and regulatory properties
inferredcites →https://doi.org/10.1016/0003-9861(88)90005-7openalex-snapshot
Affinity labeling of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase with the 2′,3′-dialdehyde derivative of ATP
inferredcites →https://doi.org/10.1016/0003-9861(90)90241-popenalex-snapshot
Analogs of oxalacetate as potential substrates for phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1016/0014-5793(95)00107-kopenalex-snapshot
Identification of reactive lysines in phosphoenolpyruvate carboxykinases from Escherichia coli and Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/0014-5793(95)00212-ropenalex-snapshot
Purification, and phosphorylation in vivo and in vitro, of phosphoenolpyruvate carboxykinase from cucumber cotyledons
inferredcites →https://doi.org/10.1016/0022-2836(80)90103-5openalex-snapshot
Structure of a complex between yeast hexokinase A and glucose
inferredcites →https://doi.org/10.1016/0022-2836(90)90278-topenalex-snapshot
Calcium binding sites in tomato bushy stunt virus visualized by laue crystallography
inferredcites →https://doi.org/10.1016/0022-2836(91)90654-oopenalex-snapshot
Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12
inferredcites →https://doi.org/10.1016/0022-2836(91)90756-vopenalex-snapshot
The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
inferredcites →https://doi.org/10.1016/0166-6851(87)90098-3openalex-snapshot
A nuclear magnetic resonance study of the role of phosphoenol pyruvate carboxykinase (PEPCK) in the glucose metabolism of Dipetalonema viteae
inferredcites →https://doi.org/10.1016/0166-6851(92)90226-aopenalex-snapshot
Cloning of a cDNA encoding phosphoenolpyruvate carboxykinase from Haemonchus contortus
inferredcites →https://doi.org/10.1016/0166-6851(95)00099-mopenalex-snapshot
Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
inferredcites →https://doi.org/10.1016/0167-4838(87)90024-0openalex-snapshot
The presence of functional arginine residues in phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/0167-4838(93)90147-jopenalex-snapshot
Comparative steady-state fluorescence studies of cytosolic rat liver (GTP), Saccharomyces cerevisiae (ATP) and Escherichia coli (ATP) phosphoenolpyruvate carboxykinases
inferredcites →https://doi.org/10.1016/0167-4838(93)90200-bopenalex-snapshot
The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1016/0167-4838(95)00107-6openalex-snapshot
Circular dichroism and fourier transform infrared spectroscopic studies on the secondary structure of Saccharomyces cerevisiae and Escherichia coli phospho enolpyruvate carboxykinases
inferredcites →https://doi.org/10.1016/0167-4838(95)00201-4openalex-snapshot
Trypanosoma cruzi phospho enol pyruvate carboxykinase (ATP-dependent) : transition metal ion requirement for activity and sulfhydryl group reactivity
inferredcites →https://doi.org/10.1016/0167-4889(89)90028-1openalex-snapshot
Studies on the degradative mechanism of phosphoenolpyruvate carboxykinase from the yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/0378-1119(92)90444-topenalex-snapshot
Sequence of the phosphoenolpyruvate carboxykinase-encoding cDNA from the rumen anaerobic fungus Neocallimastix frontalis: comparison of the amino acid sequence with animals and yeast
inferredcites →https://doi.org/10.1016/0378-1119(93)90449-dopenalex-snapshot
Cloning and characterization of the gene encoding ATP-dependent phospho-enol-pyruvate carboxykinase in Trypanosoma cruzi: comparison of primary and predicted secondary structure with host GTP-dependent enzyme
inferredcites →https://doi.org/10.1016/0959-440x(92)90178-aopenalex-snapshot
Binding of nucleotides by proteins
inferredcites →https://doi.org/10.1016/0968-0004(90)90281-fopenalex-snapshot
The P-loop — a common motif in ATP- and GTP-binding proteins
inferredcites →https://doi.org/10.1016/s0021-9258(17)31219-xopenalex-snapshot
Cysteine 288: An essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP)
inferredcites →https://doi.org/10.1016/s0021-9258(17)34850-0openalex-snapshot
Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions.
inferredcites →https://doi.org/10.1016/s0021-9258(18)42965-1openalex-snapshot
The role of cations in avian liver phosphoenolpyruvate carboxykinase catalysis. Activation and regulation.
inferredcites →https://doi.org/10.1016/s0021-9258(18)53899-0openalex-snapshot
Identification of vicinal thiols of phosphoenolpyruvate carboxykinase (GTP).
inferredcites →https://doi.org/10.1016/s0021-9258(18)55350-3openalex-snapshot
Inactivation of chicken mitochondrial phosphoenolpyruvate carboxykinase by o-phthalaldehyde.
inferredcites →https://doi.org/10.1016/s0021-9258(18)94068-8openalex-snapshot
Arginine Residues at the Active Site of Avian Liver Phosphoenolpyruvate Carboxykinase
inferredcites →https://doi.org/10.1016/s0021-9258(19)39115-xopenalex-snapshot
Mitochondrial phosphoenolpyruvate carboxykinase from the chicken. Comparison of the cDNA and protein sequences with the cytosolic isozyme.
inferredcites →https://doi.org/10.1016/s0021-9258(19)39124-0openalex-snapshot
Mammalian and avian liver phosphoenolpyruvate carboxykinase. Alternate substrates and inhibition by analogues of oxaloacetate.
inferredcites →https://doi.org/10.1016/s0021-9258(19)40698-4openalex-snapshot
Decarboxylation of oxalacetate to pyruvate by purified avian liver phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1016/s0021-9258(19)47165-2openalex-snapshot
A Histidine Residue at the Active Site of Avian Liver Phosphoenolpyruvate Carboxykinase
inferredcites →https://doi.org/10.1016/s0021-9258(19)83807-3openalex-snapshot
Phosphoenolpyruvate carboxykinase. Mn2+ and Mn2+ substrate complexes.
inferredcites →https://doi.org/10.1016/s0021-9258(19)86044-1openalex-snapshot
Allosteric control by calcium and mechanism of desensitization of phosphoenolpyruvate carboxykinase of Escherichia coli.
inferredcites →https://doi.org/10.1016/s0022-2836(05)80134-2openalex-snapshot
SCOP: A structural classification of proteins database for the investigation of sequences and structures
inferredcites →https://doi.org/10.1016/s0022-2836(05)80250-5openalex-snapshot
Induced-fit movements in adenylate kinases
inferredcites →https://doi.org/10.1016/s1874-6047(08)60024-4openalex-snapshot
6 Catalytic Strategies in Enzymic Carboxylation and Decarboxylation
inferredcites →https://doi.org/10.1016/s1874-6047(08)60039-6openalex-snapshot
4 Formation of Oxalacetate by CO2 Fixation on Phosphoenolpyruvate
inferredcites →https://doi.org/10.1021/bi00100a018openalex-snapshot
An active-site lysine in avian liver phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1021/bi00132a029openalex-snapshot
Binding of carbon dioxide to phosphoenolpyruvate carboxykinase deduced from carbon kinetic isotope effects
inferredcites →https://doi.org/10.1021/bi00188a001openalex-snapshot
Structural Mechanisms for Domain Movements in Proteins
inferredcites →https://doi.org/10.1021/bi00231a006openalex-snapshot
Isotope trapping and positional isotope exchange with rat and chicken liver phosphoenolpyruvate carboxykinases
inferredcites →https://doi.org/10.1021/bi00303a030openalex-snapshot
Stereochemical course of thiophosphoryl group transfer catalyzed by mitochondrial phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1021/bi00321a036openalex-snapshot
Phosphorus-31 nuclear relaxation rate studies of the nucleotides on phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1021/bi00326a014openalex-snapshot
Proton and phosphorus-31 relaxation rate studies of the interaction of phosphoenolpyruvate and its analogs with avian phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1021/bi00367a034openalex-snapshot
Stereochemical course of thiophosphoryl transfer catalyzed by cytosolic phosphoenolpyruvate carboxykinase
inferredcites →https://doi.org/10.1021/bi00513a008openalex-snapshot
Phosphoenolpyruvate carboxykinase (guanosine 5'-triphosphate) from rat liver cytosol. Dual-cation requirement for the carboxylation reaction
inferredcites →https://doi.org/10.1021/bi00513a009openalex-snapshot
Phosphoenolpyruvate carboxykinase (guanosine 5'-triphosphate) from rat liver cytosol. Divalent cation involvement in the decarboxylation reactions
inferredcites →https://doi.org/10.1038/355318a0openalex-snapshot
The structure of the E. coli recA protein monomer and polymer
inferredcites →https://doi.org/10.1038/nsb0496-355openalex-snapshot
Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg2+–oxalate ternary complex of Escherichia coli PEP carboxykinase
inferredcites →https://doi.org/10.1073/pnas.83.20.7583openalex-snapshot
Nucleotide sequence of the mRNA encoding the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) from the chicken.
inferredcites →https://doi.org/10.1073/pnas.91.19.9151openalex-snapshot
Transgenic mice overexpressing phosphoenolpyruvate carboxykinase develop non-insulin-dependent diabetes mellitus.
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb18835.xopenalex-snapshot
The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide‐binding sites
inferredcites →https://doi.org/10.1128/jb.141.3.1115-1121.1980openalex-snapshot
Genetic and physiological characterization of Escherichia coli mutants deficient in phosphoenolpyruvate carboxykinase activity
inferredcites →https://doi.org/10.1128/jb.172.12.7151-7156.1990openalex-snapshot
Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1128/jb.177.6.1452-1460.1995openalex-snapshot
Molecular and expression analysis of the Rhizobium meliloti phosphoenolpyruvate carboxykinase (pckA) gene
inferredcites →https://doi.org/10.1128/jb.177.6.1620-1623.1995openalex-snapshot
A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity
inferredcites →https://doi.org/10.1139/o80-041openalex-snapshot
The kinetic properties of phosphoenolpyruvate carboxykinase of Escherichia coli
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Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution 1 1Edited by R. Huber
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inferred← citeshttps://doi.org/10.1007/s007260170041openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10142-023-00993-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10695-017-0431-7openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10930-006-9054-zopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10930-010-9252-6openalex-snapshot
Saccharomyces cerevisiae Phosphoenolpyruvate Carboxykinase: The Relevance of Glu299 and Leu460 for Nucleotide Binding
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The Phosphoenolpyruvate Carboxykinase of Mycobacterium Tuberculosis Induces Strong Cell-Mediated Immune Responses in Mice
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Substrate binding to fluorescent labeled wild type, Lys213Arg, and His233Gln Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases
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Nucleotide specificity of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
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Structure of a GTP-dependent Bacterial PEP-carboxykinase from Corynebacterium glutamicum
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Site-directed mutagenesis study of the microenvironment characteristics of Lys213 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
inferred← citeshttps://doi.org/10.1016/j.biochi.2008.07.002openalex-snapshot
Stereochemistry of the carboxylation reaction catalyzed by the ATP-dependent phosphoenolpyruvate carboxykinases from Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens
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Structural attributes of leishmanial phosphoenolpyruvate carboxykinase and identification of its novel inhibitors
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Molecular cloning of PEPCK and stress response of black porgy (Acanthopagrus schlegeli) to increased temperature in freshwater and seawater
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Regulation and roles of phosphoenolpyruvate carboxykinase in plants
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Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity
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Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP‐carboxykinase: expanding the P‐loop nucleotidyl transferase superfamily
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Effect of hyperosmotic shock on phosphoenolpyruvate carboxykinase gene expression and gluconeogenic activity in the crab muscle
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Plasmodium falciparum phosphoenolpyruvate carboxykinase is developmentally regulated in gametocytes☆
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Interaction of adenosine nucleotide analogs with Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
inferred← citeshttps://doi.org/10.1016/s1095-6433(02)00267-2openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/s1570-9639(02)00400-4openalex-snapshot
Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase: theoretical and experimental study of the effect of glutamic acid 284 on the protonation state of lysine 213
inferred← citeshttps://doi.org/10.1017/s0031182015001742openalex-snapshot
Biocomputational analysis of phosphoenolpyruvate carboxykinase fromRaillietina echinobothrida, a cestode parasite, and its interaction with possible modulators
inferred← citeshttps://doi.org/10.1017/s0033583599003480openalex-snapshot
Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer
inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00963openalex-snapshot
Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase
inferred← citeshttps://doi.org/10.1021/acs.jnatprod.6b00601openalex-snapshot
Insights into the Biosynthetic Origin of 3-(3-Furyl)alanine in Stachylidium sp. 293 K04 Tetrapeptides
inferred← citeshttps://doi.org/10.1021/bi100244jopenalex-snapshot
Kinetic Mechanistic Studies of Cdk5/p25-Catalyzed H1P Phosphorylation: Metal Effect and Solvent Kinetic Isotope Effect
inferred← citeshttps://doi.org/10.1021/es4019332openalex-snapshot
Metabolic and Reproductive Effects of Relatively Low Concentrations of Beclomethasone Dipropionate, a Synthetic Glucocorticoid, on Fathead Minnows
inferred← citeshttps://doi.org/10.1023/a:1020602222808openalex-snapshot
Characterization of the Oxaloacetate Decarboxylase and Pyruvate Kinase-like Activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens Phosphoenolpyruvate Carboxykinases
inferred← citeshttps://doi.org/10.1023/a:1021178432158openalex-snapshot
Evaluation by Site-Directed Mutagenesis of Active Site Amino Acid Residues of Anaerobiospirillum succiniciproducens Phosphoenolpyruvate Carboxykinase
inferred← citeshttps://doi.org/10.1023/a:1021342918955openalex-snapshot
The Effect of Active Site Mutations in the Oxaloacetate Decarboxylase and Pyruvate Kinase-Like Activities of Anaerobiospirillum succiniciproducens Phosphoenolpyruvate Carboxykinase
inferred← citeshttps://doi.org/10.1023/a:1025306105105openalex-snapshot
Thermal Stability of Phosphoenolpyruvate Carboxykinases from Escherichia coli, Trypanosoma brucei, and Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1038/nsb1297-990openalex-snapshot
Mg2+–Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions
inferred← citeshttps://doi.org/10.1042/bcj20190523openalex-snapshot
Biochemical characterization of phosphoenolpyruvate carboxykinases from Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03196.xopenalex-snapshot
Ligand interactions and protein conformational changes of phosphopyridoxyl‐labeled Escherichia coli phosphoenolpyruvate carboxykinase determined by fluorescence spectroscopy
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2003.03935.xopenalex-snapshot
Mycoplasma pneumoniae HPr kinase/phosphorylase
inferred← citeshttps://doi.org/10.1063/5.0288283openalex-snapshot
Off the beaten (catalytic) path: Charting the mechanistic space of enzyme reactions
inferred← citeshttps://doi.org/10.1073/pnas.052461499openalex-snapshot
Structure of the full-length HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 Å resolution: Mimicking the product/substrate of the phospho transfer reactions
inferred← citeshttps://doi.org/10.1073/pnas.0704422105openalex-snapshot
Detecting evolutionary relationships across existing fold space, using sequence order-independent profile–profile alignments
inferred← citeshttps://doi.org/10.1073/pnas.1000715107openalex-snapshot
Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection
inferred← citeshttps://doi.org/10.1073/pnas.192368699openalex-snapshot
X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr
inferred← citeshttps://doi.org/10.1074/jbc.m008960200openalex-snapshot
A GTP-dependent Vertebrate-type Phosphoenolpyruvate Carboxykinase from Mycobacterium smegmatis
inferred← citeshttps://doi.org/10.1074/jbc.m109527200openalex-snapshot
A New Family of Phosphotransferases with a P-loop Motif
inferred← citeshttps://doi.org/10.1074/jbc.m115.672907openalex-snapshot
Discovery of PPi-type Phosphoenolpyruvate Carboxykinase Genes in Eukaryotes and Bacteria
inferred← citeshttps://doi.org/10.1074/jbc.m411942200openalex-snapshot
Structural and Mechanistic Analysis of Sialic Acid Synthase NeuB from Neisseria meningitidis in Complex with Mn2+, Phosphoenolpyruvate, and N-Acetylmannosaminitol
inferred← citeshttps://doi.org/10.1074/jbc.m507483200openalex-snapshot
Identification and Characterization of NeuB3 from Campylobacter jejuni as a Pseudaminic Acid Synthase
inferred← citeshttps://doi.org/10.1074/jbc.m602591200openalex-snapshot
Roles of Asp75, Asp78, and Glu83 of GTP-dependent Phosphoenolpyruvate Carboxykinase from Mycobacterium smegmatis
inferred← citeshttps://doi.org/10.1074/jbc.ra119.010920openalex-snapshot
Structural comparisons of phosphoenolpyruvate carboxykinases reveal the evolutionary trajectories of these phosphodiester energy conversion enzymes
inferred← citeshttps://doi.org/10.1093/aobpla/plad053openalex-snapshot
Integrating multiple regulations on enzyme activity: the case of phosphoenolpyruvate carboxykinases
inferred← citeshttps://doi.org/10.1093/femsre/fuaa061openalex-snapshot
The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism
inferred← citeshttps://doi.org/10.1093/jxb/eraa583openalex-snapshot
Proteolytic cleavage of Arabidopsis thaliana phospho enol pyruvate carboxykinase-1 modifies its allosteric regulation
inferred← citeshttps://doi.org/10.1099/00221287-148-10-3019openalex-snapshot
Production of avirulent mutants of Mycobacterium bovis with vaccine properties by the use of illegitimate recombination and screening of stationary-phase cultures
inferred← citeshttps://doi.org/10.1107/s0907444905008723openalex-snapshot
Structure of PEP carboxykinase from the succinate-producingActinobacillus succinogenes: a new conserved active-site motif
inferred← citeshttps://doi.org/10.1107/s090744490502651xopenalex-snapshot
Structure of ATP-dependent phosphoenolpyruvate carboxykinase fromThermus thermophilusHB8 showing the structural basis of induced fit and thermostability
inferred← citeshttps://doi.org/10.1111/are.13841openalex-snapshot
Effects of dietary carbohydrate levels on growth, glucose tolerance, glucose homeostasis and GLUT4 gene expression in Tilapia nilotica
inferred← citeshttps://doi.org/10.1111/ivb.12381openalex-snapshot
Differences in the expression of soluble proteins in freshwater and brackish‐water ecotypes of the snail Theodoxus fluviatilis
inferred← citeshttps://doi.org/10.1111/j.1365-2672.2009.04631.xopenalex-snapshot
Unravelling the C 3 /C 4 carbon metabolism in Ralstonia eutropha H16
inferred← citeshttps://doi.org/10.1111/j.1550-7408.2001.tb00184.xopenalex-snapshot
Archaebacterial Relationships of the Phosphoenolpyruvate Carboxykinase Gene Reveal Mosaicism of Giardia intestinalis Core Metabolism
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2008.06702.xopenalex-snapshot
Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion–quadrupole interaction with phosphoenolpyruvate carboxylate
inferred← citeshttps://doi.org/10.1111/jpy.70069openalex-snapshot
Biochemical characterization of phosphoenolpyruvate carboxykinases from multiple species of brown algae
inferred← citeshttps://doi.org/10.1111/tpj.16215openalex-snapshot
The involvement of allosteric effectors and post‐translational modifications in the control of plant central carbon metabolism
inferred← citeshttps://doi.org/10.1128/iai.67.1.327-336.1999openalex-snapshot
Identification of Fur, Aconitase, and Other Proteins Expressed by Mycobacterium tuberculosis under Conditions of Low and High Concentrations of Iron by Combined Two-Dimensional Gel Electrophoresis and Mass Spectrometry
inferred← citeshttps://doi.org/10.1128/jb.181.9.2689-2696.1999openalex-snapshot
Molecular and Functional Characterization of the Rhodopseudomonas palustris No. 7 Phosphoenolpyruvate Carboxykinase Gene
inferred← citeshttps://doi.org/10.1128/jb.181.9.2752-2758.1999openalex-snapshot
Evidence for an Inducible Nucleotide-Dependent Acetone Carboxylase in Rhodococcus rhodochrous B276
inferred← citeshttps://doi.org/10.1128/jb.186.14.4620-4627.2004openalex-snapshot
First Characterization of an Archaeal GTP-Dependent Phosphoenolpyruvate Carboxykinase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis KOD1
inferred← citeshttps://doi.org/10.1128/jb.186.15.5129-5137.2004openalex-snapshot
The Phosphoenolpyruvate Carboxylase from Methanothermobacter thermautotrophicus Has a Novel Structure
inferred← citeshttps://doi.org/10.1128/jb.187.17.6231-6237.2005openalex-snapshot
Xanthomonas campestris pv. campestris Possesses a Single Gluconeogenic Pathway That Is Required for Virulence
inferred← citeshttps://doi.org/10.1142/s2737416526500043openalex-snapshot
Leveraging Subtractive Genomics to Combat Visceral Leishmaniasis: New Insights into Vaccine and Drug Target Identification
inferred← citeshttps://doi.org/10.1155/2014/176863openalex-snapshot
Characterization of Ten Heterotetrameric NDP-Dependent Acyl-CoA Synthetases of the Hyperthermophilic ArchaeonPyrococcus furiosus
inferred← citeshttps://doi.org/10.1177/117693430700300012openalex-snapshot
Phylogenetic Study of the Evolution of PEP-Carboxykinase
inferred← citeshttps://doi.org/10.1242/jeb.204.2.359openalex-snapshot
Hepatic Phosphoenolpyruvate Carboxykinase Gene Expression is not Repressed by Dietary Carbohydrates in Rainbow Trout (Oncorhynchus Mykiss)
inferred← citeshttps://doi.org/10.1371/journal.pcbi.1000700openalex-snapshot
Quantitative Comparison of Catalytic Mechanisms and Overall Reactions in Convergently Evolved Enzymes: Implications for Classification of Enzyme Function
inferred← citeshttps://doi.org/10.1371/journal.pone.0120682openalex-snapshot
Structural and Functional Studies of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1590/1806-9061-2019-1128openalex-snapshot
Molecular Characterization of Goose Phosphoenolpyruvate Carboxylase Kinase 1 (Pepck) Gene and Its Potential Role in Hepatic Steatosis Induced by Overfeeding
inferred← citeshttps://doi.org/10.3389/fgene.2020.00580openalex-snapshot
Screening of Potential Key Transcripts Involved in Planarian Regeneration and Analysis of Its Regeneration Patterns by PacBio Long-Read Sequencing
inferred← citeshttps://doi.org/10.3390/biology15020147openalex-snapshot
Characterization and Expression of Two Cytoplasmic Phosphoenolpyruvate Carboxykinase Genes Associated with Larval Diapause and Temperature Stress in the Wheat Blossom Midge, Sitodiplosis mosellana
inferred← citeshttps://doi.org/10.4067/s0716-97602010000200007openalex-snapshot
The Role of Tyrosine 207 in the Reaction Catalyzed by Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
inferred← citeshttps://doi.org/10.4155/fmc.11.115openalex-snapshot
Challenges and Opportunities in Developing Novel Drugs for TB
inferred← citeshttps://doi.org/10.5897/ajpp12.1432openalex-snapshot
Effect of Persian shallot (Allium hirtifolium Boiss.) extract on glucokinase (GCK), glycogen phosphorylase and phosphoenolpyruvate carboxykinase (PEPCK) genes expression in diabetic rats
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