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APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, ISSN 0175-7598, 08/2019, Volume 103, Issue 16, pp. 6571 - 6580
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2010, Volume 107, Issue 1, pp. 502 - 507
The PII protein is a signal integrator involved in the regulation of nitrogen metabolism in bacteria and plants. Upon sensing of cellular carbon and energy... 
Proteins | Enzymes | Signal transduction | Protein metabolism | Chloroplasts | Gene expression regulation | Nitrogen | Resins | Plastids | Chromatography | Arabidopsis thaliana | Biotin carboxy | PII protein organic acids fatty acid metabolism | Carrier protein | ARABIDOPSIS-THALIANA | L-GLUTAMATE KINASE | fatty acid metabolism | MULTIDISCIPLINARY SCIENCES | PUTATIVE NITROGEN SENSOR | organic acids | N-ACETYLGLUTAMATE-KINASE | SIGNAL-TRANSDUCTION PROTEIN | COMPLEX-FORMATION | PII protein | HIGHER-PLANTS | BIOSYNTHESIS | P-II | ARGININE | biotin carboxyl carrier protein | Arabidopsis Proteins - genetics | Chloroplasts - enzymology | Arabidopsis - enzymology | Arabidopsis - cytology | Molecular Sequence Data | Recombinant Fusion Proteins - metabolism | Acetyl Coenzyme A - metabolism | Acetyl-CoA Carboxylase - genetics | Protein Subunits - metabolism | Arabidopsis Proteins - metabolism | Arabidopsis Proteins - chemistry | PII Nitrogen Regulatory Proteins - metabolism | PII Nitrogen Regulatory Proteins - genetics | Recombinant Fusion Proteins - genetics | Biotin - metabolism | Protein Subunits - chemistry | Ketoglutaric Acids - metabolism | Plant Leaves - enzymology | Acetyl-CoA Carboxylase - metabolism | Plant Leaves - ultrastructure | Acetyl-CoA Carboxylase - chemistry | Protein Subunits - genetics | Physiological aspects | Cellular proteins | Biotin | Cellular signal transduction | Research | Carboxylases | Chlorophyll | Bacteria | Effects | Mass spectrometry | Adenosine triphosphatase | Index Medicus | Biological Sciences
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2018, Volume 13, Issue 6, pp. e0198414 - e0198414
Citrus canker is a disease caused by the phytopathogen Xanthomonas citri subsp. citri (Xcc), bacterium which is unable to survive out of the host for extended... 
AXONOPODIS PV. CITRI | SUBSTRATE-SPECIFICITY | GRAM-NEGATIVE BACTERIA | STREPTOMYCES-COELICOLOR A3 | PSEUDOMONAS-AERUGINOSA | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | BIOTIN-DEPENDENT ENZYMES | CARRIER PROTEIN | BIOLOGICAL-CONTROL | MOLECULAR-BASIS | Leucine - metabolism | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Substrate Specificity | Plant Diseases - microbiology | Recombinant Proteins - biosynthesis | Open Reading Frames - genetics | Protein Subunits - metabolism | Recombinant Proteins - isolation & purification | Carbon-Carbon Ligases - metabolism | Citrus - microbiology | Mutagenesis | Xanthomonas - enzymology | Bacterial Proteins - metabolism | Kinetics | Protein Stability | Carbon-Carbon Ligases - genetics | Xanthomonas - growth & development | Xanthomonas - physiology | Protein Subunits - genetics | Gene mutations | Analysis | Host-parasite relationships | Citrus canker | Genetic aspects | Research | Risk factors | Carboxylases | Dehydrogenases | Genes | Chain branching | Amino acids | Chains | Infections | Leucine | Proteins | E coli | Metabolites | Bacteria | Coenzyme A | Biocompatibility | Gram-negative bacteria | Lesions | Enzymes | Cloning | Biotin | RNA polymerase | Metabolism | Fatty acids | Plant diseases | Biofilms | Host plants | Canker | Catabolism | Fitness | Index Medicus
Journal Article
Journal Article
Journal Article
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 1384 - 13
Pyruvate carboxylase (PC) catalyzes the ATP-dependent carboxylation of pyruvate to oxaloacetate. The reaction occurs in two separate catalytic domains, coupled... 
TRANSFERASE DOMAIN | ACETYL-COA | MECHANISM | CRYOELECTRON MICROSCOPY | ASPERGILLUS-NIDULANS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | BIOTIN | FATTY-ACID SYNTHASE | RHIZOBIUM-ETLI | COENZYME-A | Allosteric Regulation | Protein Multimerization | Substrate Specificity | Crystallography, X-Ray | Protein Subunits - metabolism | Rhizobium etli - chemistry | Thermodynamics | Aspergillus nidulans - chemistry | Escherichia coli - metabolism | Protein Structure, Quaternary | Aspergillus nidulans - enzymology | Protein Interaction Domains and Motifs | Protein Subunits - genetics | Acetyl Coenzyme A - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Gene Expression | Biocatalysis | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Pyruvate Carboxylase - genetics | Recombinant Proteins - genetics | Rhizobium etli - enzymology | Pyruvate Carboxylase - metabolism | Acetyl Coenzyme A - metabolism | Pyruvate Carboxylase - chemistry | Escherichia coli - genetics | Allosteric Site | Protein Binding | Aspartic Acid - metabolism | Protein Subunits - chemistry | Aspartic Acid - chemistry | Kinetics | Translocation | Enzymes | Enzyme activity | Pyruvic acid | Pyruvate carboxylase | Carriers | Allosteric properties | Pathways | Enzymatic activity | Natural products | Carboxylation | Carboxyl group | Catalysis | Carrier mobility | Index Medicus
Journal Article
Journal Article
Journal Article
Journal Article
Journal Article
Nature, ISSN 0028-0836, 10/2015, Volume 526, Issue 7575, pp. 723 - 727
Acetyl-CoA carboxylase (ACC) has crucial roles in fatty acid metabolism and is an attractive target for drug discovery against diabetes, cancer and other... 
COENZYME | COMPLEX | FATTY-ACID SYNTHESIS | INHIBITION | PYRUVATE-CARBOXYLASE | MULTIDISCIPLINARY SCIENCES | CARBOXYLTRANSFERASE DOMAIN | BACTERIAL BIOTIN CARBOX