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
Drug Interaction Between Paracetamol and Warfarin - Full Text View - ClinicalTrials.gov
PhD MCCA - PhD MCCA
Blood Coagulation Proteins - Weight Loss - Barnard Health Care
The Record: External Scholarship List
Tom Prophet Hsiung » P2X1
Biotin 5000 ,Allergy Research Group,60 Vegetarian Caps
HEK-293T Cells Human PCCB Lysate | ABIN1332882
1W5C | Genus
PROSITE
Publikationen der Gruppe | Max-Planck-Institut für Molekulare Pflanzenphysiologie
Publikationen der Gruppe | Max-Planck-Institut für Molekulare Pflanzenphysiologie
Learning for the future | ACCA Global
omicron pharmaceuticals
Vivitrol Program Information | Drug Rehab | Alcohol Rehabilitation Center - CT | MCCA
propionyl-CoA carboxylase - oi
Mutagenetix > Incidental...
Human Factor X - Creative Enzymes
Reactome | Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
GGCX - PCR Primer Pair - SYBR | PrimePCR | Bio-Rad
Arabidopsisphosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed...
Hemorrhagic stroke - WikEM
Intracranial hemorrhage (main) - WikEM
Michigan Community College Association
Protein S human - DrugBank
Haematological · Part One
ACCA Revision Series: Managing People Paper 1.3 : ACCA : 9780748353071
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Carboxylated nitrile butadiene rubber | Clwyd Compounders
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 ...
Acetyl-CoA carboxylase
Ligases: carbon-carbon ligases (EC 6.4). Biotin dependent carboxylation. *Pyruvate carboxylase. *Acetyl-CoA carboxylase ...
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 ...
Penicillium emmonsii
List of Penicillium species MycoBank Straininfo of Penicillium emmonsii Q. Ashton Acton, PhD (2012). Carbon-Carbon Ligases: ...
Acetone carboxylase
... specifically those forming carbon-carbon bonds. The systematic name of this enzyme class is acetone:carbon-dioxide ligase (AMP- ... This enzyme belongs to the family of ligases, ...
2-oxoglutarate carboxylase
This enzyme belongs to the family of ligases, specifically those forming carbon-carbon bonds. The systematic name of this ...
Biotin carboxylase
The systematic name of this enzyme class is biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). This enzyme is ... This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. ...
Nicotinate phosphoribosyltransferase
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of ... this enzyme class is 5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) . Other names in ...
Urea carboxylase
The systematic name of this enzyme class is urea:carbon-dioxide ligase (ADP-forming). Other names in common use include urease ... This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. ...
5-(carboxyamino)imidazole ribonucleotide synthase
The systematic name of this enzyme class is 5-amino-1-(5-phospho-D-ribosyl)imidazole:carbon-dioxide ligase (ADP-forming). Other ... This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. ...
Carboxylation
In the EC scheme, such carboxylases are classed under EC 6.3.4, "Other Carbon-Nitrogen Ligases". Another example is the ... Braunstein, Pierre; Matt, Dominique; Nobel, Dominique (August 1988). "Reactions of Carbon Dioxide with Carbon-Carbon Bond ... Carbon-based life originates from carboxylation that couples atmospheric carbon dioxide to a sugar. The process is usually ... Carboxylation is a chemical reaction in which a carboxylic acid group is produced by treating a substrate with carbon dioxide. ...
Dethiobiotin synthase
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... carbon-dioxide cyclo-ligase (ADP-forming). This enzyme is also called desthiobiotin synthase. This enzyme participates in ...
acetyl-CoA carboxylase)-phosphatase
The systematic name of this enzyme class is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase. ...
carboxyethyl)arginine beta-lactam-synthase
This enzyme belongs to the family of ligases, specifically the cyclo-ligases, which form carbon-nitrogen bonds. The systematic ... arginine cyclo-ligase (AMP-forming). This enzyme participates in clavulanic acid biosynthesis. Miller, M. T.; Bachmann, B. O.; ... name of this enzyme class is L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming). This enzyme is also called L-2-N-(2- ...
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- ...
Acetophenone carboxylase
... (EC 6.4.1.8) is an enzyme with systematic name acetophenone:carbon-dioxide ligase (ADP-forming). This ...
Glutathione synthetase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... "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 ... Galperin MY, Koonin EV (1997). "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity". ...
Carnosine synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... The gene encoding the Carnosine synthase is ATPGD1, a member of the "ATP-grasp family" of ligases. Because of its involvement ... peptide synthases). The systematic name of this enzyme class is 'L-histidine:beta-alanine ligase (AMP-forming)' (incorrect on ...
Trypanothione synthase
Its C-terminal domain is a synthetase and has an ATP-grasp family fold that is usually found in carbon-nitrogen ligases. The N- ... This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is glutathionylspermidine:glutathione ligase (ADP-forming ...
Tetrahydrofolate synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... L-glutamate gamma-ligase (ADP-forming), tetrahydropteroyl-[gamma-Glu]n:L-glutamate gamma-ligase, and (ADP-forming). This enzyme ... Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437-52. doi:10.1016 ... L-glutamate gamma-ligase (ADP-forming). Other names in common use include folylpolyglutamate synthase, folate polyglutamate ...
Homoglutathione synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteine:beta-alanine ligase (ADP-forming). ...
Aerobactin synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is citrate:N6-acetyl-N6-hydroxy-L-lysine ligase (ADP-forming). ... This enzyme is also called citrate:6-N-acetyl-6-N-hydroxy-L-lysine ligase (ADP-forming). This enzyme participates in lysine ...
Indoleacetate-lysine synthetase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... L-lysine ligase (ADP-forming). Glass NL, Kosuge T (1986). "Cloning of the gene for indoleacetic acid-lysine synthetase from ... peptide synthases). The systematic name of this enzyme class is (indol-3-yl)acetate:L-lysine ligase (ADP-forming). This enzyme ...
Dihydrofolate synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... Cossins EA, Chen L (1997). "Folates and one-carbon metabolism in plants and fungi". Phytochemistry. 45 (3): 437-52. doi:10.1016 ... L-glutamate ligase (ADP-forming), and DHFS. This enzyme participates in folate biosynthesis. As of late 2007, 3 structures have ... peptide synthases). The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming). Other ...
Gamma-glutamylhistamine synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases ( ... peptide synthases). The systematic name of this enzyme class is L-glutamate:histamine ligase. Other names in common use include ...
Asparaginyl-tRNA synthase (glutamine-hydrolysing)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). Other names in common use ... include Asp-AdT, Asp-tRNAAsn amidotransferase, aspartyl-tRNAAsn amidotransferase, and Asn-tRNAAsn:L-glutamine amido-ligase (ADP ...
GMP synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). Other names in ...
Glutathionylspermidine synthase
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ... ligases (amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase ( ... spermidine ligase (ADP-forming). This enzyme participates in glutathione metabolism. It employs one cofactor, magnesium. As of ...
NAD+ synthase (glutamine-hydrolysing)
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with ... The systematic name of this enzyme class is deamido-NAD+:L-glutamine amido-ligase (AMP-forming). Other names in common use ...
Phosphoribosylformylglycinamidine synthase
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 ...
Carbon-Nitrogen Ligases | Journal of Bacteriology
Enzyme Commission (EC): Other carbon--nitrogen ligases
Forming carbon-nitrogen bonds [6.3] <5>. (59,78). (58,59,38). 0: Other carbon--nitrogen ligases [6.3.4] <24>. (28,31). (27,28, ... Phosphoribosylamine--glycine ligase [6.3.4.13]. (6,6). (6,6,6). - 1: Ribose-5-phosphate--ammonia ligase [6.3.4.7]. (0,0). (0,0, ... ligase ,, Biotin--[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase ,, Biotin--[biotin carboxyl-carrier protein] ligase. ... Glutamate--methylamine ligase [6.3.4.12]. (0,0). (0,0,0). - 1: Imidazoleacetate--phosphoribosyldiphosphate ligase [6.3.4.8]. (0 ...
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. ...
Network Portal - Function ligase activity, forming carbon-nitrogen bonds
ligase activity, forming carbon-nitrogen bonds. id: GO:0016879. name: ligase activity, forming carbon-nitrogen bonds. namespace ... Description: Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, ... acid-amino acid ligase activity. GO:0016882. cyclo-ligase activity. GO:0016884. carbon-nitrogen ligase activity, with glutamine ... acid-ammonia (or amide) ligase activity. GO:0016881. ... citrate-L-glutamate ligase activity. Parent Functions. id. name ...
Aminoacyl tRNA synthetase - Wikipedia
pafA - Pup--protein ligase - Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) - pafA gene & protein
ligase activity, forming carbon-nitrogen bonds Source: InterPro. *magnesium ion binding Source: UniProtKB-UniRule ... Belongs to the Pup ligase/Pup deamidase family. Pup-conjugating enzyme subfamily.UniRule annotation. Manual assertion according ... sp,D2ATU8,PAFA_STRRD Pup--protein ligase OS=Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) OX= ...
Alanine-tRNA Ligase | Harvard Catalyst Profiles | Harvard Catalyst
Carbon-Oxygen Ligases [D08.811.464.263]. *Amino Acyl-tRNA Synthetases [D08.811.464.263.200] ... "Alanine-tRNA Ligase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Alanine-tRNA Ligase" by people in Harvard Catalyst Profiles by ... Below are the most recent publications written about "Alanine-tRNA Ligase" by people in Profiles. ...
Glutamate-Cysteine Ligase
Summary Report | CureHunter
Glutamate-Cysteine Ligase: One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma- ... Ligases: 2113*Carbon-Nitrogen Ligases*Peptide Synthases: 6*Glutamate-Cysteine Ligase: 110*human glutamate-cysteine ligase ... Glutamate-Cysteine Ligase. Subscribe to New Research on Glutamate-Cysteine Ligase One of the enzymes active in the gamma- ... Glutamylcysteine Synthetase; Glutamate Cysteine Ligase; Ligase, Glutamate-Cysteine; Synthetase, Glutamylcysteine; Synthetase, ...
Phenylalanine-tRNA Ligase - RightDiagnosis.com
Phenylalanine-tRNA Ligase information including symptoms, causes, diseases, symptoms, treatments, and other medical and health ... Ligase Terms associated with Phenylalanine-tRNA Ligase:. Terms Similar to Phenylalanine-tRNA Ligase:. *Phenylalanyl T RNA ... Introduction: Phenylalanine-tRNA Ligase. Description of Phenylalanine-tRNA Ligase. Phenylalanine-tRNA Ligase: An enzyme that ... Hierarchical classifications of Phenylalanine-tRNA Ligase. The following list attempts to classify Phenylalanine-tRNA Ligase ...
Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide
Carboxylase overexpression effects full carboxylation but poor release and secretion of factor IX: implications for the release...
Metal-free Photocatalysts for the C-H Bond Oxygenation Reactions Using Oxygen as the Oxidant.
Carbon-oxygen Ligases. Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1. ... Carbon-oxygen Lyases. Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. ... A protocol for three-component reactions of cyclic ethers, α-diazo esters, and weak nitrogen, oxygen, carbon, and sulfur ...
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 ... Carbon-carbon Double Bond Isomerases. Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to ... enzymes shifting a carbon-carbon double bond (CARBON-CARBON DOUBLE BOND ISOMERASES), and enzymes transposing S-S bonds (SULFUR- ...
PCCA gene: MedlinePlus Genetics
PCCB gene: MedlinePlus Genetics
Human Metabolome Database: Showing Protein E3 ubiquitin-protein ligase UBR2 (HMDBP09274)
ligase activity, forming carbon-nitrogen bonds. acid-amino acid ligase activity. ubiquitin-protein ligase activity. ... E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N ... Kume K, Iizumi Y, Shimada M, Ito Y, Kishi T, Yamaguchi Y, Handa H: Role of N-end rule ubiquitin ligases UBR1 and UBR2 in ... Showing Protein E3 ubiquitin-protein ligase UBR2 (HMDBP09274). IdentificationBiological propertiesGene propertiesProtein ...
Human Metabolome Database: Showing Protein Asparagine--tRNA ligase, cytoplasmic (HMDBP00611)
Human Metabolome Database: Showing Protein Threonine--tRNA ligase, mitochondrial (HMDBP09249)
Transcriptome analysis reveals the activation of neuroendocrine-immune system in shrimp hemocytes at the early stage of WSSV...
Identification of biomarkers for amyotrophic lateral sclerosis by comprehensive analysis of exosomal mRNAs in human...
ligase activity, forming carbon-nitrogen bonds. down. 2.30E-09. acid-amino acid ligase activity ... Decrease in ligase activity was ranked at the top (Table 3). Subsequently, decreases in response to oxidative stress and ... ubiquitin-protein ligase activity were included. Next, pathway analysis was also performed, by IPA. As in GO analysis, protein ...
Propionyl-CoA carboxylase alpha chain - Myxococcus xanthus
Von Hippel-Lindau tumor suppressor - wikidoc
6.2: Carbon-Sulfur. *Succinyl coenzyme A synthetase. *Acetyl-CoA synthetase. *Long-chain-fatty-acid-CoA ligase ... Kamura T, Conaway JW, Conaway RC (2002). "Roles of SCF and VHL ubiquitin ligases in regulation of cell growth". Prog. Mol. ... The main action of the VHL protein is thought to be its E3 ubiquitin ligase activity that results in specific target proteins ... and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible ...
SWISSPROT: A4F6R8 SACEN
Mycobacterium tuberculosis FadD28 protein
Summary Report | CureHunter
TIGR03686
GO:0016879: ligase activity, forming carbon-nitrogen bonds molecular_function. GO:0019941: modification-dependent protein ... Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a ... Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady- ... RN [2] RM PMID:22910360 RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification ...
Penicillium emmonsii - Wikipedia
Monoclonal Antibody Cardiac Muscle Development to Monoclonal Antibody Branched-Chain-Amino-Acid Transaminase Activity from Cell...
Ribose-5-phosphate-ammonia ligase - Wikipedia
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 ... this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). Other names in common use include 5-phosphoribosylamine ...
KEGG T00827: ECED1 0655
Enzyme23
- 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)
- An aminoacyl-tRNA synthetase ( aaRS or ARS ), also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its tRNA . (wikipedia.org)
- In enzymology, a ribose-5-phosphate-ammonia ligase (EC 6.3.4.7) is an enzyme that catalyzes the chemical reaction ATP + ribose 5-phosphate + NH3 ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate + 5-phosphoribosylamine The 3 substrates of this enzyme are ATP, ribose 5-phosphate, and NH3, whereas its 3 products are ADP, phosphate, and 5-phosphoribosylamine. (wikipedia.org)
- This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. (wikipedia.org)
- The systematic name of this enzyme class is ribose-5-phosphate:ammonia ligase (ADP-forming). (wikipedia.org)
- The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). (wikibooks.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)
- Its ability to reduce carbon dioxide at ambient temperature and pressure with a single enzyme and energy provided by light makes the methane-producing strain of R. palustris an excellent starting point to understand how a biological system can marshal resources to produce an energy-rich hydrocarbon in one enzymatic step. (pnas.org)
- The systematic name of this enzyme class is 7,8-dihydropteroate:L-glutamate ligase (ADP-forming) . (wikidoc.org)
- BirA acts both as a biotin-operon repressor and as the enzyme that synthesizes the corepressor, acetyl-CoA:carbon-dioxide ligase. (acris-antibodies.com)
- Carbamoyl Phosphate Synthetase I is a ligase enzyme located in the mitochondria involved in the production of urea. (omicsgroup.org)
- An R. palustris mutant carrying a disrupted 4-hydroxybenzoate-coenzyme A ligase gene was unable to grow with 4-hydroxybenzoate under anaerobic conditions, indicating that the enzyme is essential for anaerobic degradation of this compound. (asm.org)
Synthetase3
- 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)
- Mammalian DHOase (S-dihydroorotate amidohydrolase, EC 3.5.2.3) is part of a large multifunctional protein called CAD, which also has a carbamoyl-phosphate synthetase [carbon-dioxide: L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating), EC 6.3.5.5] and aspartate transcarbamoylase (carbamoyl-phosphate: L-aspartate carbamoyltransferase, EC 2.1.3.2) activities. (pnas.org)
Bonds1
- 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)
Protein9
- E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. (hmdb.ca)
- 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)
- Members of this family are the Pup--protein ligase PafA (proteasome accessory factor A), a protein shown to regulate steady-state levels of certain proteasome targets in Mycobacterium tuberculosis. (jcvi.org)
- Phosphoproteomics under conditions of C/N-nutrient stress showed a global change in the phosphorylation status of proteins, including plasma membrane H + -ATPase, carbon and nitrogen metabolic enzymes and signaling proteins such as protein kinases and transcription factors. (frontiersin.org)
- Ozz directs destruction of â-catenin by assembling an active ubiquitin ligase complex, Ozz-E3, which breaks down this pool of the protein in muscle cells. (innovations-report.com)
- Use of ligases in protein engineering are expected to offer growth opportunities to the market in developing regions such as Latin America, Middle East & Africa, and Asia Pacific. (biospace.com)
- 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)
Metabolism8
- Nutrient availability, in particular the availability of sugar [carbon (C)] and nitrogen (N), is important for the regulation of plant metabolism and development. (frontiersin.org)
- 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)
- Expression of Formate-Tetrahydrofolate Ligase Did Not Improve Growth but Interferes With Nitrogen and Carbon Metabolism ofSynechocystissp. (mpg.de)
- Genes subject to glucose repression were mainly involved in the metabolism of alternative carbon sources including the control of glycerol uptake and metabolism. (biomedcentral.com)
Dioxide4
- Microalgae are photosynthetic microorganisms that can grow using carbon dioxide as sole carbon source and with minimal nutrient requirements. (biomedcentral.com)
- A nitrogenase variant has been described that converts carbon dioxide to methane in vitro. (pnas.org)
- A purified remodeled nitrogenase containing two amino acid substitutions near the site of its FeMo cofactor was recently described as having the capacity to reduce carbon dioxide (CO 2 ) to methane (CH 4 ). (pnas.org)
- 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)
Subunit1
- Data show that the catalytic subunit of glutamate cysteine ligase (Gclc)-derived glutathione buffers reactive oxygen species (ROS), and regulates metabolic reprogramming. (nih.gov)
Carboxylase2
- Biotin--[acetyl-CoA-carboxylase] ligase. (cathdb.info)
- Biotin--[methylcrotonoyl-CoA-carboxylase] ligase. (expasy.org)
Metabolic3
- Its ability to use methanol as a carbon and energy source, its non-fermentative utilization of glucose and its efficient growth on glycerol are key metabolic features that make it attractive for bioprocess development. (biomedcentral.com)
- Transcript profiling has suggested that Candida albicans , a major pathogen of humans, regulates its carbon assimilation in an analogous fashion to the model yeast Saccharomyces cerevisiae , repressing metabolic pathways required for the use of alterative nonpreferred carbon sources when sugars are available. (asm.org)
- We conclude that evolutionary rewiring of ubiquitination targets has meant that following glucose exposure, C. albicans retains key metabolic functions, allowing it to continue to assimilate alternative carbon sources. (asm.org)
Nucleic acid1
- Ligase can join two complementary fragments of nucleic acid and repair single stranded breaks that arise in double stranded DNA during replication. (wikipedia.org)
Proteins2
- 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)
- Same as all enzymes, ligases are embedded with proteins that have a target molecule identification site. (biospace.com)
TRNA5
- Alanine-tRNA Ligase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
- This graph shows the total number of publications written about "Alanine-tRNA Ligase" by people in Harvard Catalyst Profiles by year, and whether "Alanine-tRNA Ligase" was a major or minor topic of these publication. (harvard.edu)
- Below are the most recent publications written about "Alanine-tRNA Ligase" by people in Profiles. (harvard.edu)
- The following list attempts to classify Phenylalanine-tRNA Ligase into categories where each line is subset of the next. (rightdiagnosis.com)
- 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)
Forming1
- 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)
Substrate2
- This unusual regulatory behavior prompted us to study the regulation of carbon substrate utilization in different bioprocess conditions on a genome wide scale. (biomedcentral.com)
- Peroxisomal and methanol utilization genes were confirmed to be subject to carbon substrate repression in excess glucose or glycerol, but were found to be strongly de-repressed in limiting glucose-conditions (as are often applied in fed batch cultivations) in addition to induction by methanol. (biomedcentral.com)
Activity4
- Doping-induced enhancement of crystallinity in polymeric carbon nitride nanosheets to improve their visible-light photocatalytic activity. (bioportfolio.com)
- The researchers showed that the delicate balance between accumulation and removal of â-catenin at a specific cellular site, the sarcolemma - the membrane covering each muscle fiber - is achieved by the activity of the Ozz-E3 ligase. (innovations-report.com)
- GO annotations related to this gene include hydrolase activity and carbon-nitrogen ligase activity, with glutamine as amido-N-donor . (genecards.org)
- FAAH2 has several biochemical functions, for example, carbon-nitrogen ligase activity, with glutamine as amido-N-donor, hydrolase activity. (creativebiomart.net)
Reaction1
- 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)
PafA2
- Iyer, et al (2008) first suggested that PafA is the ligase for Pup, a ubiquitin analog attached to an epsilon-amino group of a Lys side-chain to direct the target to the proteasome. (jcvi.org)
- RN [2] RM PMID:22910360 RT Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. (jcvi.org)
Formation of a carbon-oxyg1
- Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. (bvsalud.org)
Escherichia2
Fixation2
- Template free synthesis of lithium doped three-dimensional macroporous graphitic carbon nitride for photocatalytic N fixation: the effect of Li-N active sites. (bioportfolio.com)
- To avoid confusion and allow us to focus on the key points of carbon fixation that are the subject of this paper, the bioenergetic aspects of the discussion have been framed in largely conventional terms. (royalsocietypublishing.org)
Saccharomyces1
- Current views about carbon assimilation in the pathogenic yeast Candida albicans are strongly influenced by the Saccharomyces cerevisiae paradigm in which cells faced with choices of nutrients first use energetically favorable sugars, degrading enzymes required for the assimilation of less favorable alternative carbon sources. (asm.org)
Amino3
- In the first step, an amino group given by glutamine is attached at carbon 1 of PRPP. (wikibooks.org)
- Nitrogen (N) and carbon (C) are two of the most important nutrients for plant growth, and in the majority of plant species, they are transported in the phloem to sink organs in the form of amino acids and sucrose, respectively. (plantcell.org)
- The deduced gene product showed about 20% amino acid identity with bacterial coenzyme A ligases involved in aerobic degradation of aromatic acids. (asm.org)
Nrf21
- Title: Alteration of Nrf2 and Glutamate Cysteine Ligase expression contribute to lesions growth and fibrogenesis in ectopic endometriosis. (nih.gov)
Diphosphate1
- Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. (systemsbiology.net)
Fatty2
- Interestingly, in aap2 seeds, total carbon (C) levels were unchanged, while fatty acid levels were elevated. (plantcell.org)
- As a result, this major pathogen of humans retains enzymes required for the utilization of physiologically relevant carbon sources such as lactic acid and fatty acids, allowing it to continue to use these host nutrients even when glucose is available. (asm.org)