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
IV THERAPY
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
Trans-feruloyl-CoA synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... systematic name of this enzyme class is trans-ferulate:CoASH ligase (ATP-hydrolysing). This enzyme is also called trans- ...
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 ...
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 ...
Muramyl ligase
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ... All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each ...
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 + ... Antranikian G, Herzberg C, Gottschalk G (1985). "Covalent modification of citrate lyase ligase from Clostridium sphenoides by ...
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 that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\ ... "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 ... systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). ...
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 ...
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 + ... systematic name of this enzyme class is anthranilate:CoA ligase (AMP-forming). Other names in common use include anthraniloyl ...
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 ⇌ {\ ... CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle. Lill U, Schreil A, Eggerer H (1982). " ... systematic name of this enzyme class is citrate:CoA ligase (ADP-forming). Other names in common use include citryl-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 ... systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-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 ⇌ {\ ... systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA ...
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- ... systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include ...
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 ⇌ {\ ... systematic name of this enzyme class is oxalate:CoA ligase (AMP-forming). Other names in common use include oxalyl-CoA ... Organisms with Oxalate-CoA Ligases include: Arabidopsis thaliana Saccharomyces cerevisiae http://www.plantcell.org/content/24/3 ...
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 + ... systematic name of this enzyme class is arachidonate:CoA ligase (AMP-forming). This enzyme is also called arachidonoyl-CoA ...
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- ... systematic name of this enzyme class is 4-hydroxybenzoate:CoA ligase (AMP-forming). Other names in common use include 4- ...
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 ... systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase ( ...
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 + ... systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ...
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 ... 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 ... systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in ...
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 3alpha,7alpha-dihydroxy-5beta-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997-1004. PMID ...
Aminoacyl tRNA synthetase
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... An aminoacyl-tRNA synthetase (aaRS or ARS), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto ...
Glutamine synthetase
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... glutamate-ammonia ligase. Active site between two monomers of glutamine synthetase from Salmonella typhimurium. Cation binding ... "Evidence of covalent modification of glutamine synthetase in the purple sulfur bacterium". FEMS Microbiology Letters. 122 (1-2 ...
Carbamoyl phosphate synthetase
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ...
Phosphoribosylformylglycinamidine synthase
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... L-glutamine amido-ligase, (ADP-forming), 2-N-formyl-1-N-(5-phospho-D-ribosyl)glycinamide:L-glutamine, and amido-ligase (ADP- ... The systematic name of this enzyme class is N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide:L-glutamine amido-ligase (ADP-forming ...
Mdm2
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... E3 ligase activity[edit]. The E3 ubiquitin ligase MDM2 is a negative regulator of the p53 tumor suppressor protein. MDM2 binds ... ubiquitin protein ligase activity. • NEDD8 ligase activity. • disordered domain specific binding. • protein domain specific ... The RING domain of Mdm2 confers E3 ubiquitin ligase activity and is sufficient for E3 ligase activity in Mdm2 RING ...
Asparagine synthase (glutamine-hydrolysing)
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... L-glutamine amido-ligase (AMP-forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction ...
List of enzymes
Category:EC 6.2 (form carbon-sulfur bonds)Edit. *EC 6.2.1.1: Acetate--CoA ligase ... Category:Ligases (EC 6) (Ligase)Edit. Category:EC 6.1 (form carbon-oxygen bonds)Edit. 6-carboxytetrahydropterin synthase ... 6 Category:Ligases (EC 6) (Ligase) *6.1 Category:EC 6.1 (form carbon-oxygen bonds) ... Category:EC 4.4 (carbon-sulfur lyases)Edit. *Category:EC 4.4.1 *Cystathionine gamma-lyase ...
Superoxide dismutase
Aconitase is one of several iron-sulfur-containing (de)hydratases in metabolic pathways shown to be inactivated by superoxide.[ ... SOD2 knockout or null mutations cause growth inhibition on respiratory carbon sources in addition to decreased post-diauxic ...
Cysteine
... because of the presence of sulfur (resp. selenium) as a second neighbor to the asymmetric carbon. The remaining chiral amino ... Ubiquitin ligases transfer ubiquitin to its pendant, proteins, and caspases, which engage in proteolysis in the apoptotic cycle ... Precursor to iron-sulfur clusters[edit]. Cysteine is an important source of sulfide in human metabolism. The sulfide in iron- ... The sulfur is derived from methionine, which is converted to homocysteine through the intermediate S-adenosylmethionine. ...
Catalytic triad
The lone pair of electrons present on the oxygen or sulfur attacks the electropositive carbonyl carbon.[3] The 20 naturally ... 1994). "A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues". Science. 266 (5183 ... Use of oxygen or sulfur as the nucleophilic atom causes minor differences in catalysis. Compared to oxygen, sulfur's extra d ... Sterically, the sulfur of cysteine also forms longer bonds and has a bulkier van der Waals radius[2] and if mutated to serine ...
Oxygenase
SW, Ryter; J, Alam (April 2006). "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications". Physiol ... These constitute a major intracellular source of iron and carbon monoxide[7] ... 1.14.15: reduced iron-sulfur protein. *11B1. *11B2. *11A1. 1.14.16: reduced pteridine (BH4 dependent). *Phenylalanine ...
Succinate dehydrogenase
The basic residue or cofactor deprotonates the alpha carbon, and FAD accepts the hydride from the beta carbon, oxidizing the ... Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial. Pfam PF13085, Pfam PF13183 3. SdhC. C560_HUMAN. ... The first two subunits, a flavoprotein (SdhA) and an iron-sulfur protein (SdhB), form a hydrophilic head where enzymatic ... The complex is also thought to be capable of inserting the iron-sulphur clusters in SDHB during its maturation. The studies ...
Protease
Sims GK, Wander MM (2002). "Proteolytic activity under nitrogen or sulfur limitation". Appl. Soil Ecol. 568: 1-5.. ... Bacterial and fungal proteases are particularly important to the global carbon and nitrogen cycles in the recycling of proteins ... present in soil can be observed at the overall microbial community level as proteins are broken down in response to carbon, ... nitrogen, or sulfur limitation.[11] Bacteria contain proteases responsible for general protein quality control (e.g. the AAA+ ...
Cofactor (biochemistry)
Iron-sulfur clusters[edit]. Further information: Iron-sulfur protein. Iron-sulfur clusters are complexes of iron and sulfur ... 2-carbon groups, α cleavage. Bacteria, archaea and eukaryotes NAD+ and NADP+ [31]. Niacin (B3). ADP. Electrons. Bacteria, ... Meyer J (February 2008). "Iron-sulfur protein folds, iron-sulfur chemistry, and evolution". J. Biol. Inorg. Chem. 13 (2): 157- ... A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues. ...
Arachidonate 5-lipoxygenase
... which bind the sulfur of cysteine's thio (i.e. SH) residue in the tripeptide glutamate-cysteine-glycine to carbon 6 of LTA4 ... at carbon 5 of its 1,4 diene group (i.e. its 5Z,8Z double bonds) to form 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid ( ... is identical to AA except that has a single rather than double bond between its 15th and 16th carbon. ALOX5 metabolizes mead ...
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 ...
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- ... systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6- ...
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 ...
Muramyl ligase - Wikipedia
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC),[1] MurD (EC),[2] MurE (EC) [3] and MurF (EC).[4] These ... 6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes ... All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each ...
Ligase - Wikipedia
EC 6.2 includes ligases used to form carbon-sulfur bonds. *EC 6.3 includes ligases used to form carbon-nitrogen bonds ( ... The common names of ligases often include the word "ligase", such as DNA ligase, an enzyme commonly used in molecular biology ... DNA ligase. References[edit]. *^ "Synthases and ligases". chem.qmul.ac.uk. Archived from the original on October 15, 2012. ... This article is about general ligases. For DNA specific ligases, see DNA ligase. ...
KEGG ENZYME: 6.2.1.7
Ligases;. Forming carbon-sulfur bonds;. Acid-thiol ligases. Sysname. cholate:CoA ligase (AMP-forming). ... cholate---CoA ligase;. BAL;. bile acid CoA ligase;. bile acid coenzyme A ligase;. choloyl-CoA synthetase;. choloyl coenzyme A ... THCA-CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate---CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta- ... cholic acid:CoA ligase;. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase;. 3alpha,7alpha,12alpha- ...
KEGG ENZYME: 6.2.1.2
Ligases;. Forming carbon-sulfur bonds;. Acid-thiol ligases. BRITE hierarchy. Sysname. medium-chain fatty acid:CoA ligase (AMP- ... butyrate---CoA ligase;. butyryl-coenzyme A synthetase;. L-(+)-3-hydroxybutyryl CoA ligase;. short-chain acyl-CoA synthetase;. ... medium-chain acyl-CoA ligase;. fadK (gene name);. lvaE (gene name);. butyryl-CoA synthetase;. fatty acid thiokinase (medium ...
Mycobacterium tuberculosis FadD28 protein
Summary Report | CureHunter
... acyl AMP ligase family member required for biosynthesis of phthiocerol dimycocerosate lipid found in the cell wall of ... a fatty -acyl AMP ligase family member required for biosynthesis of phthiocerol dimycocerosate lipid found in the cell wall of ... Ligases: 2113*Carbon-Sulfur Ligases*Mycobacterium tuberculosis FadD28 protein. CureHunter Inc. provides medical information and ...
EC 6.2.1
Forming Carbon Sulfur Bonds. EC 6.2.1 Acid Thiol Ligases. Contents. EC 6.2.1.1 acetate CoA ligase. EC 6.2.1.2 medium-chain acyl ... EC 6.2.1.6 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 ... CoA ligase; p-coumaryl-CoA ligase; p-hydroxycinnamic acid:CoA ligase; 4CL Systematic name: 4-coumarate:CoA ligase (AMP-forming) ... EC 6.2.1.22 citrate (pro-3S)-lyase ligase. EC 6.2.1.23 dicarboxylate CoA ligase. EC 6.2.1.24 phytanate CoA ligase. EC 6.2.1.25 ...
KEGG ORTHOLOGY: K01906
6. Ligases. 6.2 Forming carbon-sulfur bonds. 6.2.1 Acid-thiol ligases. 6.2.1.14 6-carboxyhexanoate---CoA ligase. K01906 bioW; 6 ... K01906 bioW; 6-carboxyhexanoate--CoA ligase. Enzymes [BR:ko01000]. ... Ligases;. Forming carbon-sulfur bonds;. Acid-thiol ligases. BRITE hierarchy. Sysname. 6-carboxyhexanoate:CoA ligase (AMP- ...
Human Metabolome Database: Showing Protein Acetyl-coenzyme A synthetase 2-like, mitochondrial (HMDBP00042)
KEGG BRITE: Enzymes - Aeromonas hydrophila pc104A
6.2 Forming carbon-sulfur bonds 6.3 Forming carbon-nitrogen bonds 6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases) ... 6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date) ... 6.3.4.9 biotin---[methylmalonyl-CoA-carboxytransferase] ligase 6.3.4.10 biotin---[propionyl-CoA-carboxylase (ATP-hydrolysing)] ...
Phenylacetate-CoA ligase - Wikipedia
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 that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\ ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...
Phytanate-CoA ligase - Wikipedia
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 ... systematic name of this enzyme class is phytanate:CoA ligase (AMP-forming). ...
Proteogenomics Reveals Novel Reductive Dehalogenases and Methyltransferases Expressed during Anaerobic Dichloromethane...
... methylated corrinoid/iron-sulfur protein; CH3CO-SCoA, acetyl-CoA; CO, carbon monoxide; CH3CO-PO4, acetyl phosphate; CH3COO−, ... Formyl-THF ligase. Syntrophobotulus glycolicus. 85. Membrane. Yes. 00605. fchA. Methenyl-THF cyclohydrolase. Desulfosporosinus ... Carbon monoxide dehydrogenase. Dehalobacter sp. FTH1. 93. Cytoplasm. Yes. 00220. cooS. Carbon monoxide dehydrogenase catalytic ... B) The RDase subunit A genes encode twin-arginine translocation (Tat) pathway signals and iron-sulfur binding domains. The ...
ENZYME: 6.2.1.
Ligases. Forming carbon-sulfur bonds. Acid--thiol ligases. All UniProtKB/Swiss-Prot entries corresponding to class 6.2.1.-.. ... CoA ligase 6.2.1.7 Cholate--CoA ligase 6.2.1.8 Oxalate--CoA ligase 6.2.1.9 Malate--CoA ligase 6.2.1.10 Acid--CoA ligase (GDP- ... CoA ligase 6.2.1.17 Propionate--CoA ligase 6.2.1.18 Citrate--CoA ligase 6.2.1.19 Long-chain-fatty-acid--protein ligase 6.2.1.20 ... CoA ligase 6.2.1.3 Long-chain-fatty-acid--CoA ligase 6.2.1.4 Succinate--CoA ligase (GDP-forming) 6.2.1.5 Succinate--CoA ligase ...
Ligases Enzyme Market: Key Trends, Segmentation & Regional Analysis | BioSpace
Same as all enzymes, ligases are embedded with proteins that have a target molecule identification site. ... New covalent bonds between two molecules are created by the enzyme called ligase. ... carbon-carbon bond, and carbon-sulphur bond. The energy of a molecule of Guanosine-5-triphosphate or Adenosine Triphosphate is ... which promotes the DNA ligases to bring the two pieces of DNA together. A ligase is also known as a Synthetase. Ligases are one ...
On the specificity of the uridine diphospho-N-acetylmuramyl-alanyl- D-glutamic acid: Diamino acid ligase of Bifidobacterium...
... monocarboxylic acid with 4-6 carbon atoms. Methylation of the ε-amino group or hydroxylation of the δ-carbon atom of lysine ... decreases the competitive properties of the analog, whereas the substitution of the γ-methylen group by sulfur (S-2-aminoethyl ... I. Kinetics and specificity of uridine diphospho-N-acetylmuramyl-L-alanyl-D-glutamyl-L-lysine: D-alanyl-D-alanine ligase ( ... The uridine diphospho-N-acetylmuramyl-alanyl-D-glutamic acid: diamino acid ligase of this organism was purified 700-fold. Since ...
Genome Sequence of the PCE-Dechlorinating Bacterium Dehalococcoides ethenogenes | Science
These include formyl-tetrahydrofolate ligase, a corrinoid iron-sulfur protein, and the α subunit of carbon monoxide ... Previous studies have shown that D. ethenogenes reduces PCE to ethene using two RDs (18) belonging to a family of iron-sulfur ... D. ethenogenes requires acetate as a carbon source (2). Acetyl-coenzyme A (CoA) synthetase, pyruvate-ferredoxin oxidoreductase ...
The draft genome of tropical fruit durian ( Durio zibethinus ) | Nature Genetics
Transcriptomic analysis showed upregulation of sulfur-, ethylene-, and lipid-related pathways in durian fruits. We observed ... associated with production of volatile sulfur compounds (VSCs). MGL and the ethylene-related gene ACS (aminocyclopropane-1- ... Transcriptome and metabolome analyses show that methionine γ-lyase is upregulated and that volatile sulfur compounds are ... of which acid-thiol ligase enzymes (containing a number of key enzymes in carbon-sulfur reactions and flavonoid production) and ...
biotin-CoA ligase(EC 6.2.1.11) - Creative Enzymes
... specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme participates in biotin metabolism. ... This enzyme belongs to the family of ligases, ... those forming carbon-sulfur bonds as acid-thiol ligases. This ... This enzyme belongs to the family of ligases, specifically ...
Frontiers | Genome of a Novel Bacterium "Candidatus Jettenia ecosi" Reconstructed From the Metagenome of an Anammox Bioreactor ...
Autotrophic carbon fixation could be accomplished through the acetyl-coenzyme A pathway. The presence of hydrogenase and ... corrinoid iron-sulfur protein methyltransferase, and the carbon monoxide dehydrogenase/acetyl-CoA synthase complex. ... Jettenia ecosi" J2 genome, namely formate dehydrogenase, formate-tetrahydrofolate ligase, methylenetetrahydrofolate ... 2004). Stable carbon isotopic fractionations associated with inorganic carbon fixation by anaerobic ammonium-oxidizing bacteria ...
YRC Public Data Repository - Protein Overview - gi|7303012
Energy Conservation Associated with Ethanol Formation from H2 and CO2 in Clostridium autoethanogenum Involving Electron...
RnfC2 contains FMN and iron-sulfur clusters and is the site of NADH oxidation, and MetV is an iron-sulfur protein that mediates ... Carbon monoxide dehydrogenase.The specific activity of the enzyme in cell extracts of H2/CO2-grown cells was 5.6 U/mg and thus ... and ligase); CAETHG_1868-69 (clustered with a FixC protein); and CAETHG_3471-72 (clustered with an FMN/FAD binding protein). It ... HytB is an iron-sulfur flavoprotein harboring the NADP binding site, and the other subunits are iron-sulfur proteins. The ...
Frontiers | Bacterial Catabolism of Dimethylsulfoniopropionate (DMSP) | Microbiology
... review will focus on the recent discoveries in the biochemical pathways that mineralize and assimilate DMSP carbon and sulfur, ... a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. The activity of these ... a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. The activity of these ... pathways control the natural flux of sulfur released to the atmosphere. Although these biochemical pathways and the factors ...
ENZYME search by enzyme class
Cyclo-ligases. 6. 2. -.- Forming carbon-sulfur bonds. 6. 2. 1.- Acid--thiol ligases. 6. 3. -.- Forming carbon-nitrogen bonds. 6 ... Acting on carbon-sulfur bonds. 3.13. 1.- Acting on carbon-sulfur bonds. 4. -. -.- Lyases. 4. 1. -.- Carbon-carbon lyases. 4. 1 ... 4. 3.99.- Other carbon-nitrogen lyases. 4. 4. -.- Carbon-sulfur lyases. 4. 4. 1.- Carbon-sulfur lyases. 4. 5. -.- Carbon-halide ... 1.- Acting on carbon-phosphorus bonds. 3.12. -.- Acting on sulfur-sulfur bonds. 3.12. 1.- Acting on sulfur-sulfur bonds. 3.13 ...
DNA ligase
ligase I, DNA, ATP-dependent Identifiers Symbol LIG1 Entrez 3978 HUGO 6598 OMIM 126391 RefSeq NM_000234 ... 6.1 - Carbon-Oxygen. Aminoacyl tRNA synthetase. 6.2 - Carbon-Sulfur. Succinyl coenzyme A synthetase - Acetyl Co-A synthetase - ... DNA ligase has applications in both DNA repair and DNA replication (see Mammalian ligases). In addition, DNA ligase has ... Mammalian ligases. In mammals, there are four specific types of ligase. *DNA ligase I: ligates Okazaki fragments during lagging ...
Difference between revisions of "Coexpression cluster:C1294" - resource browser
Doping-induced Hydrogen-Bond Engineering in Polymeric Carbon Nitride to Significantly Boost the Photocatalytic H2 Evolution...
... graphitic carbon nitride (CN) polymer contains weak hydrogen bond and van der Waals (vdWs) interactions besides strong covalent ... Carbon-carbon Ligases. Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are ... enzymes shifting a carbon-carbon double bond (CARBON-CARBON DOUBLE BOND ISOMERASES), and enzymes transposing S-S bonds (SULFUR- ... Carbon-carbon Double Bond Isomerases. Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to ...
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.. ...
DeCS Ingl s+escopo
D08.811.464 Ligases .. D08.811.464.267 Carbon-Sulfur Ligases .. D08.811.464.267.500 Coenzyme A Ligases .. D08.811.464.267. ... Acetate-CoA Ligase .. Acetothiokinase .. Acetyl Coenzyme A Synthetase .. Acetate CoA Ligase .. Activating Enzyme, Acetyl .. CoA ... Ligase, Acetate-CoA .. Synthetase, Acetyl CoA .. Thiokinase, Acetate .. Acetate Thiokinase .. Acetyl Activating Enzyme .. ... 500.200 Acetate-CoA Ligase .. D08.811.913 Transferases .. D08.811.913.696 Phosphotransferases .. D08.811.913.696.650 ...
The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase | PNAS
... which catalyzes the insertion of sulfur atoms into the six- and eight-carbon positions of the corresponding fatty acid (5-7). ... lipoyl protein ligase A;. mtbLipB,. LipB from Mycobacterium tuberculosis.. * Freely available online through the PNAS open ... it is plausible to assume that the eight-carbon substrate should superimpose with carbon positions C3-C10 of decanoic acid (Fig ... leaves little doubt that the carbon C3 position of decanoic acid mimics the thioester carbon of octanoic acid where the LipB ...
WO2016161043 BIOCONVERSION OF SHORT-CHAIN HYDROCARBONS TO FUELS AND CHEMICALS
Ligases forming carbon-sulfur bonds (6.2). 01. Acid-Thiol Ligases (6.2.1). 01005. Succinate-CoA ligase (ADP-forming) (6.2.1.5) ... Ligases forming carbon-carbon bonds (6.4). 01. Ligases forming carbon-carbon bonds (6.4.1). 01003. Propionyl-CoA carboxylase ( ... Ligases forming carbon-sulfur bonds (6.2). 01. Acid-Thiol Ligases (6.2.1). ... Carbon-carbon lyases (4.1). 03. Oxo-acid-lyases (4.1.3). 03024. Malyl-CoA lyase (4.1.3.24). ...
EnzymeBondsIsomerasesUbiquitinSynthetaseOxidoreductasesAcetateDioxideMetabolismProtein ligaseSynthaseMoleculeAminoReactionNitrogenAtomsHydrogenFormingFlux of sulfurSuccinateProteinsGenesPathwaySubunitPathwaysAcetylCitrateCysteineGroup of donorsMethionineComplexesActivityRecombinationCompoundsPseudomonasAcyl
Enzyme26
- The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales. (wikipedia.org)
- In biochemistry , a ligase is an enzyme that can catalyze the joining of two large molecules by forming a new chemical bond , usually with accompanying hydrolysis of a small pendant chemical group on one of the larger molecules or the enzyme catalyzing the linking together of two compounds, e.g., enzymes that catalyze joining of C-O, C-S, C-N, etc. (wikipedia.org)
- The common names of ligases often include the word "ligase", such as DNA ligase , an enzyme commonly used in molecular biology laboratories to join together DNA fragments. (wikipedia.org)
- It is also said that a synthase is a lyase (a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure) and does not require any energy, whereas a synthetase is a ligase (a ligase is an enzyme that binds two chemicals or compounds) and thus requires energy. (wikipedia.org)
- In enzymology, a phenylacetate-CoA ligase is an enzyme that catalyzes the chemical reaction ATP + phenylacetate + CoA ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + phenylacetyl-CoA The 3 substrates of this enzyme are ATP, phenylacetate, and CoA, whereas its 3 products are AMP, diphosphate, and phenylacetyl-CoA. (wikipedia.org)
- This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. (wikipedia.org)
- The systematic name of this enzyme class is phenylacetate:CoA ligase (AMP-forming). (wikipedia.org)
- This enzyme is also called phytanoyl-CoA ligase. (wikipedia.org)
- New covalent bonds between two molecules are created by the enzyme called ligase. (biospace.com)
- Carbon-nitrogen bonds are formed by the action of the same enzyme as peptide synthetases and amide synthetases. (biospace.com)
- DNA ligase is an enzyme that regulates irregularities. (biospace.com)
- Research activities for sequencing applications, increase in the birth rate, rise in the incidence of infectious diseases, and increase in genetic disorders are key factors that are estimated to boost the global ligases enzyme market . (biospace.com)
- However, high sensitivity of the enzyme to factors such as ligase concentration, DNA concentration, temperature, and buffer composition are expected to restrain the market. (biospace.com)
- The global ligases enzyme market can be segmented based on source, application, end-user, and region. (biospace.com)
- Based on source, the global ligases enzyme market can be classified into microorganisms, animal, and plant. (biospace.com)
- In terms of application, the global ligases enzyme market can be divided into polymerase chain reaction, mutation detection, cloning, drug target, and next generation sequencing. (biospace.com)
- Based on end-user, the global ligases enzyme market can be classified into diagnostic centers & hospitals and research institutes. (biospace.com)
- In terms of region, the global ligases enzyme market can be divided into North America, Europe, Asia Pacific, Latin America, and Middle East & Africa. (biospace.com)
- Studies on the specificity of the ligase toward analogs of ornithine have shown that the enzyme requires a diamino, monocarboxylic acid with 4-6 carbon atoms. (springer.com)
- Ligase will also work with blunt ends , although higher enzyme concentrations and different reaction conditions are required. (chemeurope.com)
- Most experiments use T4 DNA Ligase (isolated from bacteriophage T4) which is most active at 25°C. However in order to perform successful ligations, the optimal enzyme temperature needs to be balanced with the melting temperature T m (also the annealing temperature) of the DNA fragments being ligated. (chemeurope.com)
- Several multicomponent enzyme complexes that catalyze key metabolic reactions in the citric acid cycle and single-carbon metabolism are posttranslationally modified by attachment to lipoic acid ( 1 ). (pnas.org)
- These octanoylated domains are converted into lipoylated derivatives by the S -adenosyl- l -methionine-dependent enzyme, lipoyl synthase (LipA), which catalyzes the insertion of sulfur atoms into the six- and eight-carbon positions of the corresponding fatty acid ( 5 - 7 ). (pnas.org)
- The oxaloacetate is decarboxylated into carbon dioxide and pyruvate in a reaction catalyzed by the enzyme oxaloacetate decarboxylase (Fig. 1 , reaction 4). (asm.org)
- Carbamoyl phosphate synthetase I is a ligase enzyme located in the mitochondria involved in the production of urea. (wikidoc.org)
- That means that one molecule of the enzyme can cause a million molecules of carbon dioxide to react in one second. (thefreedictionary.com)
Bonds2
- The mechanism of DNA ligase is to form covalent phosphodiester bonds between 3' hydroxyl ends of one nucleotide with the 5' phosphate end of another. (chemeurope.com)
- Ligases are used in catalysis where two substrates are ligated and the formation of carbon-carbon, carbon-sulfide, carbon-nitrogen, and carbon-oxygen bonds due to condensation reactions. (wikibooks.org)
Isomerases1
- These enzymes are grouped into six classes: hydrolases (including proteases, amylases and lipases that break down the main nutrients - fats, carbohydrates and proteins), isomerases, ligases, lyases , oxidoreductases and transferases. (thefreedictionary.com)
Ubiquitin5
- Some ligases associate with biological membranes as peripheral membrane proteins or anchored through a single transmembrane helix , [2] for example certain ubiquitin ligase related proteins. (wikipedia.org)
- A recent study revealed that a human PRC1 complex composed of Bmi-1, HPH2, PC3 and Ring proteins (Ring1A & Ring1B), which are homologs of Drosophila Psc, Ph, Pc and dRing, respectively, is an E3 ubiquitin ligase complex that mono-ubiquitinates lysine 119 of nucleosomal histone H2A (15). (maixius.com)
- It was shown that Bmi-1, a Drosophila Psc homolog that was originally discovered through its ability to collaborate with Myc in lymphomagenesis (20-22), plays a central role in the assembly of the PRC1 complex and, while Bmi-1 displays no detectable ubiquitin ligase activity, the binding of Bmi-1 greatly stimulates the E3 ligase activity of Ring1B (15,19). (maixius.com)
- The protein encoded by this gene is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. (wikidoc.org)
- The main action of the VHL protein is thought to be its E3 ubiquitin ligase activity that results in specific target proteins being 'marked' for degradation. (wikidoc.org)
Synthetase4
- Other common names for ligases include the word "synthetase", because they are used to synthesize new molecules. (wikipedia.org)
- A ligase is also known as a Synthetase. (biospace.com)
- Anaerobic" isozyme of acetyl-coenzyme A synthetase, which is required for growth on fermentable carbon sources such as glucose. (ymdb.ca)
- A complete archaeal acetogenesis pathway is identified in the ANME-2a genome, and apparent acetogenic activity of the key enzymes ADP-forming acetate-CoA ligase and acetyl-CoA synthetase is demonstrated. (nature.com)
Oxidoreductases3
- The most distinct phylogenetic finding was a high correlation between iron-sulfur oxidoreductases in combination with carbon nitrogen ligases and Chlorobium. (mirnaarray.com)
- Enzymes can be grouped on the basis of the type reactions they catalyse (oxidoreductases, hydrolases, ligases, etc. (scribd.com)
- He covers chiral discrimination in the active site of oxidoreductases, transferases and chiral discrimination, the influence of chirality on the hydrolysis reactions within the active site of hydrolases, the influence of chirality on the reactions in the active site of lyases , and chiral discrimination in the active site of ligases. (thefreedictionary.com)
Acetate2
- Here, we propose a modified model of carbon cycling in cold seeps: during AOM process, methane can be converted into organic carbon, such as acetate, which further fuels the heterotrophic community in the ecosystem. (nature.com)
- Lastly, two different groups of methanogens, the hydrogenotrophic methanogens and the acetotrophic methanogens, complete the process by converting acetate, formate, and hydrogen produced by other microorganisms to methane and carbon dioxide. (pubmedcentralcanada.ca)
Dioxide9
- Lactic acid bacteria of the genus Leuconostoc play important roles in the dairy industry because of their ability to produce carbon dioxide and C 4 aroma compounds through lactose heterofermentation and citrate utilization. (asm.org)
- The carbon dioxide produced is responsible for eye formation in certain types of cheese. (asm.org)
- Berg IA, Kockelkorn D, Buckel W, Fuchs G (2007) A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in archaea. (springer.com)
- Carbonic anhydrase, which removes carbon dioxide from the blood by binding it to water, has a turnover rate of 10 6 . (thefreedictionary.com)
- Carbon source: Carbon dioxide. (scribd.com)
- [2] [3] Biotin assists in various metabolic reactions involving the transfer of carbon dioxide. (sms4pk.tk)
- The chemosynthetic microorganisms inhabiting cold seeps convert the methane into organic matter and carbon dioxide to generate energy. (nature.com)
- This is surprising because the primary energy source is the AOM process, where carbon dioxide is the end product. (nature.com)
- 7. If glucose were completely oxidized to carbon dioxide and water, yielding the maximum amount of ATP, approximately what percentage of the ATP would be generated via aerobic respiration? (biology-online.org)
Metabolism7
- Impairment of hepatic metabolism of sulfur-containing amino acids has been known to be linked with induction of liver injury. (elsevier.com)
- The contributions vary from insights in the taxonomy of these genera, use of genomics for forward genetics and genomic adaptations, to specific stories addressing virulence, carbon starvation, sulphur metabolism, feruloyl esterases, secondary metabolism and pH modulation, to the development of novel methodology for use in parallel to genome sequencing. (caister.com)
- Building upon this conviction, we have assessed extant types of energy and carbon metabolism for their appropriateness to conditions probably pertaining in those settings of the Hadean planet that fulfil the thermodynamic requirements for life to come into being. (royalsocietypublishing.org)
- The quest for the earliest type of biomass-generating carbon metabolism is mostly informed by either or both of two distinct but equally concerned disciplines: palaeogeochemistry and biology. (royalsocietypublishing.org)
- In the past, attempts towards deducing the nature of the ancestral carbon metabolism were frequently torn between apparently opposing exigencies exerted by geochemistry, on the one hand, and by biology, on the other hand. (royalsocietypublishing.org)
- More recently, inferences towards an ancestral carbon metabolism have increasingly tried to integrate requirements from both geochemistry and biology [ 1 - 5 ]. (royalsocietypublishing.org)
- In short, thinking about the earliest carbon metabolism and about the origin of life in general has turned to searching extant carbon fixation pathways which do not conflict with geochemical boundary conditions and which, furthermore, directly couple energy metabolism to the biomass-generating process, both of which obviously need to be coupled to the abiotically available sources of free energy. (royalsocietypublishing.org)
Protein ligase3
- Structural comparison of LipB with lipoate protein ligase A indicates that, despite conserved structural and sequence active-site features in the two enzymes, 4′-phosphopantetheine-bound octanoic acid recognition is a specific property of LipB. (pnas.org)
- Structure guided design of biotin protein ligase inhibitors for antibiotic discovery. (embl-heidelberg.de)
- Biotin protein ligase (BPL) represents a promising target for the discovery of new antibacterial chemotherapeutics. (embl-heidelberg.de)
Synthase1
- Biotin synthase reductively cleaves SAM into a deoxyadenosyl radical, which abstracts an H atom from dethiobiotin to give an intermediate that is trapped by the sulfur donor. (sms4pk.tk)
Molecule1
- Same as all enzymes, ligases are embedded with proteins that have a target molecule identification site. (biospace.com)
Amino6
- Aminoacyl tRNA-synthetases is included in ligases that join amino acids to the relative tRNA, which promotes the DNA ligases to bring the two pieces of DNA together. (biospace.com)
- A reaction of ligase catalyzing the formation of a carbon-oxygen bond between an amino acid and transfer RNA leads to the formation of the amino acid-RNA ligase bond. (biospace.com)
- Methylation of the ε-amino group or hydroxylation of the δ-carbon atom of lysine decreases the competitive properties of the analog, whereas the substitution of the γ-methylen group by sulfur (S-2-aminoethyl cysteine) results in a highly competitive compound. (springer.com)
- 5. The method of claim 1, wherein said 4-coumarate-CoA ligase comprises the amino acid sequence of SEQ ID No. (patentsencyclopedia.com)
- 13. The chimeric DNA of claim 9, wherein said 4-coumarate-CoA ligase comprises the amino acid sequence of according to SEQ ID No. (patentsencyclopedia.com)
- It is a hyper-ammonia producing bacterium and is able to catabolize amino acids as important carbon and energy sources via Stickland reactions and the development of the specific pathways. (cyberleninka.org)
Reaction1
- ATP is required for the ligase reaction. (chemeurope.com)
Nitrogen3
- The type of ligase varies depending on the type of covalent bond that they catalyze such as carbon-nitrogen bond, carbon-carbon bond, and carbon-sulphur bond. (biospace.com)
- 19. The method of claim 18, wherein the ligase generates a carbon-oxygen bond, a carbon-sulfur bond, a carbon-nitrogen bond, or a carbon-carbon bond between the therapeutic agent and the fibrin microthread. (patentsencyclopedia.com)
- A protocol for three-component reactions of cyclic ethers, α-diazo esters, and weak nitrogen, oxygen, carbon, and sulfur nucleophiles (pKa = 2.2-14.8) to afford a variety of structurally complex α-o. (bioportfolio.com)
Atoms3
- Carbon atoms in the graphitic carbon skeleton can be replaced by heteroatoms with different electronegative from that of the carbon atom (i.e., heteroatom doping) to modulate the charge distribution o. (bioportfolio.com)
- Side-on sulfur monoxide complexes of tantalum, niobium, and vanadium oxyfluorides OMF(η-SO) were prepared via the reactions of metal atoms and SOF upon UV-vis irradiation in a cryogenic matrix. (bioportfolio.com)
- A valeric acid substituent is attached to one of the carbon atoms of the tetrahydrothiophene ring. (sms4pk.tk)
Hydrogen5
- Doping-induced Hydrogen-Bond Engineering in Polymeric Carbon Nitride to Significantly Boost the Photocatalytic H2 Evolution Performance. (bioportfolio.com)
- Unlike graphene, graphitic carbon nitride (CN) polymer contains weak hydrogen bond and van der Waals (vdWs) interactions besides strong covalent bond, which control its final morphology and functionality. (bioportfolio.com)
- Nanorod carbon nitride as a carbo catalyst for selective oxidation of hydrogen sulfide to sulfur. (bioportfolio.com)
- Adessi A, Corneli E, De Philippis R (2017) Photosynthetic purple non sulfur bacteria in hydrogen producing systems: new approaches in the use of well-known and innovative substrates. (springer.com)
- In the transition from dark anaerobiosis to light, oxygen deactivates the hydrogenase pool, but only after carbon fixation outcompetes hydrogen production for electrons. (plantphysiol.org)
Forming3
- Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). (wikipedia.org)
- DNA ligase has the function of forming a bond between the end of an 'acceptor' nucleotide and at the end of a 'donor' nucleotide. (biospace.com)
- C. autoethanogenum can grow on CO as the sole carbon and energy source, forming mainly ethanol and acetic acid but also 2,3-butanediol, lactic acid, and some H 2 as fermentation products ( 6 , 10 ). (asm.org)
Flux of sulfur2
- The activity of these pathways control the natural flux of sulfur released to the atmosphere. (frontiersin.org)
- Glutamate cysteine ligase activity determines flux of sulfur into protein synthesis via the Target of Rapamycin sensor kinase in Arabidopsis. (plantphysiol.org)
Succinate1
- The resulting citrate will have numbers of chemical transformations, whereby it loses one carboxyl group (leading to the 5-carbon compound called alpha-ketoglutarate) and then a second carboxyl group (leading to the 4-carbon compound called succinate). (smpdb.ca)
Proteins1
- The proteins involved are citrate permease (1), citrate lyase α subunit citrate:acetyl-ACP transferase (EC 2.8.3.10 ) (2), citrate lyase β subunit citryl-S-ACP lyase (EC 4.1.3.34 ) (3) oxaloacetate decarboxylase (4), acetate:SH-CL ligase (EC 6.2.1.22 ) (5), and lactate dehydrogenase (6). (asm.org)
Genes3
- For example, DNA ligases are used with restriction enzymes to insert DNA fragments, often genes, into plasmids. (chemeurope.com)
- Multiple dimethyl sulfoxide-molybdopterin (DMSO-MPT) oxidoreductase genes, which are implicated in the reduction of sulfur and arsenic, were identified. (asm.org)
- This pathway is principally under metabolic control, but regulation of the transcription of PP pathway genes can exert a stronger effect, by redirecting larger amounts of carbon to this pathway to satisfy the demand for NADPH. (biomedcentral.com)
Pathway2
- Autotrophic carbon fixation could be accomplished through the Wood Ljungdahl pathway. (frontiersin.org)
- An alternative demethylation/demethiolation pathway results in the eventual release of methanethiol, a highly reactive volatile sulfur compound that contributes little to the atmospheric sulfur flux. (frontiersin.org)
Subunit1
- The catalytic subunit of the PRC1 E3 ligase complex is Ring1B. (maixius.com)
Pathways3
- Transcriptomic analysis showed upregulation of sulfur-, ethylene-, and lipid-related pathways in durian fruits. (nature.com)
- This review will focus on the recent discoveries in the biochemical pathways that mineralize and assimilate DMSP carbon and sulfur, as well as the areas for which a comprehensive understanding is still lacking. (frontiersin.org)
- Using this metabolic map, the analysis of genetic potential for functioning of tricarboxylic acid cycle replenishment pathways was carried out for seven strains of purple non-sulfur bacterium Rhodopseudomonas palustris . (springer.com)
Acetyl2
- At beginning, acetyl-CoA first transfers its 2-carbon acetyl group to the 4-carbon acceptor compound called oxaloacetate to form the 6-carbon compound (citrate) for which the cycle is named. (smpdb.ca)
- Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. (string-db.org)
Citrate2
Cysteine1
- Glutathione (GSH) concentration in liver was elevated in 4̃8 h and then returned to normal in accordance with the changes in glutamate cysteine ligase activity. (elsevier.com)
Group of donors1
- Acting on a sulfur group of donors. (expasy.org)
Methionine1
- We observed paleopolyploidization events shared by durian and cotton and durian-specific gene expansions in MGL (methionine γ-lyase), associated with production of volatile sulfur compounds (VSCs). (nature.com)
Complexes3
- DNA ligase III: complexes with DNA repair protein XRCC1 to aid in sealing base excision mutations and recombinant fragments. (chemeurope.com)
- DNA ligase IV: complexes with XRCC4. (chemeurope.com)
- Side-On Sulfur Monoxide Complexes of Tantalum, Niobium, and Vanadium Oxyfluorides. (bioportfolio.com)
Activity4
- Doping-induced enhancement of crystallinity in polymeric carbon nitride nanosheets to improve their visible-light photocatalytic activity. (bioportfolio.com)
- The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. (maixius.com)
- The two regions of interaction have a synergistic effect on the E3 ligase activity. (maixius.com)
- The E3 ligase activity has been shown to be important for the involvement of PRC1 in X-chromosome inactivation and the control of Hox gene expression (16-19). (maixius.com)
Recombination2
- In addition, DNA ligase has extensive use in molecular biology laboratories for Genetic recombination experiments (see Applications in molecular biology research ). (chemeurope.com)
- One vital, and often tricky, aspect to performing successful recombination experiments involving ligase is controlling the optimal temperature. (chemeurope.com)
Compounds1
- Carbon source: Organic compounds. (scribd.com)
Pseudomonas1
- Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. (wikipedia.org)
Acyl1
- Enzymes transferring one-carbon groups, acyl and glucosyl residues, alkyl or aryl groups, nitrogenous groups, phosphorus-containing groups, and sulfur-containing groups. (thefreedictionary.com)