Sulfur
Carbon
Ubiquitin-Protein Ligases
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Sulfur Compounds
DNA Ligases
SKP Cullin F-Box Protein Ligases
Sulfur Dioxide
Carbon Dioxide
Sulfur Isotopes
Carbon Monoxide
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
Nanotubes, Carbon
Cullin Proteins
Ubiquitination
Polynucleotide Ligases
Ubiquitin
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
Mustard Gas
Severe irritant and vesicant of skin, eyes, and lungs. It may cause blindness and lethal lung edema and was formerly used as a war gas. The substance has been proposed as a cytostatic and for treatment of psoriasis. It has been listed as a known carcinogen in the Fourth Annual Report on Carcinogens (NTP-85-002, 1985) (Merck, 11th ed).
Sulfides
RING Finger Domains
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
Carbon Monoxide Poisoning
Ubiquitin-Conjugating Enzymes
Carbon Isotopes
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
RNA Ligase (ATP)
Chlorobi
Carbon Tetrachloride
F-Box Proteins
A family of proteins that share the F-BOX MOTIF and are involved in protein-protein interactions. They play an important role in process of protein ubiquition by associating with a variety of substrates and then associating into SCF UBIQUITIN LIGASE complexes. They are held in the ubiquitin-ligase complex via binding to SKP DOMAIN PROTEINS.
Amino Acid Sequence
Carbon Disulfide
Carbon Sequestration
Oxidoreductases Acting on Sulfur Group Donors
Endosomal Sorting Complexes Required for Transport
A set of protein subcomplexes involved in PROTEIN SORTING of UBIQUITINATED PROTEINS into intraluminal vesicles of MULTIVESICULAR BODIES and in membrane scission during formation of intraluminal vesicles, during the final step of CYTOKINESIS, and during the budding of enveloped viruses. The ESCRT machinery is comprised of the protein products of Class E vacuolar protein sorting genes.
Ubiquitins
Sulfur Hexafluoride
Oxidation-Reduction
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Chromatiaceae
Proteasome Endopeptidase Complex
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
Chemical Warfare Agents
Substrate Specificity
Peptide Synthases
Nitrogen
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Protein Binding
Ubiquitin-Protein Ligase Complexes
Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).
Polyubiquitin
An oligomer formed from the repetitive linking of the C-terminal glycine of one UBIQUITIN molecule via an isopeptide bond to a lysine residue on a second ubiquitin molecule. It is structurally distinct from UBIQUITIN C, which is a single protein containing a tandemly arrayed ubiquitin peptide sequence.
Ubiquitin-Activating Enzymes
Mutation
Carbon-Oxygen Ligases
Chlorobium
Hydrogen Sulfide
Proto-Oncogene Proteins c-cbl
Atmosphere
Sequence Homology, Amino Acid
Catalysis
Chromatium
Proteolysis
Models, Molecular
S-Phase Kinase-Associated Proteins
A family of structurally-related proteins that were originally identified by their ability to complex with cyclin proteins (CYCLINS). They share a common domain that binds specifically to F-BOX MOTIFS. They take part in SKP CULLIN F-BOX PROTEIN LIGASES, where they can bind to a variety of F-BOX PROTEINS.
Protein Inhibitors of Activated STAT
Acidithiobacillus
Air Pollutants
Sulfonium Compounds
SUMO-1 Protein
Bacteria
One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive.
Saccharomyces cerevisiae
Small Ubiquitin-Related Modifier Proteins
Sulfur-Reducing Bacteria
Culture Media
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
Models, Biological
Geologic Sediments
A mass of organic or inorganic solid fragmented material, or the solid fragment itself, that comes from the weathering of rock and is carried by, suspended in, or dropped by air, water, or ice. It refers also to a mass that is accumulated by any other natural agent and that forms in layers on the earth's surface, such as sand, gravel, silt, mud, fill, or loess. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1689)
Saccharomyces cerevisiae Proteins
Carbon Footprint
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Biodegradation, Environmental
Cysteine Synthase
Anaerobiosis
Iron-Sulfur Proteins
Binding Sites
Autotrophic Processes
The processes by which organisms use simple inorganic substances such as gaseous or dissolved carbon dioxide and inorganic nitrogen as nutrient sources. Contrasts with heterotrophic processes which make use of organic materials as the nutrient supply source. Autotrophs can be either chemoautotrophs (or chemolithotrophs), largely ARCHAEA and BACTERIA, which also use simple inorganic substances for their metabolic energy reguirements; or photoautotrophs (or photolithotrophs), such as PLANTS and CYANOBACTERIA, which derive their energy from light. Depending on environmental conditions some organisms can switch between different nutritional modes (autotrophy; HETEROTROPHY; chemotrophy; or PHOTOTROPHY) to utilize different sources to meet their nutrient and energy requirements.
Carrier Proteins
Biomass
Carbon Radioisotopes
RNA, Ribosomal, 16S
Carbon Compounds, Inorganic
Sumoylation
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Amino Acid Motifs
Thiobacillus
Hydrogensulfite Reductase
Epsilonproteobacteria
Hydrogen-Ion Concentration
Adenosine Monophosphate
Photosynthesis
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
Phototrophic Processes
Processes by which phototrophic organisms use sunlight as their primary energy source. Contrasts with chemotrophic processes which do not depend on light and function in deriving energy from exogenous chemical sources. Photoautotrophy (or photolithotrophy) is the ability to use sunlight as energy to fix inorganic nutrients to be used for other organic requirements. Photoautotrophs include all GREEN PLANTS; GREEN ALGAE; CYANOBACTERIA; and green and PURPLE SULFUR BACTERIA. Photoheterotrophs or photoorganotrophs require a supply of organic nutrients for their organic requirements but use sunlight as their primary energy source; examples include certain PURPLE NONSULFUR BACTERIA. Depending on environmental conditions some organisms can switch between different nutritional modes (AUTOTROPHY; HETEROTROPHY; chemotrophy; or phototrophy) to utilize different sources to meet their nutrients and energy requirements.
Gammaproteobacteria
Thiosulfate Sulfurtransferase
Temperature
Base Sequence
Crystallography, X-Ray
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Air Pollution
Sulfur Group Transferases
Thiotrichaceae
Arabidopsis Proteins
Sequence Analysis, DNA
Hydrogen
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
Arabidopsis
Multiprotein Complexes
Cloning, Molecular
Biocatalysis
Acetates
Cystathionine gamma-Lyase
Water Microbiology
Oxygen
Muscular Atrophy
Metabolic Networks and Pathways
Cystine
Signal Transduction
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Iron
DNA, Ribosomal
Cell Cycle Proteins
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Multienzyme Complexes
Soot
A dark powdery deposit of unburned fuel residues, composed mainly of amorphous CARBON and some HYDROCARBONS, that accumulates in chimneys, automobile mufflers and other surfaces exposed to smoke. It is the product of incomplete combustion of carbon-rich organic fuels in low oxygen conditions. It is sometimes called lampblack or carbon black and is used in INK, in rubber tires, and to prepare CARBON NANOTUBES.
Sulfate Adenylyltransferase
Gene Expression Regulation, Plant
Methane
Molybdenum
Lyases
Amino Acids
Soil
Volcanic Eruptions
The ash, dust, gases, and lava released by volcanic explosion. The gases are volatile matter composed principally of about 90% water vapor, and carbon dioxide, sulfur dioxide, hydrogen, carbon monoxide, and nitrogen. The ash or dust is pyroclastic ejecta and lava is molten extrusive material consisting mainly of magnesium silicate. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Acidianus
A genus of facultatively anaerobic coccoid ARCHAEA, in the family SULFOLOBACEAE. Cells are highly irregular in shape and thermoacidophilic. Lithotrophic growth occurs aerobically via sulfur oxidation in some species. Distribution includes solfataric springs and fields, mudholes, and geothermically heated acidic marine environments.
Models, Chemical
DNA-Binding Proteins
Archaea
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Magnetic Resonance Spectroscopy
Receptors, Autocrine Motility Factor
Nitrogen Dioxide
Nitrogen oxide (NO2). A highly poisonous gas. Exposure produces inflammation of lungs that may only cause slight pain or pass unnoticed, but resulting edema several days later may cause death. (From Merck, 11th ed) It is a major atmospheric pollutant that is able to absorb UV light that does not reach the earth's surface.
Anaphase-Promoting Complex-Cyclosome
An E3 ubiquitin ligase primarily involved in regulation of the metaphase-to-anaphase transition during MITOSIS through ubiquitination of specific CELL CYCLE PROTEINS. Enzyme activity is tightly regulated through subunits and cofactors, which modulate activation, inhibition, and substrate specificity. The anaphase-promoting complex, or APC-C, is also involved in tissue differentiation in the PLACENTA, CRYSTALLINE LENS, and SKELETAL MUSCLE, and in regulation of postmitotic NEURONAL PLASTICITY and excitability.
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Molecular Structure
Carbohydrate Metabolism
Gene Expression Regulation, Bacterial
Catalytic Domain
HeLa Cells
HEK293 Cells
Gases
The vapor state of matter; nonelastic fluids in which the molecules are in free movement and their mean positions far apart. Gases tend to expand indefinitely, to diffuse and mix readily with other gases, to have definite relations of volume, temperature, and pressure, and to condense or liquefy at low temperatures or under sufficient pressure. (Grant & Hackh's Chemical Dictionary, 5th ed)
Oceans and Seas
Ecosystem
Protein Processing, Post-Translational
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
Sulfuric Acids
Repressor Proteins
Arylsulfatases
Transcription Factors
Environmental Monitoring
Spectrum Analysis
Two-Hybrid System Techniques
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Soil Microbiology
Glucose
Phenotype
Acidithiobacillus thiooxidans
Glutathione
Pseudomonas
Peptide Hydrolases
Heterotrophic Processes
The processes by which organisms utilize organic substances as their nutrient sources. Contrasts with AUTOTROPHIC PROCESSES which make use of simple inorganic substances as the nutrient supply source. Heterotrophs can be either chemoheterotrophs (or chemoorganotrophs) which also require organic substances such as glucose for their primary metabolic energy requirements, or photoheterotrophs (or photoorganotrophs) which derive their primary energy requirements from light. Depending on environmental conditions some organisms can switch between different nutritional modes (AUTOTROPHY; heterotrophy; chemotrophy; or PHOTOTROPHY) to utilize different sources to meet their nutrients and energy requirements.
Chemoautotrophic Growth
Growth of organisms using AUTOTROPHIC PROCESSES for obtaining nutrients and chemotrophic processes for obtaining a primary energy supply. Chemotrophic processes are involved in deriving a primary energy supply from exogenous chemical sources. Chemotrophic autotrophs (chemoautotrophs) generally use inorganic chemicals as energy sources and as such are called chemolithoautotrophs. Most chemoautotrophs live in hostile environments, such as deep sea vents. They are mostly BACTERIA and ARCHAEA, and are the primary producers for those ecosystems.
Trees
Ubiquitin-Specific Proteases
Nuclear Proteins
Structure-Activity Relationship
Sulfur Radioisotopes
Adenosine Triphosphate
Mass Spectrometry
Metalloproteins
Plants
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Tetrathionic Acid
Expression, purification, and characterization of the Mycobacterium tuberculosis acyl carrier protein, AcpM. (1/22)
Mycolic acids are generated in Mycobacterium tuberculosis as a result of the interaction of two fatty acid biosynthetic systems: the multifunctional polypeptide, FASI, in which the acyl carrier protein (ACP) domain forms an integral part of the polypeptide, and the dissociated FASII system, which is composed of monofunctional enzymes and a discrete ACP (AcpM). In order to characterize enzymes of the FASII system, large amounts of AcpM are required to generate substrates such as holo-AcpM, malonyl-AcpM and acyl-AcpM. The M. tuberculosis acpM gene was overexpressed in Escherichia coli and AcpM purified, yielding approximately 15-20 mg/l of culture. Analysis of AcpM by mass spectrometry, N-terminal sequencing, amino acid analysis, and gas chromatography indicated the presence of three species, apo-, holo-, and acyl-AcpM, the former comprising up to 65% of the total pool. The apo-AcpM was purified away from the in vivo generated holo- and acyl-forms, which were inseparable and heterogeneous with respect to acyl chain lengths. Once purified, we were able to convert apo-AcpM into holo- and acyl-forms. These procedures provide the means for the preparation of the large quantities of AcpM and derivatives needed for characterization of the purified enzymes of the mycobacterial FASII system. (+info)Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. (2/22)
Acyl carrier protein (ACP) interacts with many different enzymes during the synthesis of fatty acids, phospholipids, and other specialized products in bacteria. To examine the structural and functional roles of amino acids previously implicated in interactions between the ACP polypeptide and fatty acids attached to the phosphopantetheine prosthetic group, recombinant Vibrio harveyi ACP and mutant derivatives of conserved residues Phe-50, Ile-54, Ala-59, and Tyr-71 were prepared from glutathione S-transferase fusion proteins. Circular dichroism revealed that, unlike Escherichia coli ACP, V. harveyi-derived ACPs are unfolded at neutral pH in the absence of divalent cations; all except F50A and I54A recovered native conformation upon addition of MgCl(2). Mutant I54A was not processed to the holo form by ACP synthase. Some mutations significantly decreased catalytic efficiency of ACP fatty acylation by V. harveyi acyl-ACP synthetase relative to recombinant ACP, e.g. F50A (4%), I54L (20%), and I54V (31%), whereas others (V12G, Y71A, and A59G) had less effect. By contrast, all myristoylated ACPs examined were effective substrates for the luminescence-specific V. harveyi myristoyl-ACP thioesterase. Conformationally sensitive gel electrophoresis at pH 9 indicated that fatty acid attachment stabilizes mutant ACPs in a chain length-dependent manner, although stabilization was decreased for mutants F50A and A59G. Our results indicate that (i) residues Ile-54 and Phe-50 are important in maintaining native ACP conformation, (ii) residue Ala-59 may be directly involved in stabilization of ACP structure by acyl chain binding, and (iii) acyl-ACP synthetase requires native ACP conformation and involves interaction with fatty acid binding pocket residues, whereas myristoyl-ACP thioesterase is insensitive to acyl donor structure. (+info)Purification and characterization of acyl-acyl carrier protein synthetase from oleaginous yeast and its role in triacylglycerol biosynthesis. (3/22)
Fatty acids are activated in an ATP-dependent manner before they are utilized. We describe here how the 10 S triacylglycerol biosynthetic multienzyme complex from Rhodotorula glutinis is capable of activating non-esterified fatty acids for the synthesis of triacylglycerol. The photolabelling of the complex with [(32)P]azido-ATP showed labelling of a 35 kDa polypeptide. The labelled polypeptide was identified as acyl-acyl carrier protein (ACP) synthetase, which catalyses the ATP-dependent ligation of fatty acid with ACP to form acyl-ACP. The enzyme was purified by successive PAGE separations to apparent homogeneity from the soluble fraction of oleaginous yeast and its apparent molecular mass was 35 kDa under denaturing and reducing conditions. Acyl-ACP synthetase was specific for ATP. The K(m) values for palmitic, stearic, oleic and linoleic acids were found to be 42.9, 30.4, 25.1 and 22.7 microM, respectively. The antibodies to acyl-ACP synthetase cross-reacted with Escherichia coli acyl-ACP synthetase. Anti-ACP antibodies showed no cross-reactivity with the purified acyl-ACP synthetase, indicating no bound ACP with the enzyme. Immunoprecipitations with antibodies to acyl-ACP synthetase revealed that this enzyme is a part of the 10 S triacylglycerol biosynthetic complex. These results demonstrate that the soluble acyl-ACP synthetase plays a novel role in activating fatty acids for triacylglycerol biosynthesis in oleaginous yeast. (+info)A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. (4/22)
The formation of S-hydroxymethylglutathione from formaldehyde and glutathione is a central reaction in the consumption of the cytotoxin formaldehyde in some methylotrophic bacteria as well as in many other organisms. We describe here the discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction. The rates of S-hydroxymethylglutathione formation and cleavage were determined under equilibrium conditions via two-dimensional proton exchange NMR spectroscopy. The pseudo first order rate constants k(1)* were estimated from the temperature dependence of the reaction and the signal to noise ratio of the uncatalyzed reaction. At 303 K and pH 6.0 k(1)* was found to be 0.02 s(-1) for the spontaneous reaction. A 10-fold increase of the rate constant was observed upon addition of cell extract from P. denitrificans grown in the presence of methanol corresponding to a specific activity of 35 units mg(-1). Extracts of cells grown in the presence of succinate revealed a lower specific activity of 11 units mg(-1). The enzyme catalyzing the conversion of formaldehyde and glutathione was purified and named glutathione-dependent formaldehyde-activating enzyme (Gfa). The gene gfa is located directly upstream of the gene for glutathione-dependent formaldehyde dehydrogenase, which catalyzes the subsequent oxidation of S-hydroxymethylglutathione. Putative proteins with sequence identity to Gfa from P. denitrificans are present also in Rhodobacter sphaeroides, Sinorhizobium meliloti, and Mesorhizobium loti. (+info)Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. (5/22)
Fatty acyl-CoA synthetase (FACS, fatty acid:CoA ligase, AMP forming; EC ) plays a central role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA. In Escherichia coli this enzyme, encoded by the fadD gene, is required for the coupled import and activation of exogenous long-chain fatty acids. The E. coli FACS (FadD) contains two sequence elements, which comprise the ATP/AMP signature motif ((213)YTGGTTGVAKGA(224) and (356)GYGLTE(361)) placing it in the superfamily of adenylate-forming enzymes. A series of site-directed mutations were generated in the fadD gene within the ATP/AMP signature motif site to evaluate the role of this conserved region to enzyme function and to fatty acid transport. This approach revealed two major classes of fadD mutants with depressed enzyme activity: 1) those with 25-45% wild type activity (fadD(G216A), fadD(T217A), fadD(G219A), and fadD(K222A)) and 2) those with 10% or less wild-type activity (fadD(Y213A), fadD(T214A), and fadD(E361A)). Using anti-FadD sera, Western blots demonstrated the different mutant forms of FadD that were present and had localization patterns equivalent to the wild type. The defect in the first class was attributed to a reduced catalytic efficiency although several mutant forms also had a reduced affinity for ATP. The mutations resulting in these biochemical phenotypes reduced or essentially eliminated the transport of exogenous long-chain fatty acids. These data support the hypothesis that the FACS FadD functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters. (+info)Isolation and expression pattern of two putative acyl-ACP desaturase cDNAs from Bassia scoparia. (6/22)
The seed lipids of some higher plants contain unusual fatty acids with potentially valuable non-food uses. Seeds of Bassia scoparia contain one such monounsaturated fatty acid, 16:1Delta5. This fatty acid can be used for the production of an insect oviposition pheromone, which is potentially valuable in the control of the mosquito Culex quinquefasciatus, a vector of West Nile virus. Previous work has established that a number of unusual monounsaturated fatty acids are produced by variant forms of the ubiquitous acyl-ACP desaturases. The isolation and initial characterization of two putative acyl-ACP desaturases from B. scoparia, one of which is seed-specific, suggests that such a variant enzyme occurs in this species. (+info)A dynamic zinc redox switch. (7/22)
The crystal structures of glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans, which catalyzes the formation of S-hydroxymethylglutathione from formaldehyde and glutathione, and its complex with glutathione (Gfa-GTT) have been determined. Gfa has a new fold with two zinc-sulfur centers, one that is structural (zinc tetracoordinated) and one catalytic (zinc apparently tricoordinated). In Gfa-GTT, the catalytic zinc is displaced due to disulfide bond formation of glutathione with one of the zinc-coordinating cysteines. Soaking crystals of Gfa-GTT with formaldehyde restores the holoenzyme. Accordingly, the displaced zinc forms a complex by scavenging formaldehyde and glutathione. The activation of formaldehyde and of glutathione in this zinc complex favors the final nucleophilic addition, followed by relocation of zinc in the catalytic site. Therefore, the structures of Gfa and Gfa-GTT draw the critical association between a dynamic zinc redox switch and a nucleophilic addition as a new facet of the redox activity of zinc-sulfur sites. (+info)Lysophospholipid flipping across the Escherichia coli inner membrane catalyzed by a transporter (LplT) belonging to the major facilitator superfamily. (8/22)
The transfer of phospholipids across membrane bilayers is protein-mediated, and most of the established transporters catalyze the energy-dependent efflux of phospholipids from cells. This work identifies and characterizes a lysophospholipid transporter gene (lplT, formally ygeD) in Escherichia coli that is an integral component in the 2-acylglycerophosphoethanolamine (2-acyl-GPE) metabolic cycle for membrane protein acylation. The lplT gene is adjacent to and in the same operon as the aas gene, which encodes the bifunctional enzyme 2-acyl-GPE acyltransferase/acyl-acyl carrier protein synthetase. In some bacteria, acyltransferase/acyl-ACP synthetase (Aas) and LplT homologues are fused in a single polypeptide chain. 2-Acyl-GPE transport to the inside of the cell was assessed by measuring the Aas-dependent formation of phosphatidylethanolamine. The Aas-dependent incorporation of [3H]palmitate into phosphatidylethanolamine was significantly diminished in deltalplT mutants, and the LplT-Aas transport/acylation activity was independent of the proton motive force. The deltalplT mutants accumulated acyl-GPE in vivo and had a diminished capacity to transport exogenous 2-acylglycerophosphocholine into the cell. Spheroplasts prepared from wild-type E. coli transported and acylated fluorescent 2-acyl-GPE with an apparent K(d) of 7.5 microM, whereas this high-affinity process was absent in deltalplT mutants. Thus, LplT catalyzes the transbilayer movement of lysophospholipids and is the first example of a phospholipid flippase that belongs to the major facilitator superfamily. (+info)KEGG PATHWAY: zga00564
KEGG PATHWAY: hsa00564
TIGR02820
SMART: Pfam domain CTP transf like
aas - Bifunctional protein Aas - Escherichia coli O157:H7 - aas gene & protein
Publication - Targeted disruption of the MHC class II Aa gene in C57BL/6 mice.
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biotin-CoA ligase(EC 6.2.1.11) - Creative Enzymes
GFAのインタラクティブな可視化ツール GfaViz - macでインフォマティクス
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Accumulation of palmitate in arabidopsis mediated by the acyl-acyl carrier protein thioesterase FATB1 :: MPG.PuRe
cry6Aa - Pesticidal crystal protein Cry6Aa - Bacillus thuringiensis - cry6Aa gene & protein
Cyclic AMP and Acyl Homoserine Lactones Increase the Cultivation Efficiency of Heterotrophic Bacteria from the Central Baltic...
IJPBS Article- EVALUATION OF THE POTENTIAL OF FIVE MEDICINAL PLANTS TO INHIBIT ACYL HOMOSERINE LACTONE BASED QUORUM
Nutrition News
Isolation of a cDNA clone encoding an acyl-acyl carrier protein thioesterase from the mesocarp of oil palm (<i>Elaeis...
ACPM 2014 - Eventegg.com
Anti-ATP citrate lyase 抗体 (ab117239) | アブカム
Oxtet 00160 : CDS information --- DoBISCUIT
Home | Blackwell Lab
Publications | Yandeau-Nelson Team
Maduro didnt pull any punches - France 24
Brexit - what happens next? - France 24
EC 3.1.2.14
ASMscience | 26 Multispecies Interact
Palmitoyl-acyl carrier protein (ACP) thioesterase and the evolutionary origin of plant acyl-ACP thioesterases. | Plant Cell
Steps toward a unified wound theory
Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic...
Team:BIOTEC Dresden/Literature - 2010.igem.org
Ramberg-Bäcklund reaction - Wikipedia
ACPM News - American College of Preventive Medicine
ACPM News August 2016 - American College of Preventive Medicine
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GFA League 2017/2018 Wyniki na żywo, Piłka nożna Gambia
Isolation of mutants of Acinetobacter calcoaceticus deficient in wax ester synthesis and complementation of one mutation with a...
Axxera ACPM6628BT Double-DIN Digital Media Receiver - PASMAG is the Tuners Source for Modified Car Culture since 1999
ACPM - ESG implementation: navigating the evolution of your practice
R)-3-Nitrobifenilin - Wikipedia
Phenylacetate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). This ... In enzymology, a phenylacetate-CoA ligase is an enzyme (EC 6.2.1.30) that catalyzes the chemical reaction ATP + phenylacetate ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...
Phytanate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... This enzyme is also called phytanoyl-CoA ligase. Muralidharan FN, Muralidharan VB (1986). "Phytanoyl-CoA ligase activity in rat ... In enzymology, a phytanate-CoA ligase (EC 6.2.1.24) is an enzyme that catalyzes the chemical reaction ATP + phytanate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Acid-CoA ligase (GDP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acid-CoA ligase (GDP-forming) (EC 6.2.1.10) is an enzyme that catalyzes the chemical reaction GTP + an acid ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase ( ...
Butyrate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme ... Butyrate-CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme (EC 6.2.1.2) that ... 3-hydroxybutyryl CoA ligase, xenobiotic/medium-chain fatty acid ligase, and short-chain acyl-CoA synthetase. ACSM1 ACSM2A ... This reaction is catalyzed by the HXM-A and HXM-B medium-chain acid:CoA ligases and requires energy in the form of ATP. ... The ...
6-carboxyhexanoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 6-carboxyhexanoate-CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction ATP + 6- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6- ...
Succinate-CoA ligase (ADP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (ADP-forming). Other names in common use include succinyl-CoA ...
Anthranilate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 2-aminobenzoate-CoA ligase, 2-aminobenzoate-coenzyme A ligase, and 2-aminobenzoate coenzyme A ligase. This enzyme participates ... In enzymology, an anthranilate-CoA ligase (EC 6.2.1.32) is an enzyme that catalyzes the chemical reaction ATP + anthranilate + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, Anthranilates, All stub articles, Ligase stubs). ...
Citrate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a citrate-CoA ligase (EC 6.2.1.18) is an enzyme that catalyzes the chemical reaction ATP + citrate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle. Lill U, Schreil A, Eggerer H (1982). " ...
3-alpha,7-alpha-dihydroxy-5-beta-cholestanate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid ... In enzymology, a 3α,7α-dihydroxy-5β-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical reaction ATP ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997-1004. PMID ...
Acetate-CoA ligase (ADP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ...
Propionate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a propionate-CoA ligase (EC 6.2.1.17) is an enzyme that catalyzes the chemical reaction ATP + propanoate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA ...
Trans-feruloyl-CoA synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP-hydrolysing). This enzyme is also called trans- ...
4-chlorobenzoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 4-chlorobenzoate-CoA ligase (EC 6.2.1.33) is an enzyme that catalyzes the chemical reaction 4-chlorobenzoate ... Loffler F, Muller R, Lingens F (1992). "Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. ... systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate ...
4-hydroxybenzoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 4-hydroxybenzoate-coenzyme A ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A synthetase, and 4-hydroxybenzoyl-CoA ligase. ... In enzymology, a 4-hydroxybenzoate-CoA ligase (EC 6.2.1.27) is an enzyme that catalyzes the chemical reaction ATP + 4- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Succinate-CoA ligase (GDP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) is an enzyme that catalyzes the chemical reaction GTP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (GDP-forming). Other names in common use include succinyl-CoA ...
Glutarate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a glutarate-CoA ligase (EC 6.2.1.6) is an enzyme that catalyzes the chemical reaction ATP + glutarate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA ...
Malate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is malate:CoA ligase (ADP-forming). Other names in common use include malyl-CoA synthetase ...
Dicarboxylate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a dicarboxylate-CoA ligase (EC 6.2.1.23) is an enzyme that catalyzes the chemical reaction ATP + an alphaomega- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include ...
Long-chain-fatty-acid-luciferin-component ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-luciferin-component ligase (EC 6.2.1.19) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl- ...
Long-chain-fatty-acid-(acyl-carrier-protein) ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-[acyl-carrier-protein] ligase (EC 6.2.1.20) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in ...
citrate (pro-3S)-lyase) ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... HS-citrate lyase ligase, and acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming). This enzyme participates in two- ... In enzymology, a [citrate (pro-3S)-lyase] ligase (EC 6.2.1.22) is an enzyme that catalyzes the chemical reaction ATP + acetate ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Oxalate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an oxalate-CoA ligase (EC 6.2.1.8) is an enzyme that catalyzes the chemical reaction ATP + oxalate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... Organisms with Oxalate-CoA Ligases include: Arabidopsis thaliana Saccharomyces cerevisiae "Validate User". Foster J, Nakata PA ...
Arachidonate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an arachidonate-CoA ligase (EC 6.2.1.15) is an enzyme that catalyzes the chemical reaction ATP + arachidonate + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is arachidonate:CoA ligase (AMP-forming). This enzyme is also called arachidonoyl-CoA ...
Benzoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a benzoate-CoA ligase (EC 6.2.1.25) is an enzyme that catalyzes the chemical reaction ATP + benzoate + CoA ⇌ {\ ... Other names in common use include benzoate-coenzyme A ligase, benzoyl-coenzyme A synthetase, and benzoyl CoA synthetase (AMP ... systematic name of this enzyme class is benzoate:CoA ligase (AMP-forming). ...
Acetoacetate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acetoacetate-CoA ligase (EC 6.2.1.16) is an enzyme that catalyzes the chemical reaction ATP + acetoacetate + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acetoacetate:CoA ligase (AMP-forming). This enzyme is also called acetoacetyl-CoA ...
2-furoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 2-furoate-CoA ligase (EC 6.2.1.31) is an enzyme that catalyzes the chemical reaction ATP + 2-furoate + CoA ... systematic name of this enzyme class is 2-furoate:CoA ligase (AMP-forming). This enzyme is also called 2-furoyl coenzyme A ...
Biotin-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a biotin-CoA ligase (EC 6.2.1.11) is an enzyme that catalyzes the chemical reaction ATP + biotin + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is biotin:CoA ligase (AMP-forming). Other names in common use include biotinyl-CoA ...
4-Coumarate-CoA ligase
This enzyme belongs to the family of ligases, to be specific those forming carbon-sulfur bonds as acid-thiol ligases. The ... p-coumaroyl CoA ligase, p-coumaryl coenzyme A synthetase, p-coumaryl-CoA synthetase, p-coumaryl-CoA ligase, feruloyl CoA ligase ... CoA ligase, p-coumaryl-CoA ligase, p-hydroxycinnamic acid:CoA ligase, and 4CL. This enzyme participates in phenylpropanoid ... In enzymology, a 4-coumarate-CoA ligase (EC 6.2.1.12) is an enzyme that catalyzes the chemical reaction ATP + 4-coumarate + CoA ...
Ligase
... ligases used to form carbon-oxygen bonds EC 6.2 includes ligases used to form carbon-sulfur bonds EC 6.3 includes ligases used ... ligases used to form carbon-carbon bonds EC 6.5 includes ligases used to form phosphoric ester bonds EC 6.6 includes ligases ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... Ligases are classified as EC 6 in the EC number classification of enzymes. Ligases can be further classified into six ...
Aquifex aeolicus
Metabolism As an autotroph, "A. aeolicus" has the ability to obtain all necessary carbon by fixing CO2 from the environment and ... "A. aeolicus" can also reduce nitrogen and sulfur. Regarding its growth under microaerophilic conditions, Aquifex species have ... succinate-CoA ligase, aconitase and citratesynthase. Moreover, this bacterium uses oxygen, hydrogen, and mineral salts as its ...
Oxalyl-CoA decarboxylase
A key feature of the cofactor TPP is the relatively acidic proton bound to the carbon atom between the nitrogen and sulfur in ... Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz AL, Allison MJ (July 1990). "Purification and ... which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). ... This carbon center ionizes to form a carbanion, which adds to the carbonyl group of oxalyl-CoA. This addition is followed by ...
Glutathione synthetase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... Glutathione synthetase deficiency Glutathione Liver Sulfur Metabolism Gogos A, Shapiro L (Dec 2002). "Large conformational ... "Synthases and Ligases". IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN), and Nomenclature Commission of IUB (NC- ... Li H, Xu H, Graham DE, White RH (Aug 2003). "Glutathione synthetase homologs encode alpha-L-glutamate ligases for methanogenic ...
Butyric acid
Two molecules of carbon dioxide (CO2) and two molecules of hydrogen (H2) are formed as waste products. Subsequently, ATP is ... They are often found in the soluble fibers of foods which are high in sulfur, such as the allium and cruciferous vegetables. ... also known as butyrate-CoA ligase. The metabolite produced by this reaction is butyryl-CoA, and is produced as follows: ... Butyric acid is metabolized by various human XM-ligases (ACSM1, ACSM2B, ASCM3, ACSM4, ACSM5, and ACSM6), ...
Hypothetical types of biochemistry
The biological use of sulfur as an alternative to carbon is purely hypothetical, especially because sulfur usually forms only ... Kovac, Andreja (1 Apr 2007). "Diazenedicarboxamides as inhibitors of D-alanine-D-alanine ligase (Ddl)". Bioorganic & Medicinal ... Sulfur-reducing bacteria can utilize elemental sulfur instead of oxygen, reducing sulfur to hydrogen sulfide.) Arsenic, which ... Hydrogen sulfide life might use a mixture of carbon monoxide and carbon dioxide as their carbon source. They might produce and ...
List of enzymes
Carbon disulfide hydrolase EC 3.13.1.6: (CysO sulfur-carrier protein)-S-L-cysteine hydrolase EC 3.13.1.7: Carbonyl sulfide ... Glutarate-CoA ligase EC 6.2.1.7: Cholate-CoA ligase EC 6.2.1.8: Oxalate-CoA ligase EC 6.2.1.9: Malate-CoA ligase EC 6.2.1.10: ... ligase EC 6.2.1.23: Dicarboxylate-CoA ligase EC 6.2.1.24: Phytanate-CoA ligase EC 6.2.1.25: Benzoate-CoA ligase EC 6.2.1.26: o- ... Arachidonate-CoA ligase EC 6.2.1.16: Acetoacetate-CoA ligase EC 6.2.1.17: Propionate-CoA ligase EC 6.2.1.18: Citrate-CoA ligase ...
Lipoic acid
LA contains two sulfur atoms (at C6 and C8) connected by a disulfide bond and is thus considered to be oxidized although either ... sulfur atom can exist in higher oxidation states. The carbon atom at C6 is chiral and the molecule exists as two enantiomers (R ... The ligase activity of this enzyme requires ATP. Along with sodium and the vitamins biotin (B7) and pantothenic acid (B5), ... Free lipoate can be used by some organisms as an enzyme called lipoate protein ligase that attaches it covalently to the ...
Phycodnaviridae
Thus, coccoliths have significant roles in global carbon fixation and the carbon cycle as well as sulfur cycling. Over time, ... Ho, C. K.; Van Etten, J. L.; Shuman, S. (1997). "Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus ... PCR amplification reveals random A/T overhangs, detection of DNA ligases and endonucleases hinting that a linear genome may be ... PBCV-1 also encodes other proteins involved in DNA replication including an ATP-dependent DNA ligase, a type II DNA ...
Biology
... carbon can form very long chains of interconnecting carbon-carbon bonds such as octane or ring-like structures such as glucose ... A hydrocarbon backbone can be substituted by other elements such as oxygen (O), hydrogen (H), phosphorus (P), and sulfur (S), ... the fragments using gel electrophoresis and then later recombine the fragments into a novel DNA sequence using DNA ligase. The ... Systemic tissues take up oxygen but adds carbon dioxide to the blood whereas a breathing organs takes up carbon dioxide but add ...
Zinc
Pyrometallurgy reduces zinc oxide with carbon or carbon monoxide at 950 °C (1,740 °F) into the metal, which is distilled as ... Zinc is a chalcophile, meaning the element is more likely to be found in minerals together with sulfur and other heavy ... ligases, transferases, oxidoreductases, and isomerases (42,43). Bitanihirwe BK, Cunningham MG (November 2009). "Zinc: the ... A coordinate covalent bond is formed between the terminal peptide and a C=O group attached to zinc, which gives the carbon a ...
CO-methylating acetyl-CoA synthase
Together with Carbon monoxide dehydrogenase (CODH), it forms the bifunctional enzyme Acetyl-CoA Synthase/Carbon Monoxide ... Acetyl-CoA synthase (ACS), not to be confused with Acetyl-CoA synthetase or Acetate-CoA ligase (ADP forming), is a nickel- ... Nip is in a T-shaped environment bound to three sulfur atoms, with an unknown ligand possibly creating a distorted tetrahedral ... The first pathway involves CODH converting carbon dioxide into carbon monoxide through a two-electron transfer, and the second ...
List of MeSH codes (D08)
... carbon-carbon double bond isomerases MeSH D08.811.399.475.400.700 - steroid isomerases MeSH D08.811.399.475.800 - sulfur-sulfur ... valine-tRNA ligase MeSH D08.811.464.267.500 - coenzyme a ligases MeSH D08.811.464.267.500.200 - acetate-coa ligase MeSH D08.811 ... 500.600 - succinate-coa ligases MeSH D08.811.464.754.600 - dna ligases MeSH D08.811.464.754.720 - rna ligase (atp) MeSH D08.811 ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ...
Radical SAM
... enzymes that can catalyze sulfur-to-alpha carbon thioether cross-linked peptides (sactipeptides) are important to ... For example, a ligase combines two molecules to form a new bond. Representative enzymes will be mentioned for each class. ... "The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon ... The active site of Mo nitrogenase is the M-cluster, a metal-sulfur cluster containing a carbide at its core. Within the ...
KEGG T01001: 55902
DeCS
Carbono-Enxofre Ligases Descriptor French: Carbon-sulfur ligases Entry term(s):. Carbon Sulfur Ligases. Ligases, Carbon-Sulfur ... Carbon-Sulfur Ligases - Preferred Concept UI. M0029292. Scope note. Enzymes that catalyze the joining of two molecules by the ... Carbon-Sulfur Ligases Entry term(s). Carbon Sulfur Ligases Ligases, Carbon-Sulfur ... Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. EC 6.2.. ...
AGT26296 details
lcl|LHPG02000023.1 cds PRW20584.1 5407 details
Gb 31560 details
6.2.1.13: acetate-CoA ligase (ADP-forming) - BRENDA Enzyme Database
6.2 Forming carbon-sulfur bonds. 6.2.1 Acid-thiol ligases. 6.2.1.13 acetate-CoA ligase (ADP-forming) ... 6.2.1.13: acetate-CoA ligase (ADP-forming). This is an abbreviated version!. For detailed information about acetate-CoA ligase ... coenzyme A ligase (ADP-forming), PF1787, PF1540, TK0944/TK0943 protein, ADP-forming acetyl-CoA synthetase isoenzyme I, ADP ... acetyl-coenzyme A synthetase, EhACD, ADP-forming acetyl-coenzyme A synthetase, acetate:CoA ligase [ADP-forming], ADP-forming ...
Nutrients | Free Full-Text | A Review of Dietary (Phyto)Nutrients for Glutathione Support
CGL cleaves the sulfur-gamma carbon bond of cystathionine, resulting in the release of cysteine which can be used by GCL and ... First, cysteine is conjoined with glutamate through the action of glutamate cysteine ligase to produce gamma-glutamylcysteine, ... Cysteine is a sulfur amino acid, which might imply that consuming sulfur-rich foods, especially those containing the sulfur ... CGL cleaves the sulfur-gamma carbon bond of cystathionine, resulting in the release of cysteine which can be used by GCL and ...
Biomolecules & Therapeutics
| Korea Science
ligase in the aged mice. The elevation of hepatic cysteine levels may be involved in the maintenance of hepatic GSH levels. The ... Alterations in sulfur amino acid metabolism are associated with an increased risk of a number of common late-life diseases, ... Carbon monoxide (CO) is a gaseous molecule produced from heme by heme oxygenase (HO). Endogenous CO production occurring at low ... The levels of sulfur amino acids and their metabolites were not significantly different among 2-, 6- and 18-month-old mice, ...
Bioinorganic Chemistry - Paperback - Dieter Rehder; - Oxford University Press
9. The Sulfur Cycle. 10. The Nitrogen Cycle. 10.1. Overview, and Native Nitrogenase. 10.2. Overview, and Native Nitrogenase. ... 13.2.1. Ligases and synthases. 13.2.2. Carboanhydrases based on Zn or Cd. 13.2.3. Hydrolases. 13.2.4. Alcoholdehydrogenase. ... The Biogenic Metalloid- and Metal-Carbon Bond. 14.1. Vitamin B12. 14.2. Others. 15. Inorganics in Medicine. 15.1. Toxic Metals ...
Carbon-Oxygen Ligases | Profiles RNS
Carbon-Carbon Ligases. *Carbon-Nitrogen Ligases. *Carbon-Oxygen Ligases. *Carbon-Sulfur Ligases ... "Carbon-Oxygen Ligases" by people in UAMS Profiles by year, and whether "Carbon-Oxygen Ligases" was a major or minor topic of ... "Carbon-Oxygen Ligases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Carbon-Oxygen Ligases" by people in Profiles over the past ten years. ...
Sulfide regulation of cardiovascular function in health and disease | Nature Reviews Cardiology
The oxidation state of sulfur has a broad range, from −2 in H2S, 0 in elemental sulfur (S8), +2 in sulfur monoxide (SO), and a ... Carbon monoxide (CO) and nitric oxide (NO) are the other two gaseous neurotransmitters in this class. Before the identification ... CARS, cysteinyl-tRNA synthetase (also known as cytoplasmic cysteine-tRNA ligase); CAT, cysteine aminotransferase; CysSH, ... such as iron-sulfur clusters) and bound sulfane sulfur16,17,18 (such as hydropersulfides and polysulfides). H2S predominantly ...
KNA52718 details
protein deficiency
Biochemistry For Dummies | BiggerBooks
First reaction: Nitrogen base + 5-carbon sugar = nucleoside 148. Second reaction: Phosphoric acid + nucleoside = nucleotide 149 ... Putting it together: Ligases 87. Enzymes as Catalysts: When Fast Is Not Fast Enough 88 ... Functional groups with oxygen and sulfur 37. Functional groups containing nitrogen 38 ...
Classification of enzymes
6. Ligases. These enzymes are otherwise known as synthetases. They catalyse synthesis reactions by joining two molecules, ... Sulphur containing groups (2.8). 3. Hydrolases. The hydrolases are those enzymes which catalyse hydrolysis reactions i.e the ... one carbon compounds (2.1). · aldehyde or ketonic groups (2.2). · acyl groups (2.3). ... The subclasses of ligases are based on the nature of bond formed in the product. Formation of. ...
Ben-Gurion University of the Negev - Research output
- Ben-Gurion University Research Portal
Subject: basic-leucine zipper transcription factors / Subject term: basic-leucine zipper transcription factors - PubAg Search...
... carbon monoxide; food intake; gastric acid; glutamate-cysteine ligase; heme oxygenase (biliverdin-producing); iron; quinones; ... sulfur; transcription (genetics). Abstract:. ... BACKGROUND: Glutaredoxins (GRXs) are small proteins which bind glutathione to ... glutamate-cysteine ligase, and NAD(P)H quinone dehydrogenase 1, among which HO-1 is an enzyme catalyzing the degradation of ... either reduce disulfide bonds or to coordinate iron sulfur clusters. Whereas these well-established functions are associated ...
KEGG REACTION: R08088
acetate---CoA ligase (ADP-forming) subunit beta [EC:6.2.1.13]. K23756 medium-chain acyl-CoA ligase / lipoate-activating enzyme ... Carbon metabolism. rn01212 Fatty acid metabolism. rn01220 Degradation of aromatic compounds. rn01240 Biosynthesis of cofactors ... Sulfur metabolism. rn00930 Caprolactam degradation. rn00980 Metabolism of xenobiotics by cytochrome P450. ... 4-hydroxybutyrate---CoA ligase (ADP-forming) [EC:6.2.1.56]. K18594 3-hydroxypropionyl-CoA synthetase (ADP-forming) [EC:6.2.1.-] ...
DeCS 2008 - versión 17 de Marzo de 2008
Structural Biochemistry/Enzyme - Wikibooks, open books for an open world
Ligases are used in catalysis where two substrates are litigated and the formation of carbon-carbon, carbon-sulfide, carbon- ... The succinate dehydrogenase complex showing several cofactors, including flavin, iron-sulfur centers and heme. ... Ligases Catalyze bond formation coupled with ATP hydrolysis. Citric acid synthetase Lyases Catalyze a group elimination in ... The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. Then the carbonic acid becomes a ...
Domain IPR003439:ABC transporter-like
Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain 63 Domain IPR025877:MobA-like NTP transferase ... iron-sulphur binding, conserved site 477 Domain IPR001387:Cro/C1-type helix-turn-helix domain 462 Domain IPR001647:DNA-binding ... Carbon monoxide dehydrogenase subunit G 12 Family IPR004484:Cobyrinic acid a,c-diamide synthase CbiA 12 Family IPR005770: ... D-alanine ligase, N-terminal domain 34 Domain IPR001086:Prephenate dehydratase 34 Domain IPR004150:NAD-dependent DNA ligase, OB ...
birA protein (Pseudomonas aeruginosa) - STRING interaction network
Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a ... Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin ... and carbon dioxide ... ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase ... Pantoate--beta-alanine ligase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a ...
Download Soil Monitoring: Early Detection And Surveying Of Soil Contamination And Degradation 1993
1990; Farnet and Haseltine 1990, 1991). The calcium of in sulphur complexes with been recombination allows searched its ... IRS suppresses one of the ligases of download Soil Monitoring: Early activating cells. It is known by health and is a ... 1992), which is itself launched by a 18-carbon repression characterized the E2( Martinon et al. Processing and ligand of IL1B ... ventilating ligases( UCPs) are Differences of the alternative download telomere tumorigenesis, and are increased internalized ...
Frontiers | Interactions between Bacteria and Bile Salts in the Gastrointestinal and Hepatobiliary Tracts
iii) Planktonic Salmonella cells can multiply in the gall bladder lumen, presumably using phospholipids as carbon and energy ... and ATP-dependent reaction catalyzed by CoA ligase (30). The bile salt-Coa thioester is then oxidized at the 3-hydroxy group by ... increasing organic sulfur availability for B. wadswortia (43). ... while glycine and taurine can be used as sources of carbon and ...
Download Javascript Demystified
Lime-sulfur was not assigned in U. Zdenko Hans Skraup( CZ) performed time which can use edited as an Comprehensive( 3196). ... This nucleus, there, cannot turn of modern carbon; but then is first to upload, that there is a new acara betwixt domain and ... ligase: principally justified at one of the temperatures largest ions with the original wasgreat, they do the first liver of ... ve on the neuralgia of adolescent carbon outline in photos. hukum of paralytic fibers to the course of elderly information. The ...
Liases
... and carbon-carbon bond formation and cleavage (lyase) reactions. Seeking to study the carbon-carbon cleavage reaction of α- ... Moreover, NEDD4 was identified as the E3 ligase for HMGCL and promoted its degradation. In addition, mutation of Ser258 to ... The Suf pathway mobilizes sulfur via SufS, a type II cysteine desulfurase. SufS is a pyridoxal-5-phosphate-dependent enzyme ... In many lignin depolymerization processes, aromatic dimers and oligomers linked by carbon-carbon bonds remain intact, ...
TCDB » Superfamilies
Iron-Sulfur Protein (ISP) Superfamily. Iron-Sulfur proteins are found within many multi-component electron carrier systems, ... Ubiquitin Ligase (UL) Superfamily These proteins are listed either under TC subclass 8.A or within ERAD families as a component ... 2.A.114 - The Putative Peptide Transporter Carbon Starvation CstA (CstA) Family. 2.A.120 - The Putative Amino Acid Permease ( ... 2.A.131 - The Aminobenzyl Carbon-arsenic Defining Exporter (ABCDE) Family. 5.A.1 - The Disulfide Bond Oxidoreductase D (DsbD) ...
YOR184W 2167.216480 INESSENTIAL SER1 phosphoserine transaminase,phosphoserine aminotransferase
CoA ligase and synthetase 4,long-chain-fatty-acid-CoA-ligase, YDL134C 0.779367 INESSENTIAL PPH21 serine-threonine protein ... sulfur amino acid metabolism, YMR175W -2.346610 INESSENTIAL SIP18 Salt-Induced Protein of 18 kDa, biological_process unknown, ... 0.744638 INESSENTIAL MLS1 carbon-catabolite sensitive malate synthase, glyoxylate cycle, malate synthase, peroxisomal matrix ... protein ligase*, nuclear ubiquitin ligase complex YLR366W -2.666972 INESSENTIAL biological_process unknown, molecular_function ...
Publications of Reimo Zoschke | Max Planck Institute of Molecular Plant Physiology
Reduced Expression of Succinyl CoA Ligase can be Compensated for by an Upregulation of the {gamma}-amino-butyrate (GABA) Shunt ... Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in ... Vitamin B1 biosynthesis in plants requires the essential iron sulfur cluster protein, THIC. Proceedings of the National Academy ...
Ubiquitin-proteiAcetateBiosynthesisBondsNitrogenMetabolismLyaseDioxideOxygenCycleMonoxideBiotinPhotosynthesisMoleculesAcidMetabolicBondStrandIronProcessPlantsCellsMetabolismProteinEnzymeEnzymesIron-sulfurSynthasePutativeCompoundsFixationMetabolitesCellularPhosphateGenesMolecularEnvironmentsGroupEffectiveFormationPropertiesSourceSubjectEarthTotal
Ubiquitin-protei1
- Ubiquitin--protein ligase. (uma.es)
Acetate1
- For detailed information about acetate-CoA ligase (ADP-forming), go to the full flat file . (brenda-enzymes.org)
Biosynthesis2
- Vitamin B1 biosynthesis in plants requires the essential iron sulfur cluster protein, THIC. (mpg.de)
- Starch is a repository of carbon which is later used during the dark phase as the primary carbon source for biomass formation [ 2 ] and fuelling of sucrose biosynthesis and its transport. (biomedcentral.com)
Bonds1
- Ligases, Forming carbon-nitrogen bonds, Acid--D-amino-acid ligases (peptide synthases). (uma.es)
Nitrogen4
- Flux Balance Analysis (FBA) of the model resulted in balanced carbon, nitrogen, proton, energy and redox states under both light and dark conditions. (biomedcentral.com)
- Methods: We used defferent operations (direct suture by shortening the traumatic finger, Study on the Conditions of Liquid Culture of Inonotus obliquus, The effects of different carbon sources,nitrogen sources,agar,natural substance,culture time and volume of culture solution on liquid culture of Inonotus obliquus were studied.The results indicated, By clicking accept or continuing to use the site, you agree to the terms outlined in our. (trends-magazine.net)
- All these processes are tightly regulated by proteins and microRNA in response to both external and internal nitrogen levels, carbon status of the plant and hormones. (scirp.org)
- Among macro nutrients, nitrogen is next to carbon in importance to plants. (scirp.org)
Metabolism2
- Furthermore, the structured metabolic model should take into account major pathways of primary metabolism such as sugar metabolism, central carbon metabolisms, photosynthesis, photorespiration, energy and redox metabolism, proton turnover, sucrose translocation from source to sink tissues and biomass growth. (biomedcentral.com)
- In future, we will use the model to recognize cause-effect relationships and describe regulatory processes in carbon metabolism and transport. (biomedcentral.com)
Lyase1
- The cytochrome P450 (CYP) superfamily of heme monooxygenases has demonstrated ability to facilitate hydroxylation, desaturation, sulfoxidation, epoxidation, heteroatom dealkylation, and carbon-carbon bond formation and cleavage (lyase) reactions. (bvsalud.org)
Dioxide4
- The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. (wikibooks.org)
- 4) How many oxygen molecules (O2) are required each time a molecule of glucose (C6H12O6) is completely oxidized to carbon dioxide and water via aerobic respiration? (easynotecards.com)
- Johan Gottlieb Gahn was the first to isolate an impure sample of manganese metal in 1774, which he did by reducing the dioxide with carbon. (alchetron.com)
- Manganese dioxide is used as the cathode (electron acceptor) material in zinc-carbon and alkaline batteries. (alchetron.com)
Oxygen3
- Carbon-Oxygen Ligases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uams.edu)
- This graph shows the total number of publications written about "Carbon-Oxygen Ligases" by people in UAMS Profiles by year, and whether "Carbon-Oxygen Ligases" was a major or minor topic of these publications. (uams.edu)
- Below are the most recent publications written about "Carbon-Oxygen Ligases" by people in Profiles over the past ten years. (uams.edu)
Cycle3
- H 2 S is a major component of the sulfur cycle and is present in the environment (such as in decaying organic matter, groundwater and natural gases). (nature.com)
- This discovery characterises a missing enzyme relevant to the global sulfur cycle. (bvsalud.org)
- Rational design of a metal-organic framework host for sulfur storage in fast, long-cycle Li-S batteries† Junwen Zhou , a Rui Li , b Xinxin Fan , a Yifa Chen , b Ruodan Han , b Wei Li , a Jie Zheng , a Bo Wang * b and Xingguo Li * a Dramas. (trends-magazine.net)
Monoxide1
- Carbon monoxide (CO) is a gaseous molecule produced from heme by heme oxygenase (HO). (koreascience.kr)
Biotin1
- Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. (string-db.org)
Photosynthesis1
- Reduced expression of aconitase results in an enhanced rate of photosynthesis and marked shifts in carbon partitioning in illuminated leaves of wild species tomato. (mpg.de)
Molecules1
- Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. (bvsalud.org)
Acid1
- Seeking to study the carbon-carbon cleavage reaction of α-hydroxy ketones in mechanistic detail using a microbial P450, we synthesized α-hydroxy ketone probes based on the physiological substrate for a well-characterized benzoic acid metabolizing P450, CYP199A4. (bvsalud.org)
Metabolic1
- Systemic analysis of these metabolic and underlying regulatory processes allow a detailed understanding of carbon distribution within the plant and the formation of associated phenotypic traits. (biomedcentral.com)
Bond1
- The subclasses of ligases are based on the nature of bond formed in the product. (brainkart.com)
Strand1
- The immune carbon is the production of a homology strand from the uncertain secreted by cells( GGTs). (familie-vos.de)
Iron1
- Monovalent iron in a sulfur-rich environment. (jefferson.edu)
Process1
- also all residues of kinases and buildings interact the toxic inflammasomes but at best the hnRNPA1 can be the phosphorylation and acetylation of the process, initiate the transcription or sulfur on Text-to-Speech to phosphorylate 6-phospho-D-gluconate subunit. (erik-mill.de)
Plants1
- In growing plants, sucrose is the most widespread sugar used to supply both carbon and energy from 'source' tissues (e.g. autotrophic mesophyll) to 'sink' tissues (e.g. heterotrophic roots, growing shoots or reproductive organs) to build up a biomass [ 1 ]. (biomedcentral.com)
Cells2
- IRS suppresses one of the ligases of download Soil Monitoring: Early activating cells. (evakoch.com)
- Within the ITAM)-like social cells transcriptional mutations are elected unraveled to tissue 4-cholesten-7alpha,12alpha,24(S)-triol-3-one leaflet, and the PITX2 somatic ligases are reviewed conserved into the signal-transducing for the kinase of Damaged events( Kopf et al. (erik-mill.de)
Metabolism11
- Overall, aim of our research is to mechanistically associate biological processes of fundamental importance for the biosphere, previously thought to be unrelated, i.e. photoperception, photoprotection, carbon and nutrient metabolism , by combining genetic, biochemical, molecular, physiological and mathematical modelling approaches. (lpcv.fr)
- What are the key molecular actors (genes, transcription factors, proteins, metabolites) for the processes of photoprotection and carbon metabolism? (lpcv.fr)
- A tRNA modification balances carbon and nitrogen metabolism by regulating phosphate homeostasis. (instem.res.in)
- 2020. Allosteric inhibition of MTHFR prevents futile SAM cycling and maintains nucleotide pools in one-carbon metabolism. . (instem.res.in)
- At the cellular level, methyl donors (e.g. methionine, choline, betaine and folic acid) interact through one-carbon metabolism to modulate metabolism, immune responses and epigenetic events. (biomedcentral.com)
- Thus, altering one-carbon metabolism through methyl donor supplementation is a viable option to modulate immunometabolism during the peripartal period. (biomedcentral.com)
- This review explores available data on the regulation of one-carbon metabolism pathways in dairy cows in the context of enzyme regulation, cellular sensors and signaling mechanisms that might respond to increased dietary supply of specific methyl donors. (biomedcentral.com)
- Effects of methyl donors beyond the one-carbon metabolism pathways, including production performance, immune cell function, mechanistic target or rapamycin signaling, and fatty acid oxidation will also be highlighted. (biomedcentral.com)
- Furthermore, the effects of body condition and feeding system (total mixed ration vs. pasture) on one-carbon metabolism pathways are explored. (biomedcentral.com)
- Methyl donors (e.g. folate, choline, betaine) serve functional roles throughout the body via their metabolic, epigenetic, and immunomodulatory properties, and share common biochemical pathways, of which one-carbon metabolism has received the most attention (Fig. 1 ). (biomedcentral.com)
- A52, Revealed the Conservation of the Pathways of Dissimilatory Sulfur Metabolism and Variations in the Genetic Inventory for Nitrogen Metabolism and Autotrophic Carbon Fixation. (academictree.org)
Protein9
- Free lipoic can be attached to the lipoyl domain by the enzyme lipoate protein ligase. (zubiaga.org)
- Lipoate protein ligases proceed via a enzyme bound lipoyl adenylate intermediate. (zubiaga.org)
- For ubiquitin alone, there exist over 600 ligases that attach it to protein substrates in humans 3 . (nature.com)
- structure of a putative lipoate protein ligase from thermoplasma acidophilum and the mechanism of target selection for post-translational modification. (liverpool.ac.uk)
- a gene encoding a putative lipoate protein ligase (lpla) of thermoplasma acidophilum was cloned and expressed in escherichia coli. (liverpool.ac.uk)
- 7. The organism of claim 1, further comprising at least one enzyme or polypeptide selected from the group consisting of a corrinoid protein, a methyltetrahydrofolate:corrinoid protein methyltransferase, a corrinoid iron-sulfur protein, a nickel-protein assembly protein, a ferredoxin, an acetyl-CoA synthase, a carbon monoxide dehydrogenase, a pyruvate ferredoxin oxidoreductase, and a hydrogenase. (patentsencyclopedia.com)
- Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). (nih.gov)
- In the lysosomal proteolysis pathway, cell uptake degraded protein by lysosomes through a non-selective process, but it may become selective during starvation especially under carbon and nitrogen starvation condition [ 11 ]. (springeropen.com)
- Protein degradation under the ubiquitin-proteasome pathway involves three major steps: (i) ATP-dependent activation of ubiquitin by E1 enzyme (ubiquitin-activating enzyme), (ii) transfer of activated ubiquitin to E2 (ubiquitin-conjugating enzyme), and (iii) transfer of ubiquitin to the protein to be degraded by E3 complex (ubiquitin protein ligase) [ 13 ]. (springeropen.com)
Enzyme5
- That means that one molecule of the enzyme can cause a million molecules of carbon dioxide to react in one second. (thefreedictionary.com)
- Like all ligases, this enzyme requires ATP. (zubiaga.org)
- Isocitrate lyase (Icl), which is a key enzyme in the glyoxylate cycle and is essential as an anapleurotic enzyme for growth using acetate and certain fatty acids as a carbon source, is upregulated in MTB organisms that are exposed to anaerobic conditions and are in the stationary phase, or growing inside macrophages. (medscape.com)
- Electron Transport Chain Mechanism Complex I: NADH dehydrogenase Complex-I also called "NADH: Ubiquinine oxidoreductase" is a large enzyme composed of 42 different polypeptide chains, including as FMN-containing flavoprotein and at least six iron-sulfur centers. (hitterslog.com)
- Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. (nih.gov)
Enzymes1
- Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. (nih.gov)
Iron-sulfur3
- Some of the plasmids also carry genes required for the molecular assembly of iron-sulfur [Fe-S] clusters. (frontiersin.org)
- Within clustered DNA lesions, they pose a serious problem for repair proteins, especially for iron-sulfur glycosylases (MutyH), which can recognize them by the electron-transfer process. (shengsci.com)
- Azotobacter has many iron-sulfur proteins in its genome, which were identified as far back as the 1960s and probably play roles in the complex redox chemistry that Azotobacter must maintain when fixing nitrogen. (imperial.ac.uk)
Synthase2
- The sulfur centers are inserted into the 6th and 8th carbons of octanoate via the a radical s-adenosyl methionine mechanism, by lipoyl synthase. (zubiaga.org)
- The sulfurs are from the lipoyl synthase polypeptide. (zubiaga.org)
Putative1
- Activation of LHCSR3 gene requires the absorption of blue-light by the photoreceptor phototropin (5) via the putative E3 ubiquitin ligase CUL4-DDB1 DET1 (9) while it also involves calcium ion signalling and active photosynthetic electron transport (6) as well as a tightly controlled methylation of cytosine to 5-methylcytosine of the promoter region of the gene (18). (lpcv.fr)
Compounds2
- [2] The kinds of living organisms currently known on Earth all use carbon compounds for basic structural and metabolic functions, water as a solvent , and DNA or RNA to define and control their form. (cloudfront.net)
- If life exists on other planets or moons it may be chemically similar, though it is also possible that there are organisms with quite different chemistries [3] - for instance, involving other classes of carbon compounds, compounds of another element, or another solvent in place of water. (cloudfront.net)
Fixation1
- The complete 3-hydroxypropionate/4-hydroxybutyrate cycle and dicarboxylate/4-hydroxybutyrate cycle involved in carbon fixation were found in all Metallosphaera genomes. (frontiersin.org)
Metabolites1
- 2017. Thiol trapping and metabolic redistribution of sulfur metabolites enable cells to overcome cysteine overload. . (instem.res.in)
Cellular2
- Nutrient and carbon limitations not only trigger a cellular metabolic readjustment but also impact the qE capacity of Chlamydomonas . (lpcv.fr)
- Cyclin D1( CCND1) fully is cellular degradation of sulfur by Signaling function modification HDAC4 to RUNX3, signaling to RUNX3 deacetylation( Lee et al. (evakoch.com)
Phosphate2
- Indeed, besides HL, LHCSR accumulation can be elicited by exposure to low Ci (13) as well as sulfur, nitrogen, phosphate) and iron (14-16) deprivation. (lpcv.fr)
- Cycles, sources, and sinks: Conceptualizing how phosphate balance modulates carbon flux using yeast metabolic networks. (instem.res.in)
Genes1
- Genes sqr , tth , sir , tqo , hdr , tst , soe , and sdo associated with sulfur oxidation, and gene clusters fox and cbs involved in iron oxidation existed in all Metallosphaera genomes. (frontiersin.org)
Molecular1
- This list contains a list of EC numbers for the sixth group, EC 6 , ligases , placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology . (wikibedia.ru)
Environments1
- Members of the genus Metallosphaera are widely found in sulfur-rich and metal-laden environments, but their physiological and ecological roles remain poorly understood. (frontiersin.org)
Group1
- Silicon is in the same group as carbon on the periodic table and, like carbon, it is tetravalent . (cloudfront.net)
Effective2
- Production of renewable hydrogen energy by water electrolysis is an effective method to reduce carbon emissions. (usda.gov)
- The E3 ubiquitin ligase Pib1 regulates effective gluconeogenic shutdown upon glucose availability. (instem.res.in)
Formation1
- NKX3-2( BAPX1), been for inhibitory production of the endocytosed caspase( Tribioli and Lufkin 1999), ligases the Archived( evergreen) processing of the RUNX2 formation and heterodimerizes its channel( Lengner et al. (erik-mill.de)
Properties1
- Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. (genome.jp)
Source1
- Desulfotignum phosphitoxidans is a rod-shaped Gram-negative bacterium that is able to grow with phosphite as a single electron donor and CO 2 as the only carbon source. (biomedcentral.com)
Subject1
- Acetate-CoA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (covidauthors.org)
Earth1
- This non-motile bacterium is a free-living marine organism that is one of the most abundant, as well as the smallest, on earth, and contributes heavily to carbon cycling in the marine environment. (up.ac.za)
Total1
- This graph shows the total number of publications written about "Acetate-CoA Ligase" by people in this website by year, and whether "Acetate-CoA Ligase" was a major or minor topic of these publications. (covidauthors.org)