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.
Carbon Dioxide
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
DNA Ligases
SKP Cullin F-Box Protein Ligases
Carbon Monoxide Poisoning
Carbon Isotopes
Cullin Proteins
Ubiquitination
Carbon Tetrachloride
Carbon Sequestration
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.
Carbon Disulfide
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.
Ubiquitin-Conjugating Enzymes
RNA Ligase (ATP)
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.
Carbon Footprint
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.
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.
Carbon Radioisotopes
Amino Acid Sequence
Ubiquitins
Nitrogen
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.
Biomass
Substrate Specificity
Peptide Synthases
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.
Atmosphere
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.
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
Mutation
Ubiquitin-Activating Enzymes
Carbon-Oxygen Ligases
Biodegradation, Environmental
Soil
Proto-Oncogene Proteins c-cbl
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.
Proteolysis
Acetates
Graphite
Carbon Compounds, Inorganic
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)
Saccharomyces cerevisiae
Carbohydrate Metabolism
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
Models, Biological
Glucose
Oxygen
Catalysis
SUMO-1 Protein
Sequence Homology, Amino Acid
Small Ubiquitin-Related Modifier Proteins
Trees
Electrodes
Saccharomyces cerevisiae Proteins
Temperature
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).
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.
Methane
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.
Hydrogen-Ion Concentration
Ecosystem
Models, Molecular
Magnetic Resonance Spectroscopy
Sumoylation
Carrier Proteins
Amino Acid Motifs
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.
Heme Oxygenase (Decyclizing)
Adenosine Monophosphate
Binding Sites
Alkanes
Base Sequence
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.
Metabolic Networks and Pathways
Multienzyme Complexes
Soil Microbiology
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.
Citric Acid Cycle
Partial Pressure
Pseudomonas
Anaerobiosis
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)
Muscular Atrophy
Greenhouse Effect
Multiprotein Complexes
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.
Cloning, Molecular
Fermentation
Electrochemistry
Repressor Proteins
Gene Expression Regulation, Bacterial
Arabidopsis Proteins
Biocatalysis
Plant Leaves
Arabidopsis
Carbonates
Crystallography, X-Ray
Fatty Acids
Glycerol
Organic Chemicals
Oceans and Seas
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.
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.
DNA-Binding Proteins
Receptors, Autocrine Motility Factor
HeLa Cells
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.
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.
HEK293 Cells
Heavy Ion Radiotherapy
Water
Electrochemical Techniques
Molecular Structure
Charcoal
Amino Acids
Gene Expression Regulation, Plant
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.
Transcription Factors
Methanol
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.
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)
Insufflation
Succinic Acid
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Gene Expression Regulation, Fungal
Acetyl Coenzyme A
Pulmonary Diffusing Capacity
Adenosine Triphosphate
Nuclear Proteins
Fullerenes
Models, Chemical
Succinates
Phenotype
Sequence Analysis, DNA
Peptide Hydrolases
Plant Roots
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).
Ubiquitin-Specific Proteases
RNA, Ribosomal, 16S
Water Microbiology
Mass Spectrometry
Environmental Monitoring
Heme Oxygenase-1
Structure-Activity Relationship
Catalytic Domain
Respiration
The act of breathing with the LUNGS, consisting of INHALATION, or the taking into the lungs of the ambient air, and of EXHALATION, or the expelling of the modified air which contains more CARBON DIOXIDE than the air taken in (Blakiston's Gould Medical Dictionary, 4th ed.). This does not include tissue respiration (= OXYGEN CONSUMPTION) or cell respiration (= CELL RESPIRATION).
Pulmonary Gas Exchange
Air Pollutants
Oxygen Consumption
Recombinant Fusion Proteins
Plasmids
Nitrogen Isotopes
DNA Repair
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
Immunoprecipitation
Stereoisomerism
NAD
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Protein Transport
Wood
Acetic Acid
Tropical Climate
Adsorption
Gene Expression Regulation, Enzymologic
Carboxylic Acids
Formates
Muscle Proteins
Pyruvic Acid
Membrane Proteins
Phytoplankton
Free-floating minute organisms that are photosynthetic. The term is non-taxonomic and refers to a lifestyle (energy utilization and motility), rather than a particular type of organism. Most, but not all, are unicellular algae. Important groups include DIATOMS; DINOFLAGELLATES; CYANOBACTERIA; CHLOROPHYTA; HAPTOPHYTA; CRYPTOMONADS; and silicoflagellates.
Alcohols
Gas Chromatography-Mass Spectrometry
The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase. (1/225)
The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the modification of specific glutamates in a number of proteins required for blood coagulation and associated with bone and calcium homeostasis. All known vitamin K-dependent proteins possess a conserved eighteen-amino acid propeptide sequence that is the primary binding site for the carboxylase. We compared the relative affinities of synthetic propeptides of nine human vitamin K-dependent proteins by determining the inhibition constants (Ki) toward a factor IX propeptide/gamma-carboxyglutamic acid domain substrate. The Ki values for six of the propeptides (factor X, matrix Gla protein, factor VII, factor IX, PRGP1, and protein S) were between 2-35 nM, with the factor X propeptide having the tightest affinity. In contrast, the inhibition constants for the propeptides of prothrombin and protein C are approximately 100-fold weaker than the factor X propeptide. The propeptide of bone Gla protein demonstrates severely impaired carboxylase binding with an inhibition constant of at least 200,000-fold weaker than the factor X propeptide. This study demonstrates that the affinities of the propeptides of the vitamin K-dependent proteins vary over a considerable range; this may have important physiological consequences in the levels of vitamin K-dependent proteins and the biochemical mechanism by which these substrates are modified by the carboxylase. (+info)Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. (2/225)
Vitamin K-dependent proteins contain a propeptide that is required for recognition by the enzyme gamma-glutamylcarboxylase. Substrates used in vitro for carboxylation studies lacking a prosequence are characterized by Km values in the millimolar range, whereas the Km for peptides containing a prosequence is three or four orders of magnitude smaller. Here we report that descarboxy-osteocalcin is an exception in this respect. With descarboxy-osteocalcin in purified propeptide-free recombinant carboxylase, the Km was 1.8 microM. Furthermore, osteocalcin was an inhibitor of descarboxy-osteocalcin carboxylation with a Ki of 76 microM. In contrast with the other vitamin K-dependent proteins, free propeptides do not inhibit descarboxy-osteocalcin carboxylation. Moreover, propeptide-containing substrates were inhibited neither by osteocalcin nor by its propeptide. From our studies we conclude that descarboxy-osteocalcin must have an internal recognition sequence that binds to gamma-glutamylcarboxylase at a site different from the propeptide-recognition site. (+info)Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (3/225)
Two genes, accA1 and accA2, with nearly identical nucleotide sequences were cloned from Streptomyces coelicolor A3(2). The deduced amino acid sequences of the product of these two genes showed high similarity to BcpA2 of Saccharopolyspora erythraea and other biotin-containing proteins from different organisms assumed to be the alpha subunit of a propionyl-CoA carboxylase. A gene, pccB, encoding the carboxyl transferase subunit of this enzyme complex was also characterized. Strains disrupted in accA1 did not show any change in acetyl- or propionyl-CoA carboxylase activity, whilst cell-free extracts of a pccB mutant strain contained a reduced level of propionyl-CoA carboxylase. No mutants in accA2 could be isolated, suggesting that the gene may be essential. Heterologous expression of accA1, accA2 and pccB in Escherichia col and in vitro reconstitution of enzyme activity confirmed that PccB is the beta subunit of a propionyl-CoA carboxylase and that either AccA1 or AccA2 could act as the alpha component of this enzyme complex. The fact that accA2 mutants appear to be inviable suggests that this gene encodes a biotinylated protein that might be shared with other carboxyl transferases essential for the growth of S. coelicolor. (+info)Molecular characterization of the non-biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase. (4/225)
The biotin enzyme, 3-methylcrotonyl-CoA carboxylase (MCCase) (3-methylcrotonyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1. 4), catalyzes a pivotal reaction required for both leucine catabolism and isoprenoid metabolism. MCCase is a heteromeric enzyme composed of biotin-containing (MCC-A) and non-biotin-containing (MCC-B) subunits. Although the sequence of the MCC-A subunit was previously determined, the primary structure of the MCC-B subunit is unknown. Based upon sequences of biotin enzymes that use substrates structurally related to 3-methylcrotonyl-CoA, we isolated the MCC-B cDNA and gene of Arabidopsis. Antibodies directed against the bacterially produced recombinant protein encoded by the MCC-B cDNA react solely with the MCC-B subunit of the purified MCCase and inhibit MCCase activity. The primary structure of the MCC-B subunit shows the highest similarity to carboxyltransferase domains of biotin enzymes that use methyl-branched thiol esters as substrate or products. The single copy MCC-B gene of Arabidopsis is interrupted by nine introns. MCC-A and MCC-B mRNAs accumulate in all cell types and organs, with the highest accumulation occurring in rapidly growing and metabolically active tissues. In addition, these two mRNAs accumulate coordinately in an approximately equal molar ratio, and they each account for between 0.01 and 0.1 mol % of cellular mRNA. The sequence of the Arabidopsis MCC-B gene has enabled the identification of animal paralogous MCC-B cDNAs and genes, which may have an impact on the molecular understanding of the lethal inherited metabolic disorder methylcrotonylglyciuria. (+info)Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase. (5/225)
Using reduced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certain glutamates by adding carbon dioxide to the gamma position of those amino acids. In vertebrates, the modification of glutamate residues of target proteins is facilitated by an interaction between a propeptide present on target proteins and the gamma-glutamyl carboxylase. Previously, the gastropod Conus was the only known invertebrate with a demonstrated vitamin K-dependent carboxylase. We report here the discovery of a gamma-glutamyl carboxylase in Drosophila. This Drosophila enzyme is remarkably similar in amino acid sequence to the known mammalian carboxylases; it has 33% sequence identity and 45% sequence similarity to human gamma-glutamyl carboxylase. The Drosophila carboxylase is vitamin K-dependent, and it has a K(m) toward a model pentapeptide substrate, FLEEL, of about 4 mm. However, unlike the human gamma-glutamyl carboxylase, it is not stimulated by human blood coagulation factor IX propeptides. We found the mRNA for Drosophila gamma-glutamyl carboxylase in virtually every embryonic and adult stage that we investigated, with the highest concentration evident in the adult head. (+info)An acyl-coenzyme A carboxylase encoding gene associated with jadomycin biosynthesis in Streptomyces venezuelae ISP5230. (6/225)
Analysis of a region of chromosomal DNA lying between jadR1 and jadI in the gene cluster for jadomycin biosynthesis in Streptomyces venezuelae ISP5230 detected an ORF encoding 584 amino acids similar in sequence to the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) components of acyl-coenzyme A carboxylases. Multiple sequence alignments of the deduced Jad protein with acyl-coenzyme A carboxylases from various sources located the BC and BCCP components in the N- and C-terminal regions, respectively, of the deduced polypeptides. The organization and amino acid sequence of the deduced polypeptide most closely resembled those in other Gram-positive bacteria broadly classified as actinomycetes. Disrupting the gene, designated jadJ, severely reduced but did not eliminate jadomycin production. The disruption had no effect on growth or morphology of the organism, implying that the product of jadJ is not essential for fatty acid biosynthesis. It is concluded that jadJ supplies malonyl-coenzyme A for biosynthesis of the polyketide intermediate that is eventually processed to form the antibiotic jadomycin B. (+info)A conserved motif within the vitamin K-dependent carboxylase gene is widely distributed across animal phyla. (7/225)
The vitamin K-dependent gamma-glutamyl carboxylase catalyzes the posttranslational conversion of glutamic acid to gamma-carboxyglutamic acid, an amino acid critical to the function of the vitamin K-dependent blood coagulation proteins. Given the functional similarity of mammalian vitamin K-dependent carboxylases and the vitamin K-dependent carboxylase from Conus textile, a marine invertebrate, we hypothesized that structurally conserved regions would identify sequences critical to this common functionality. Furthermore, we examined the diversity of animal species that maintain vitamin K-dependent carboxylation to generate gamma-carboxyglutamic acid. We have cloned carboxylase homologs in full-length or partial form from the beluga whale (Delphinapterus leucas), toadfish (Opsanus tau), chicken (Gallus gallus), hagfish (Myxine glutinosa), horseshoe crab (Limulus polyphemus), and cone snail (Conus textile) to compare these structures to the known bovine, human, rat, and mouse cDNA sequences. Comparison of the predicted amino acid sequences identified a nearly perfectly conserved 38-amino acid residue region in all of these putative carboxylases. In addition, this amino acid motif is also present in the Drosophila genome and identified a Drosophila homolog of the gamma-carboxylase. Assay of hagfish liver demonstrated vitamin K-dependent carboxylase activity in this hemichordate. These results demonstrate the broad distribution of the vitamin K-dependent carboxylase gene, including a highly conserved motif that is likely critical for enzyme function. The vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid appears to be a highly conserved function in the animal kingdom. (+info)A topological study of the human gamma-glutamyl carboxylase. (8/225)
gamma-Glutamyl carboxylase (GC), a polytopic membrane protein found in the endoplasmic reticulum (ER), catalyzes vitamin K-dependent posttranslational modification of glutamate to gamma-carboxyl glutamate. In an attempt to delineate the structure of this important enzyme, in vitro translation and in vivo mapping were used to study its membrane topology. Using terminus-tagged full-length carboxylase, expressed in 293 cells, it was demonstrated that the amino-terminus of the GC is on the cytoplasmic side of the ER, while the carboxyl-terminus is on the lumenal side. In addition, a series of fusions were made to encode each predicted transmembrane domain (TMD) followed by a leader peptidase (Lep) reporter tag, as analyzed by the computer algorithm TOPPRED II. Following in vitro translation of each fusion in the presence of canine microsomes, the topological orientation of the Lep tag was determined by proteinase K digestion and endoglycosidase H (Endo H) cleavage. From the topological orientation of the Lep tag in each fusion, the GC spans the ER membrane at least 5 times, with its N-terminus in the cytoplasm and its C-terminus in the lumen. (+info)
3-Methylcrotonyl-CoA Carboxylase Deficiency (MCCC2-Related) (MCCC2) - Sema4
Human Metabolome Database: Showing metabocard for Vitamin K1 2,3-epoxide (HMDB0002972)
Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme | Plant Physiology
Sch475 00200 : CDS information --- DoBISCUIT
Human Metabolome Database: Showing metabocard for 3-Hydroxyisovalerylcarnitine (HMDB0061189)
Part 09: ORGANIC ACIDS
8-Methyleugenitol - Biofron
rs121714145 - SNPedia
Effects of 2,3,7,8-tetrachlorodibenzo-p-dioxin or 2,2,4,4,5,...
Peter Mayerhofer - University of Surrey - Guildford
A malaria parasite subtilisin propeptide-like protein is a potent inhibitor of the egress protease SUB1 | Biochemical Journal |...
PATCH vkd3d 22/41] vkd3d: Add DXIL test for line tessellation.
PATCH vkd3d 20/41] vkd3d: Add DXIL test for tess control point phase.
Anti-MCCA Antibody (B-7) | SCBT - Santa Cruz Biotechnology
Carboxylated vs. non-carboxylated?
Produktübersicht anti-GGCX Antikörper
Buy Mitsubishi Alik Mccb Price,Size,Weight,Model,Width -Okorder.com
3-methylcrotonyl-CoA carboxylase | definition of 3-methylcrotonyl-CoA carboxylase by Medical dictionary
Evidence for the vitamin K-dependent γ-carboxylation of the first glutamic acid residue in peptide substrates containing a...
EPO - T 0339/98 (Vitamin K-dependent proteins/ELI LILLY) of 18.9.2001
A new fluorogenic peptide substrate for vitamin K-dependent blood coagulation factor, bovine protein C. - NextBio article
Matrix gla protein - Wikipedia
Structure and function of biotin-dependent carboxylases | SpringerLink
Hereditary combined deficiency of the vitamin K-dependent clotting factors | Orphanet Journal of Rare Diseases | Full Text
Pure Encapsulations - Biotin 8 mg - 60 vcaps
VITAMIN B7 - BIOTIN
Propionyl-CoA carboxylase regulator elisa and antibody
New Page 1
Proc - Vitamin K-dependent protein C precursor - Mus musculus (Mouse) - Proc gene & protein
Dietary Intake of Menaquinone Is Associated with a Reduced Risk of Coronary Heart Disease: The Rotterdam Study | cardiohub
Publicações | - CCMAR
anti-PCCB antibody [N2C3] | GeneTex
Expression of MCCC1 in cancer - Summary - The Human Protein Atlas
Members membership FAQs | ACCA | ACCA Global
ACCA Degrees | StudyLink
Drug Interaction Between Paracetamol and Warfarin - Full Text View - ClinicalTrials.gov
PhD MCCA - PhD MCCA
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Penicillium emmonsii
List of Penicillium species MycoBank Straininfo of Penicillium emmonsii Q. Ashton Acton, PhD (2012). Carbon-Carbon Ligases: ...
Ribose-5-phosphate-ammonia ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a ribose-5-phosphate-ammonia ligase (EC 6.3.4.7) is an enzyme that catalyzes the chemical reaction ATP + ribose ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). This enzyme participates in purine metabolism. Reem GH ( ...
Formate-dihydrofolate ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a formate-dihydrofolate ligase (EC 6.3.4.17) is an enzyme that catalyzes the chemical reaction ATP + formate + ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is formate:dihydrofolate ligase (ADP-forming). Drake JC, Baram J, Allegra CJ (1990). "Isolation and ...
Biotin-(methylmalonyl-CoA-carboxytransferase) ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a biotin-[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is biotin:apo[methylmalonyl-CoA:pyruvate carboxytransferase] ligase (AMP-forming). This enzyme participates ...
Imidazoleacetate-phosphoribosyldiphosphate ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... In enzymology, an imidazoleacetate-phosphoribosyldiphosphate ligase (EC 6.3.4.8) is an enzyme that catalyzes a chemical ... this enzyme class is imidazoleacetate:5-phosphoribosyl-diphosphate ligase (ADP- and diphosphate-forming). This enzyme is also ...
Glutamate-methylamine ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... In enzymology, a glutamate-methylamine ligase (EC 6.3.4.12) is an enzyme that catalyzes the chemical reaction ATP + L-glutamate ... Portal: Biology v t e (EC 6.3.4, Enzymes of unknown structure, All stub articles, Ligase stubs). ... this enzyme class is L-glutamate:methylamine ligase (ADP-forming). This enzyme is also called gamma-glutamylmethylamide ...
Phosphoribosylamine-glycine ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. In bacteria, GARS is a ... In addition to similar structure across species, GARS as a whole has a very similar structure to D-alanine:D-alanine ligase, ... Phosphoribosylamine-glycine ligase, also known as glycinamide ribonucleotide synthetase (GARS), (EC 6.3.4.13) is an enzyme that ... The systematic name of this enzyme class is 5-phospho-D-ribosylamine:glycine ligase (ADP-forming). Other names in common use ...
Formate-tetrahydrofolate ligase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. This enzyme ... The systematic name of this enzyme class is formate:tetrahydrofolate ligase (ADP-forming). Other names in common use include: ... In enzymology, a formate-tetrahydrofolate ligase (EC 6.3.4.3) is an enzyme that catalyzes the chemical reaction ATP + formate ... Human genes encoding formate-tetrahydrofolate ligases include: MTHFD1 - cytoplasmic MTHFD1L - mitochondrial As of late 2007, 3 ...
5-formyltetrahydrofolate cyclo-ligase
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... This enzyme participates in one carbon pool by folate. As of late 2007, 5 structures have been solved for this class of enzymes ... In enzymology, a 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) is an enzyme that catalyzes the chemical reaction ATP + 5- ... name of this enzyme class is 5-formyltetrahydrofolate cyclo-ligase (ADP-forming). Other names in common use include 5,10- ...
acetyl-CoA carboxylase)-phosphatase
The systematic name is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase. Krakower GR, Kim KH (March ...
Phenylacetate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... Other names in common use include phenylacetyl-CoA ligase, PA-CoA ligase, and phenylacetyl-CoA ligase (AMP-forming). This ... In enzymology, a phenylacetate-CoA ligase is an enzyme (EC 6.2.1.30) that catalyzes the chemical reaction ATP + phenylacetate ... "Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the ...
Phytanate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... This enzyme is also called phytanoyl-CoA ligase. Muralidharan FN, Muralidharan VB (1986). "Phytanoyl-CoA ligase activity in rat ... In enzymology, a phytanate-CoA ligase (EC 6.2.1.24) is an enzyme that catalyzes the chemical reaction ATP + phytanate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Acid-CoA ligase (GDP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acid-CoA ligase (GDP-forming) (EC 6.2.1.10) is an enzyme that catalyzes the chemical reaction GTP + an acid ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acid:CoA ligase (GDP-forming). Other names in common use include acyl-CoA synthetase ( ...
Butyrate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. This enzyme ... Butyrate-CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme (EC 6.2.1.2) that ... 3-hydroxybutyryl CoA ligase, xenobiotic/medium-chain fatty acid ligase, and short-chain acyl-CoA synthetase. ACSM1 ACSM2A ... This reaction is catalyzed by the HXM-A and HXM-B medium-chain acid:CoA ligases and requires energy in the form of ATP. ... The ...
6-carboxyhexanoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 6-carboxyhexanoate-CoA ligase (EC 6.2.1.14) is an enzyme that catalyzes the chemical reaction ATP + 6- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is 6-carboxyhexanoate:CoA ligase (AMP-forming). Other names in common use include 6- ...
Succinate-CoA ligase (ADP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (ADP-forming). Other names in common use include succinyl-CoA ...
Anthranilate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 2-aminobenzoate-CoA ligase, 2-aminobenzoate-coenzyme A ligase, and 2-aminobenzoate coenzyme A ligase. This enzyme participates ... In enzymology, an anthranilate-CoA ligase (EC 6.2.1.32) is an enzyme that catalyzes the chemical reaction ATP + anthranilate + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, Anthranilates, All stub articles, Ligase stubs). ...
Citrate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a citrate-CoA ligase (EC 6.2.1.18) is an enzyme that catalyzes the chemical reaction ATP + citrate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... CoA ligase, and citrate thiokinase. This enzyme participates in citric acid cycle. Lill U, Schreil A, Eggerer H (1982). " ...
3-alpha,7-alpha-dihydroxy-5-beta-cholestanate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... DHCA-CoA ligase, and 3alpha,7alpha-dihydroxy-5beta-cholestanate:CoA ligase (AMP-forming). This enzyme participates in bile acid ... In enzymology, a 3α,7α-dihydroxy-5β-cholestanate-CoA ligase (EC 6.2.1.28) is an enzyme that catalyzes the chemical reaction ATP ... 12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver". Journal of Lipid Research. 29 (8): 997-1004. PMID ...
Acetate-CoA ligase (ADP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ...
Propionate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a propionate-CoA ligase (EC 6.2.1.17) is an enzyme that catalyzes the chemical reaction ATP + propanoate + CoA ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is propanoate:CoA ligase (AMP-forming). This enzyme is also called propionyl-CoA ...
4-chlorobenzoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a 4-chlorobenzoate-CoA ligase (EC 6.2.1.33) is an enzyme that catalyzes the chemical reaction 4-chlorobenzoate ... Loffler F, Muller R, Lingens F (1992). "Purification and properties of 4-halobenzoate-coenzyme A ligase from Pseudomonas sp. ... systematic name of this enzyme class is 4-chlorobenzoate:CoA ligase. This enzyme participates in 2,4-dichlorobenzoate ...
4-hydroxybenzoate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... 4-hydroxybenzoate-coenzyme A ligase (AMP-forming), 4-hydroxybenzoyl coenzyme A synthetase, and 4-hydroxybenzoyl-CoA ligase. ... In enzymology, a 4-hydroxybenzoate-CoA ligase (EC 6.2.1.27) is an enzyme that catalyzes the chemical reaction ATP + 4- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Succinate-CoA ligase (GDP-forming)
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) is an enzyme that catalyzes the chemical reaction GTP + ... Portal: Biology v t e (EC 6.2.1, Enzymes of known structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is succinate:CoA ligase (GDP-forming). Other names in common use include succinyl-CoA ...
Glutarate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a glutarate-CoA ligase (EC 6.2.1.6) is an enzyme that catalyzes the chemical reaction ATP + glutarate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is glutarate:CoA ligase (ADP-forming). Other names in common use include glutaryl-CoA ...
Malate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is malate:CoA ligase (ADP-forming). Other names in common use include malyl-CoA synthetase ...
Dicarboxylate-CoA ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a dicarboxylate-CoA ligase (EC 6.2.1.23) is an enzyme that catalyzes the chemical reaction ATP + an alphaomega- ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is omega-dicarboxylate:CoA ligase (AMP-forming). Other names in common use include ...
Long-chain-fatty-acid-luciferin-component ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-luciferin-component ligase (EC 6.2.1.19) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl- ...
Long-chain-fatty-acid-(acyl-carrier-protein) ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... In enzymology, a long-chain-fatty-acid-[acyl-carrier-protein] ligase (EC 6.2.1.20) is an enzyme that catalyzes the chemical ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ... systematic name of this enzyme class is long-chain-fatty-acid:[acyl-carrier-protein] ligase (AMP-forming). Other names in ...
citrate (pro-3S)-lyase) ligase
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The ... HS-citrate lyase ligase, and acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming). This enzyme participates in two- ... In enzymology, a [citrate (pro-3S)-lyase] ligase (EC 6.2.1.22) is an enzyme that catalyzes the chemical reaction ATP + acetate ... Portal: Biology v t e (EC 6.2.1, Enzymes of unknown structure, All stub articles, Ligase stubs). ...
Carbon-Oxygen Ligases | Profiles RNS
"Carbon-Oxygen Ligases" by people in UAMS Profiles by year, and whether "Carbon-Oxygen Ligases" was a major or minor topic of ... "Carbon-Oxygen Ligases" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Carbon-Oxygen Ligases" by people in Profiles over the past ten years. ... Below are MeSH descriptors whose meaning is more general than "Carbon-Oxygen Ligases". ...
Carbon carbon ligase - Chemwatch
PCCB gene: MedlinePlus Genetics
KEGG T08195: CLAFUR5 06324
6.4 Forming carbon-carbon bonds. 6.4.1 Ligases that form carbon-carbon bonds (only sub-subclass identified to date). 6.4.1.2 ... 6. Ligases. 6.3 Forming carbon-nitrogen bonds. 6.3.4 Other carbon-nitrogen ligases. 6.3.4.14 biotin carboxylase. CLAFUR5_06324 ... 2.1 Transferring one-carbon groups. 2.1.3 Carboxy- and carbamoyltransferases. 2.1.3.15 acetyl-CoA carboxytransferase. CLAFUR5_ ...
KEGG ORTHOLOGY: K12709
6. Ligases. 6.3 Forming carbon-nitrogen bonds. 6.3.1 Acid-D-ammonia (or amine) ligases (amide synthases). 6.3.1.15 8- ... Ligases;. Forming carbon-nitrogen bonds;. Acid-D-ammonia (or amine) ligases (amide synthases). BRITE hierarchy. ... novobiocin ligase;. novobiocic acid synthetase (misleading);. 8-desmethyl-novobiocic acid synthetase;. 8-demethylnovobiocic ... 3-dimethylallyl-4-hydroxybenzoate:3-amino-4,7-dihydroxycoumarin ligase (AMP-forming). ...
Publikationen der Gruppe | Max-Planck-Institut für Molekulare Pflanzenphysiologie
SMART: TilS C domain annotation
nucleotide binding (GO:0000166), ligase activity, forming carbon-nitrogen bonds (GO:0016879), ATP binding (GO:0005524). ... The aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of an amino acid to its cognate ... nucleophilically attacksthe C2 carbon from the rear. Escherichia coli TilS (called MesJ) has anadditional CTD, which may ... adenylationof C34 and lysine attack on the C2 carbon. Conserved amino acid residuesare clustered around the NTD central hole. ...
Find Research outputs - Discovery - the University of Dundee Research Portal
ExplorEnz: EC 6.3.4.14
accC (gene name); biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). ... biotin carboxyl-carrier protein]-biotin-N6-L-lysine:hydrogencarbonate ligase (ADP-forming). ... ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. ...
Solyc07g020710.3.1 details
Center for Structural Genomics of Infectious Diseases - Deposits
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases and ... The 2.0 A crystal structure of D-alanine--D-alanine ligase from Bacillus anthracis complexed with ATP revealed a dimer with ... Crystal Structure of D-alanine--D-Alanine Ligase from Bacillus anthracis complexed with ATP. (tree view) ...
GMP synthase [glutamine-hydrolyzing] (P38625) - Yeast Metabolome Database
DeCS
Carbon-Oxygen Ligases - Preferred Concept UI. M0029291. Scope note. Enzymes that catalyze the joining of two molecules by the ... Carbono-Oxigênio Ligases Descriptor French: Carbon-oxygen ligases Entry term(s):. Carbon Oxygen Ligases. Ligases, Carbon-Oxygen ... do not confuse with CARBON-OXYGEN LYASES. Allowable Qualifiers:. AD administration & dosage. AE adverse effects. AI antagonists ... Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.. ...
CRP66869 details
IMSEAR at SEARO: Search
ZFIN Chebi: EC 6.3.5.1 [NAD(+) synthase (glutamine-hydrolysing)] inhibitor
EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor Show first 5 Terms ... Any EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor that interferes with the action of NAD(+) ... EC 6.3.5.* (carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor ... deamido-NAD(+):L-glutamine amido-ligase (AMP-forming) inhibitor. *deamido-NAD(+):L-glutamine amido-ligase (AMP-forming) ...
protein deficiency
6.3.4.9: biotin-[methylmalonyl-CoA-carboxytransferase] ligase - BRENDA Enzyme Database
6.3 Forming carbon-nitrogen bonds. 6.3.4 Other carbon-nitrogen ligases. 6.3.4.9 biotin-[methylmalonyl-CoA-carboxytransferase] ... ligase (AMP-forming), Biotin-[methylmalonyl-CoA-carboxyltransferase] ligase ... 6.3.4.9: biotin-[methylmalonyl-CoA-carboxytransferase] ligase. This is an abbreviated version!. For detailed information about ... methylmalonyl-CoA-pyruvate apocarboxyltransferase ligase (AMP), Biotin-apotranscarboxylase synthetase, biotin:apo[methylmalonyl ...
DeCS Ingl s
Structural Biochemistry/Enzyme - Wikibooks, open books for an open world
Ligases are used in catalysis where two substrates are litigated and the formation of carbon-carbon, carbon-sulfide, carbon- ... Ligases Catalyze bond formation coupled with ATP hydrolysis. Citric acid synthetase Lyases Catalyze a group elimination in ... The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. Then the carbonic acid becomes a ... 2. Carbonic Anhydrase (metalloenzymes) These enzymes catalyzes the rapid interconversion of carbon dioxide and water to ...
lcl|LHPG02000004.1 cds PRW59070.1 7315 details
AGT26296 details
LOC Os01g19960.1 details
UMLS. CSP-HL7-ICD9CM-NCI-NDFRT-RXNORM - Terms starting with 'U' - MEDINDEX.AM
carbon nitrogen ligase; 3. glucan [group of polysaccharides composed of repeating glucose units; they can consist of branched ... It causes the carbon dioxide produced during dough fermentation to be retained by the dough in a manner which provides the ... 49. glutamate ammonia ligase [An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and ... biosynthesis of glucose from 3-carbon precursors, including aminoacids (this is the basis of protein breakdown during ...
Subject: basic-leucine zipper transcription factors / Subject term: basic-leucine zipper transcription factors - PubAg Search...
... carbon monoxide; food intake; gastric acid; glutamate-cysteine ligase; heme oxygenase (biliverdin-producing); iron; quinones; ... glutamate-cysteine ligase, and NAD(P)H quinone dehydrogenase 1, among which HO-1 is an enzyme catalyzing the degradation of ... heme.producing biliverdin, ferrous iron, and carbon monoxide. In the s .... DOI:. 10.1016/j.abb.2020.108466. https://doi.org/ ...
Seed Viewer - Organism
fig,[email protected]~Central [email protected]^Central metabolism - no [email protected]^EC 6.4.1.- Ligases that form carbon-carbon ... fig,[email protected]~Central [email protected]^Central metabolism - no [email protected]^EC 6.4.1.- Ligases that form carbon-carbon ... Ligases that form carbon-carbon [email protected]^Acetyl-coenzyme A carboxyl transferase beta chain (EC 6.4.1.2)@^fig,[email protected]~ ... Ligases that form carbon-carbon [email protected]^Acetyl-coenzyme A carboxyl transferase alpha chain (EC 6.4.1.2)@^fig,[email protected]~ ...
WormFlux: mechanistic analysis of C. elegans metabolism
Bio2Vec
Finding step pccB for L-valine catabolism in Shewanella loihica PV-4
Curated sequence Q3J4E3: Propionyl-CoA carboxylase beta chain; PCCase; Propanoyl-CoA:carbon dioxide ligase; EC 6.4.1.3. ... Curated sequence P53003: Propionyl-CoA carboxylase beta chain; PCCase; Propanoyl-CoA:carbon dioxide ligase; EC 6.4.1.3 ... carbon dioxide ligase subunit beta; EC 6.4.1.3. propionyl-CoA carboxylase β chain, mitochondrial (EC 6.4.1.3) ... carbon dioxide ligase subunit beta; EC 6.4.1.3. propionyl-CoA carboxylase (EC 6.4.1.3) ...
Glutamine as amido-N-donor1
- carbon-nitrogen ligases with glutamine as amido-N-donor) inhibitor that interferes with the action of NAD(+) synthase (glutamine-hydrolysing) (EC 6.3.5.1). (zfin.org)
Forming carbon-nitrogen bonds2
- This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases and participates in d-alanine metabolism and peptidoglycan biosynthesis. (csgid.org)
- Ligases, Forming carbon-nitrogen bonds, Acid--D-amino-acid ligases (peptide synthases). (uma.es)
Bonds3
- For example, the protein molecules that control the functions of all living organisms are held together by amide bonds, which form a link between the carbon and nitrogen atoms of amino acid building blocks. (indiaeducationdiary.in)
- The ligase enzymes provide a cleaner more efficient and rapid way to construct amide bonds. (indiaeducationdiary.in)
- Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups. (bvsalud.org)
Subunit1
- Our work identified a novel mammalian prenyltransferase which we named GGtase3 that modifies FBXL2, an E3 ligase subunit, with geranylgeranylation (a 20-carbon lipid PTM) for localization to membrane compartments. (kuchaylab.org)
Ubiquitin ligases4
- Often substrate degradation via ubiquitin ligases is regulated for precision and fine control. (kuchaylab.org)
- We are currently involved in functional characterization of GGtase3 and extending our studies for functional characterization of PTMs involving membrane bound E3 ubiquitin ligases. (kuchaylab.org)
- We seek to elucidate the spatiotemporal mechanistic understating for the specificity of the ubiquitylation reaction by E3 ubiquitin ligases. (kuchaylab.org)
- In cells, PROTAC molecules can recognize and selectively bind target proteins, recruit specific E3 ubiquitin ligases, and form a "target protein-PROTAC-E3 ubiquitin ligase" ternary complex. (cd-bioparticles.net)
Nitrogen7
- Expression of Formate-Tetrahydrofolate Ligase Did Not Improve Growth but Interferes With Nitrogen and Carbon Metabolism of Synechocystissp. (mpg.de)
- All these processes are tightly regulated by proteins and microRNA in response to both external and internal nitrogen levels, carbon status of the plant and hormones. (scirp.org)
- Among macro nutrients, nitrogen is next to carbon in importance to plants. (scirp.org)
- Flux Balance Analysis (FBA) of the model resulted in balanced carbon, nitrogen, proton, energy and redox states under both light and dark conditions. (biomedcentral.com)
- The subsequent accumulation of TAG under nitrogen deprivation was a consequence of the reallocation of carbon, nitrogen sources, and lipids, rather than an up-regulation of TAG biosynthesis genes. (biomedcentral.com)
- on the other hand, nitrogen deprivation induced the up-regulation of cell autophagy and ubiquitin-mediated protein proteolysis which resulted in a recycling of preformed protein nitrogen and carbon. (biomedcentral.com)
- One of the most important protection mechanisms is the reallocation of limited carbon, nitrogen, and energy resources to optimize growth and metabolism [ 7 ]. (biomedcentral.com)
Biotin2
- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15 , biotin-[biotin carboxyl-carrier protein] ligase. (enzyme-database.org)
- For detailed information about biotin-[methylmalonyl-CoA-carboxytransferase] ligase, go to the full flat file . (brenda-enzymes.org)
Biosynthesis2
- Starch is a repository of carbon which is later used during the dark phase as the primary carbon source for biomass formation [ 2 ] and fuelling of sucrose biosynthesis and its transport. (biomedcentral.com)
- For more information, see the paper from 2019 on GapMind for amino acid biosynthesis, the paper from 2022 on GapMind for carbon sources, or view the source code . (lbl.gov)
Protein8
- A pyridoxal-phosphate protein that catalyzes the alpha-decarboxylation of L-glutamic acid to form gamma-aminobutyric acid and carbon dioxide. (medindex.am)
- Ubiquitin--protein ligase. (uma.es)
- In a recent article in the Journal of Biological Chemistry , Hanjie Jiang and collaborators at Brigham and Women's Hospital describe using protein microarray technology as a platform to identify WWP2 substrates using an activated version of this ligase. (asbmb.org)
- Several physio-molecular processes are initiated during this phase, including protein synthesis and the resumption of respiratory activities , observed by a significant increase in oxygen consumption and carbon dioxide release. (globalplantcouncil.org)
- PROTAC is a bifunctional molecule composed of three parts: one end is the target protein binding ligand, the other end is the E3 ubiquitin ligase ligand, and the middle is the linker chain. (cd-bioparticles.net)
- Afterwards, E3 ubiquitin ligase and E2 ubiquitin conjugating enzyme work together to ubiquitinate the target protein. (cd-bioparticles.net)
- After PROTAC completes the ubiquitination labeling of a target protein, it can be separated from the target protein and E3 ubiquitin ligase and continue to label the next protein. (cd-bioparticles.net)
- Degradation of CIC protein following lack of ATXN1L was as an alternative noticed to be mediated by the E3 ubiquitin ligase TRIM25 which was additional validated utilizing glioma-derived cell traces and the TCGA breast carcinoma and liver hepatocellular carcinoma cohorts. (ataxin.com)
Metabolism3
- The tricarboxylic acid, or TCA, cycle is essential to carbon metabolism. (asbmb.org)
- Furthermore, the structured metabolic model should take into account major pathways of primary metabolism such as sugar metabolism, central carbon metabolisms, photosynthesis, photorespiration, energy and redox metabolism, proton turnover, sucrose translocation from source to sink tissues and biomass growth. (biomedcentral.com)
- In future, we will use the model to recognize cause-effect relationships and describe regulatory processes in carbon metabolism and transport. (biomedcentral.com)
Substrates3
- Identifying new substrates for a ubiquitin ligase. (asbmb.org)
- Although, PTMs on substrates are well studied, PTMs on E3 ligases and how they regulate the UPS have not been established. (kuchaylab.org)
- The new findings have demonstrated that the ligase enzymes can accept many substrates, but in some cases proved too unstable for practical use. (indiaeducationdiary.in)
Enzyme2
- One Cohesive-End Ligation Unit (CEU) is defined as the amount of enzyme required to give 50 % ligation of Hin d III fragments of λ DNA (5' DNA termini concentration of 0.12 μM, 300 μg/ml) in a total reaction volume of 20 μl in 30 minutes at 16 °C in 1x T4 DNA Ligase Reaction Buffer. (jenabioscience.com)
- However, when they used X-ray crystallography to determine the structure of one of the ligase enzymes, they realised that the enzyme active site was relatively open and could accommodate a much wider range of substrate building blocks for production of pharmaceuticals. (indiaeducationdiary.in)
Putative1
- In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain. (embl.de)
Fixation5
- Awakening a latent carbon fixation cycle in Escherichia coli. (mpg.de)
- The origin of carbon fixation is a fundamental question in astrobiology. (researchgate.net)
- While the Calvin cycle is the most active on the modern Earth, the reductive TCA cycle (rTCA) pathway for carbon fixation has been proposed to have played an important role in early evolution. (researchgate.net)
- Fundamental to astrobiology is origin of autotrophy with reductive TCA cycle (rTCA) being often proposed as a primordial carbon fixation pathway. (researchgate.net)
- Design and analysis of synthetic carbon fixation pathways. (southcoastbiosciencesdtp.ac.uk)
Bacteria2
- They found a family of ligase enzymes that bacteria use to make amide containing toxins that kill plants. (indiaeducationdiary.in)
- For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. (lbl.gov)
Proteins1
- The HECT E3 ligase WWP2 targets lysine residues for ubiquitination in a broad range of proteins involved in different physiological processes. (asbmb.org)
Catalyzes1
- T4 DNA Ligase catalyzes the formation of a phosphodiester bond between juxtaposed 5' phosphate and 3'-hydroxyl termini in duplex DNA or RNA. (jenabioscience.com)
Chemicals1
- The production of fuels and commodities as well as fine chemicals by bacterial C 1 -assimilation (CO 2 -valorization) will compete with lignin valorization and plastics upcycling in a future circular carbon economy. (southcoastbiosciencesdtp.ac.uk)
Atoms1
- Residual gas diffuses away, whereas free carbon atoms dissolve into the nanoparticles and then segregate to the catalyst surface to form nanotubes [44]. (a-inhibitor.com)
Growth2
- The authors deleted mqo from Mycobacterium smegmatis, an environmental saprophyte - that is, it feeds on decaying matter - that lacks Mdh in its genome and found that Mqo is essential for growth on nonfermentable carbon sources. (asbmb.org)
- Complementation experiments with a heterologous Mdh from Mycobacterium tuberculosis shortened the delayed growth on fermentable carbon sources and restored growth on nonfermentable carbon sources at a reduced growth rate. (asbmb.org)
Biomass2
- In growing plants, sucrose is the most widespread sugar used to supply both carbon and energy from 'source' tissues (e.g. autotrophic mesophyll) to 'sink' tissues (e.g. heterotrophic roots, growing shoots or reproductive organs) to build up a biomass [ 1 ]. (biomedcentral.com)
- Woody biomass can also be utilized as a sustainable and carbon-neutral resource for bioenergy [1]. (researchsquare.com)
Molecules1
- Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. (uams.edu)
Bind1
- DNA ligase, activated following imbibition, is involved to bind together broken pieces of DNA. (globalplantcouncil.org)
Component1
- One potential novel T. brucei drug target is RNA editing ligase 1 ( Tb REL1), a critical component of a unique mitochondrial RNA-editing complex called the editosome [ 5 ]. (biomedcentral.com)
Family1
- New research published today, in Nature , describes a new family of enzymes (ligases) which can assemble the key chemical building blocks required for pharmaceutical production. (indiaeducationdiary.in)
Acid1
- The process involves binding water to carbon dioxide and deprotonating it into carbonic acid. (wikibooks.org)
Critical1
- For example, we are investigating FBXL2, an E3 ligase complex that regulates critical signaling networks operating from membrane compartments. (kuchaylab.org)
Synthesis1
- This paper describes the recent progress at Nottingham towards the exploitation of the unique properties of scCO 2 (supercritical carbon dioxide) for the preparation of polymeric scaffolds for tissue engineering applications and new devices for controlled drug delivery, as well as the synthesis of novel block copolymers by the combination of eROP (enzymatic ring opening polymerization) and controlled polymerization methods for the potential use as drug carriers. (portlandpress.com)
Sources1
- The authors also determined that mqo mutants grew more slowly on fermentable carbon sources. (asbmb.org)
Beta1
- The 2.0 A crystal structure of D-alanine--D-alanine ligase from Bacillus anthracis complexed with ATP revealed a dimer with each monomer consisting of three alpha-beta domains. (csgid.org)