Ornithine Carbamoyltransferase Deficiency Disease
An inherited urea cycle disorder associated with deficiency of the enzyme ORNITHINE CARBAMOYLTRANSFERASE, transmitted as an X-linked trait and featuring elevations of amino acids and ammonia in the serum. Clinical features, which are more prominent in males, include seizures, behavioral alterations, episodic vomiting, lethargy, and coma. (Menkes, Textbook of Child Neurology, 5th ed, pp49-50)
Carboxyl and Carbamoyl Transferases
Carbamoyl-Phosphate Synthase (Ammonia)
Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
Derivatives of carbamic acid, H2NC(=O)OH. Included under this heading are N-substituted and O-substituted carbamic acids. In general carbamate esters are referred to as urethanes, and polymers that include repeating units of carbamate are referred to as POLYURETHANES. Note however that polyurethanes are derived from the polymerization of ISOCYANATES and the singular term URETHANE refers to the ethyl ester of carbamic acid.
Alkyl and Aryl Transferases
Phosphotransferases (Carboxyl Group Acceptor)
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.
Transferases (Other Substituted Phosphate Groups)
Amino Acid Sequence
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.
Light-dependent changes in redox status of the plastidic acetyl-CoA carboxylase and its regulatory component. (1/77)Plastidic acetyl-CoA carboxylase (ACCase; EC 220.127.116.11), which catalyses the synthesis of malonyl-CoA and is the regulatory enzyme of fatty acid synthesis, is activated by light, presumably under redox regulation. To obtain evidence of redox regulation in vivo, the activity of ACCase was examined in pea chloroplasts isolated from plants kept in darkness (dark-ACCase) or after exposure to light for 1 h (light-ACCase) in the presence or absence of a thiol-reducing agent, dithiothreitol (DTT). The protein level was similar for light-ACCase and dark-ACCase, but the activity of light-ACCase in the absence of DTT was approx. 3-fold that of dark-ACCase. The light-ACCase and dark-ACCase were activated approx. 2-fold and 6-fold by DTT respectively, indicating that light-ACCase was in a much more reduced, active form than the dark-ACCase. This is the first demonstration of the light-dependent reduction of ACCase in vivo. Measurement of the activities of ACCase, carboxyltransferase and biotin carboxylase in the presence and absence of DTT, and the thiol-oxidizing agent, 5, 5'-dithiobis-(2-nitrobenzoic) acid, revealed that the carboxyltransferase reaction, but not the biotin carboxylase reaction, was redox-regulated. The cysteine residue(s) responsible for redox regulation probably reside on the carboxyltransferase component. Measurement of the pH dependence of biotin carboxylase and carboxyltransferase activities in the ACCase suggested that both components affect the activity of ACCase in vivo at a physiological pH range. These results suggest that the activation of ACCase by light is caused partly by the pH-dependent activation of two components and by the reductive activation of carboxyltransferase. (+info)
The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free biotin. (2/77)Acetyl-CoA carboxylase catalyzes the first committed step in the biosynthesis of long-chain fatty acids. The Escherichia coli form of the enzyme consists of a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase activity. The C-terminal 87 amino acids of the biotin carboxyl carrier protein (BCCP87) form a domain that can be independently expressed, biotinylated, and purified (Chapman-Smith, A., Turner, D. L., Cronan, J. E., Morris, T. W., and Wallace, J. C. (1994) Biochem. J. 302, 881-887). The ability of the biotinylated form of this 87-residue protein (holoBCCP87) to act as a substrate for biotin carboxylase and carboxyltransferase was assessed and compared with the results with free biotin. In the case of biotin carboxylase holoBCCP87 was an excellent substrate with a K(m) of 0.16 +/- 0.05 mM and V(max) of 1000.8 +/- 182.0 min(-1). The V/K or catalytic efficiency of biotin carboxylase with holoBCCP87 as substrate was 8000-fold greater than with biotin as substrate. Stimulation of the ATP synthesis reaction of biotin carboxylase where carbamyl phosphate reacted with ADP by holoBCCP87 was 5-fold greater than with an equivalent amount of biotin. The interaction of holoBCCP87 with carboxyltransferase was characterized in the reverse direction where malonyl-CoA reacted with holoBCCP87 to form acetyl-CoA and carboxyholoBCCP87. The K(m) for holoBCCP87 was 0.45 +/- 0.07 mM while the V(max) was 2031.8 +/- 231.0 min(-1). The V/K or catalytic efficiency of carboxyltransferase with holoBCCP87 as substrate is 2000-fold greater than with biotin as substrate. (+info)
Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain. (3/77)A series of chimeral genes, consisting of the yeast GAL10 promoter, yeast ACC1 leader, wheat acetyl-CoA carboxylase (ACCase; EC 18.104.22.168) cDNA, and yeast ACC1 3'-tail, was used to complement a yeast ACC1 mutation. These genes encode a full-length plastid enzyme, with and without the putative chloroplast transit peptide, as well as five chimeric cytosolic/plastid proteins. Four of the genes, all containing at least half of the wheat cytosolic ACCase coding region at the 5'-end, complement the yeast mutation. Aryloxyphenoxypropionate and cyclohexanedione herbicides, at concentrations below 10 microM, inhibit the growth of haploid yeast strains that express two of the chimeric ACCases. This inhibition resembles the inhibition of wheat plastid ACCase observed in vitro and in vivo. The differential response to herbicides localizes the sensitivity determinant to the third quarter of the multidomain plastid ACCase. Sequence comparisons of different multidomain and multisubunit ACCases suggest that this region includes part of the carboxyltransferase domain, and therefore that the carboxyltransferase activity of ACCase (second half-reaction) is the target of the inhibitors. The highly sensitive yeast gene-replacement strains described here provide a convenient system to study herbicide interaction with the enzyme and a powerful screening system for new inhibitors. (+info)
Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2). (4/77)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)
Metabolic biotinylation of recombinant proteins in mammalian cells and in mice. (5/77)The avidin-biotin system is a fundamental technology in biomedicine for immunolocalization, imaging, nucleic acid blotting, and protein labeling. While this technology is robust, it is limited by the fact that mammalian proteins must be expressed and purified prior to chemical biotinylation using cross-linking agents which modify proteins at random locations to heterogeneous levels and can inactivate protein function. To circumvent this limitation, we demonstrate the ability to metabolically biotinylate tagged proteins in mammalian cells and in mice using the endogenous biotinylation enzymes of the host. Endogenously biotinylated proteins were readily purified from mammalian cells using monomeric avidin and eluted under nondenaturing conditions using only biotin as the releasing agent. This technology should allow recombinant proteins and fragile protein complexes to be produced and purified from mammalian cells as well as from transgenic plants and animals. In addition, this technology may be particularly useful for cell-targeting applications in which proteins or viral gene therapy vectors can be biotinylated at genetically defined sites for combination with other targeting moieties complexed with avidin. (+info)
Molecular cloning and characterization of two genes for the biotin carboxylase and carboxyltransferase subunits of acetyl coenzyme A carboxylase in Myxococcus xanthus. (6/77)We have cloned a DNA fragment from a genomic library of Myxococcus xanthus using an oligonucleotide probe representing conserved regions of biotin carboxylase subunits of acetyl coenzyme A (acetyl-CoA) carboxylases. The fragment contained two open reading frames (ORF1 and ORF2), designated the accB and accA genes, capable of encoding a 538-amino-acid protein of 58.1 kDa and a 573-amino-acid protein of 61.5 kDa, respectively. The protein (AccA) encoded by the accA gene was strikingly similar to biotin carboxylase subunits of acetyl-CoA and propionyl-CoA carboxylases and of pyruvate carboxylase. The putative motifs for ATP binding, CO(2) fixation, and biotin binding were found in AccA. The accB gene was located upstream of the accA gene, and they formed a two-gene operon. The protein (AccB) encoded by the accB gene showed high degrees of sequence similarity with carboxyltransferase subunits of acetyl-CoA and propionyl-CoA carboxylases and of methylmalonyl-CoA decarboxylase. Carboxybiotin-binding and acyl-CoA-binding domains, which are conserved in several carboxyltransferase subunits of acyl-CoA carboxylases, were found in AccB. An accA disruption mutant showed a reduced growth rate and reduced acetyl-CoA carboxylase activity compared with the wild-type strain. Western blot analysis indicated that the product of the accA gene was a biotinylated protein that was expressed during the exponential growth phase. Based on these results, we propose that this M. xanthus acetyl-CoA carboxylase consists of two subunits, which are encoded by the accB and accA genes, and occupies a position between prokaryotic and eukaryotic acetyl-CoA carboxylases in terms of evolution. (+info)
An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedione inhibitors. (7/77)cDNA fragments encoding the carboxyltransferase domain of the multidomain plastid acetyl-CoA carboxylase (ACCase) from herbicide-resistant maize and from herbicide-sensitive and herbicide-resistant Lolium rigidum were cloned and sequenced. A Leu residue was found in ACCases from herbicide-resistant plants at a position occupied by Ile in all ACCases from sensitive grasses studied so far. Leu is present at the equivalent position in herbicide-resistant ACCases from other eukaryotes. Chimeric ACCases containing a 1000-aa fragment of two ACCase isozymes found in a herbicide-resistant maize were expressed in a yeast ACC1 null mutant to test herbicide sensitivity of the enzyme in vivo and in vitro. One of the enzymes was resistant/tolerant, and one was sensitive to haloxyfop and sethoxydim, rendering the gene-replacement yeast strains resistant and sensitive to these compounds, respectively. The sensitive enzyme has an Ile residue, and the resistant one has a Leu residue at the putative herbicide-binding site. Additionally, a single Ile to Leu replacement at an equivalent position changes the wheat plastid ACCase from sensitive to resistant. The effect of the opposite substitution, Leu to Ile, makes Toxoplasma gondii apicoplast ACCase resistant to haloxyfop and clodinafop. In this case, inhibition of the carboxyltransferase activity of ACCase (second half-reaction) of a large fragment of the Toxoplasma enzyme expressed in Escherichia coli was tested. The critical amino acid residue is located close to a highly conserved motif of the carboxyltransferase domain, which is probably a part of the enzyme active site, providing the basis for the activity of fop and dim herbicides. (+info)
Motility of single one-headed kinesin molecules along microtubules. (8/77)The motility of single one-headed kinesin molecules (K351 and K340), which were truncated fragments of Drosophila two-headed kinesin, has been tested using total internal reflection fluorescence microscopy. One-headed kinesin fragments moved continuously along the microtubules. The maximum distance traveled until the fragments dissociated from the microtubules for both K351 and K340 was approximately 600 nm. This value is considerably larger than the space resolution of the measurement system (SD approximately 30 nm). Although the movements of the fragments fluctuated in forward and backward directions, statistical analysis showed that the average movements for both K340 and K351 were toward the plus end of the microtubules, i.e., forward direction. When BDTC (a 1.3-S subunit of Propionibacterium shermanii transcarboxylase, which binds weakly to a microtubule), was fused to the tail (C-terminus) of K351, its movement was enhanced, smooth, and unidirectional, similar to that of the two-headed kinesin fragment, K411. However, the travel distance and velocity of K351BDTC molecules were approximately 3-fold smaller than that of K411. These observations suggest that a single kinesin head has basal motility, but coordination between the two heads is necessary for stabilizing the basal motility for the normal level of kinesin processivity. (+info)
Inhibition and nucleic acid binding studies of the carboxyltransferase by Brian Benson
Acetyl-CoA carboxylase is an essential enzyme, as it catalyzes the first committed and regulated step in fatty-acid biosynthesis in all organisms excepting few Archaea and Eubacteria. Acetyl-CoA carboxylase from gram-negative and gram-positive bacteria is a multifunctional enzyme composed of three separate proteins. The carboxyltransferase subunit catalyzes the transfer of a carboxyl group from carboxybiotin to acetyl-CoA, forming malonyl-CoA. The crystal structure of the Escherichia coli (E. coli) carboxyltransferase component of acetyl-CoA carboxylase revealed a unique Zn-domain, presumed to mediate nucleic acid binding, that is absent in the eukaryotic enzyme. Notably, the Zn-domain, adjacent to the active site of carboxyltransferase, makes for a unique target in the development of novel antibiotics capable of highly specific binding. Utilizing an Electrophoretic Mobility Shift Assay as part of this study, we investigated the nonspecific nucleic-acid binding and substrate (malonyl-CoA and biocytin)
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Zakrsl druh ban novn ku dorust pouh ch 1, 2 m. Listy jsou sv e zelen - jemn voskov . Kv ty bananovn ku jsou r ov a oran ov . Ban novn k ma velmi dekorativn plody o velikosti cca 7cm a r ov barvy. Plody jsou jedl a velmi sladk ! Tento druh ban novn ku je velmi tolerantn v i chladu, m ete jej m t v chladn j chodb , kde teplota nekles pod 0. Pokud jej hodn zazimujeme vyd I zimni obdob venku. Vhodn zejm na pro p stov n v byt ...
Novan (NOVN) Sets New 52-Week Low at $3.40 - Watch List News
Novan Inc (NASDAQ:NOVN)s share price hit a new 52-week low during trading on Friday . The company traded as low as $3.40 and last traded at $4.24, with a volume of 19900 shares. The stock had previously closed at $4.30. NOVN has been the subject of a number of recent research reports. ValuEngine raised shares […]
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Nursing Home Abuse | Nolo.com
|p|Its an unfortunate fact that a small percentage of nursing home residents suffer avoidable injuries because of a care facilitys negligence. And in some situations, a care facility employees carelessness or intentional actions can rise to the level of abuse. Whether a nursing home resident is harmed as a result of an accident, or by conduct that might also qualify as a crime, a civil lawsuit is always on the table as a potential legal remedy. In this section, well touch on some of the key practical and legal issues that arise in cases like these. |/p|
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A quit claim deed or deed form allows for the transfer of property from one individual to another without any guarantee as to the transferring persons interest, according to Nolo. It transfers...
October 2019 - Golden Gate ASHI
GGASHI feels all work requiring a permit should be properly permitted. Most of our members, if they find a substantial amount of non-permitted work during their inspections, will say so in their reports. Even minor home improvement projects may require a permit, according to Nolo Press, so we ask, Please dont forget the permit.. ...
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Read FAQs (frequently asked questions) on the Members section of the ACCA website for more information on the questions most often asked about membership.
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Citrónovník pravý - Wikipédia
Citrónovník pravý, staršie Citrónovník limonový (Citrus limon) je druh malého subtropického vždyzeleného stromu z čeľade rutovité. Jeho žltý plod sa nazýva citrón. Má jednoduché vajcovité listy (dlhé 8 až 14 cm), ktoré obsahujú aromatické oleje. Kvitne od apríla do mája. Malé, obojpohlavné biele kvety sú vo zväzkoch a sú veľmi voňavé. Plod je bobuľa s kožovitou šupkou (hesperídium). Dorastá do výšky 3 až 6 m a má ostré tŕne. Pôvodom je pravdepodobne zo severozápadnej Indie, rastie v Stredomorí, Juhozápadnej Ázii a na juhu Severnej Ameriky. Genetická štúdia naznačuje, že ide o kríženca medzi Citrus aurantium a Citrus medica. Bol introdukovaný do Talianska v 2. storočí pred Kr. a v Iraku a Egypte sa pestoval v 7. storočí pred Kr. Plody sa používajú na konzumáciu, ako liečivá rastlina, na čistenie (šťava, dreň aj šupka). Šťava z citróna obsahuje 5% až 6% kyseliny citrónovej, s pH približne 2,2. ...
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro | IRIS Università degli Studi di...
Although human transthyretin (TTR) is associated with systemic amyloidoses, an anti-amyloidogenic effect that prevents Aβ fibril formation in vitro and in animalmodels has been observed. Herewe studied the ability of three different types of TTR, namely human tetramers (hTTR),mouse tetramers (muTTR) and an engineered monomer of the human protein (M-TTR), to suppress the toxicity of oligomers formed by two different amyloidogenic peptides/proteins (HypF-N and Aβ42). muTTR is the most stable homotetramer, hTTR can dissociate into partially unfolded monomers, whereas M-TTR maintains a monomeric state. Preformed toxic HypF-N and Aβ42 oligomers were incubated in the presence of each TTR then added to cell culture media. hTTR, and to a greater extent MTTR, were found to protect human neuroblastoma cells and rat primary neurons against oligomer-induced toxicity, whereas muTTR had no protective effect. The thioflavin T assay and site-directed labeling experiments using pyrene ruled out disaggregation ...
accA - Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha - Helicobacter pylori FD506 - accA gene & protein
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
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accD3 - Putative acetyl-coenzyme A carboxylase carboxyl transferase subunit beta - Mycobacterium tuberculosis (strain ATCC...
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Novartis (NOVN) Given a CHF 90 Price Target at Deutsche Bank - StockNewsTimes
Novartis (VTX:NOVN) has been given a CHF 90 price objective by equities research analysts at Deutsche Bank in a research note issued on Monday. The firm presently has a
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Novartis (NOVN) Given a CHF 92 Price Target by Morgan Stanley Analysts - Community Financial News
Novartis (VTX:NOVN) has been given a CHF 92 price target by analysts at Morgan Stanley in a report issued on Friday. The firm presently has a
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RCSB PDB for 1A6X
1A6X: Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
Metabolic engineering of microorganisms for the production of L-arginine and its derivatives | Microbial Cell Factories | Full...
In the linear pathway (Figure 1A), GLU is converted to acetylglutamate (Ac-GLU) by N-acetylglutamate synthase (NAGS, encoded by argA) which is inhibited by ARG through negative feedback regulation ,. Sequential catalytic reactions catalyzed by the next three enzymes, N-acetylglutamate kinase (NAGK, encoded by argB), N-acetylglutamate semialdehyde dehydrogenase (encoded by argC) and N-acetylornithine transaminase (encoded by argD), which are common in the three pathways (Figure 1), yield N-acetylornithine (Ac-ORN) . The next step, which distinguishes the linear pathway from the other two pathways, is deacetylation of Ac-ORN by AOase to yield ORN ,. The next and final steps are carried out by ornithine carbamoyltransferase (OTC or OTCase, encoded by argF), argininosuccinate synthase (encoded by argG) and argininosuccinate lyase (encoded by argH), which finally yield ARG . This pathway has been found in a few species such as Myxococcus xanthus  and E. coli .. In many ...
Mechanistic studies of agmatine deiminase from multiple bacterial spec by Justin E. Jones, Christina J. Dreyton et al.
One subfamily of guanidino group-modifying enzymes (GMEs) consists of the agmatine deiminases (AgDs). These enzymes catalyze the conversion of agmatine (decarboxylated arginine) to N-carbamoyl putrescine and ammonia. In plants, viruses, and bacteria, these enzymes are thought to be involved in energy production, biosynthesis of polyamines, and biofilm formation. In particular, we are interested in the role that this enzyme plays in pathogenic bacteria. Previously, we reported the initial kinetic characterization of the agmatine deiminase from Helicobacter pylori and described the synthesis and characterization the two most potent AgD inactivators. Herein, we have expanded our initial efforts to characterize the catalytic mechanisms of AgD from H. pylori as well as Streptococcus mutans and Porphyromonas gingivalis. Through the use of pH rate profiles, pK(a) measurements of the active site cysteine, solvent isotope effects, and solvent viscosity effects, we have determined that the AgDs, like PADs 1 and 4
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Sipsey Street Irregulars: Sipsey Street Exclusive: Mike Vanderboegh and David Codrea file ethics complaint on Eric Holder with...
a) Notification. If an attorney is found guilty of a crime or pleads guilty or nolo contendere to a criminal charge in a District of Columbia court, the clerk of that court shall, within ten days from the date of such finding or plea, transmit to this Court and to Bar Counsel a certified copy of the court record or docket entry of the finding or plea. Bar Counsel shall forward the certified copy to the Board. Upon learning that the certified copy has not been timely transmitted by the clerk of the court in which the finding or plea was made, or that an attorney has been found guilty of a crime or has pleaded guilty or nolo contendere to a criminal charge in a court outside the District of Columbia or in any federal court, Bar Counsel shall promptly obtain a certified copy of the court record or docket entry of the finding or plea and transmit it to this Court and to the Board. The attorney shall also file with this Court and the Board, within ten days from the date of such finding or plea, a ...
Biotin Carboxyl Carrier Protein - Rediff Pages
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Complex formation and regulation of Escherichia coli acetyl-CoA carbox by Tyler Craig Broussard
Acetyl-CoA carboxylase is a biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis. The Escherichia coli enzyme is composed of a homodimeric biotin carboxylase, biotinylated biotin carboxyl carrier protein (BCCP), and an α2β2 heterotetrameric carboxyltransferase. Catalysis by acetyl-CoA carboxylase proceeds via two half-reactions. In the first half-reaction, biotin carboxylase catalyzes the ATP-dependent carboxylation of biotin, which is covalently attached to BCCP, to form carboxybiotin. In the second half-reaction, carboxyltransferase transfers the carboxyl group from carboxybiotin to acetyl-CoA to form malonyl-CoA. All biotin-dependent carboxylases are proposed to have a two-site ping-pong mechanism where the carboxylase and transferase activities are separate and do not interact. This posits two hypotheses: either biotin carboxylase and BCCP undergo the first half-reaction, BCCP dissociates, and then BCCP interacts with carboxyltransferase to
Molecules | Free Full-Text | Computational Redesign of Bacterial Biotin Carboxylase Inhibitors Using Structure-Based Virtual...
As the spread of antibiotic resistant bacteria steadily increases, there is an urgent need for new antibacterial agents. Because fatty acid synthesis is only used for membrane biogenesis in bacteria, the enzymes in this pathway are attractive targets for antibacterial agent development. Acetyl-CoA carboxylase catalyzes the committed and regulated step in fatty acid synthesis. In bacteria, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. Fragment-based screening revealed that amino-oxazole inhibits biotin carboxylase activity and also exhibits antibacterial activity against Gram-negative organisms. In this report, we redesigned previously identified lead inhibitors to expand the spectrum of bacteria sensitive to the amino-oxazole derivatives by including Gram-positive species. Using 9,411 small organic building blocks, we constructed a diverse combinatorial library of 1.2 × 108 amino-oxazole derivatives. A subset
Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or...
Kinetic studies were performed on the superoxide dismutases isolated from the anaerobic bacterium Propionibacterium shermanii as active enzymes with either iron or manganese, which were naturally incorporated into the same molecule depending on the metal supply. Both the Fe- and Mn- forms showed decreasing activity with increasing pH. This suggests the protonation of some groups near the metal, possibly a metal-bound water molecule. Thus the kinetic behaviour of this superoxide dismutase is much more dependent on the protein structure than on the metal incorporated into the active site. The secondary structures of both forms were not influenced by variations in pH, whereas the EPR spectra of the Fe-superoxide dismutase changed as a function of pH. The EPR spectra apparently consist of two overlapping species. Steady-state experiments proved that all iron-containing species show catalytic activity, but the species predominating in the alkaline pH range displays a lower reaction rate. The ...
Biotin carboxylase | Article about biotin carboxylase by The Free Dictionary
Looking for biotin carboxylase? Find out information about biotin carboxylase. An enzyme which condenses bicarbonate with biotin to form carboxybiotin Explanation of biotin carboxylase
Accepted name: methylmalonyl-CoA decarboxylase. Reaction: (S)-methylmalonyl-CoA = propanoyl-CoA + CO2. Other name(s): propionyl-CoA carboxylase (incorrect); propionyl coenzyme A carboxylase (incorrect); methylmalonyl-coenzyme A decarboxylase; (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase. Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming). Comments: The enzyme from Veillonella alcalescens is a biotinyl-protein, requires Na+ and acts as a sodium pump.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37289-44-4. References:. 1. Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253-1261. [PMID: 5646172]. 2. Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584-585. [PMID: 7070502]. 3. ...
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KEGG BRITE: KEGG Modules
K11263 bccA; acetyl-CoA/propionyl-CoA carboxylase, biotin carboxylase, biotin carboxyl carrier protein [EC:22.214.171.124 126.96.36.199 188.8.131.52 ...
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MYLK - Role for Caspase-Mediated Cleavage of Rad51 in Induction of Apoptosis
encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which can be constituted by 4 subunits: carboxyltransferase subunit OadA (termed genes was performed in and sole deletion mutants in citrate-supplemented moderate indicated that the experience of the organic is vital for citrate usage. organization from the oxaloacetate decarboxylase involved with citrate usage. (A) The locus can be constituted by genes coding for citrate transporters (could be thought to be the prototype from the Na+-translocating decarboxylase (NaT-DC) category of enzymes. It includes both membrane-bound subunits (OadA (gene, renamed (termed cells during citrate fermentation. Strategies and Components Bacterial strains and development circumstances. Cultures of had been expanded at 37C, without shaking, in Luria-Bertani moderate (LB; Difco, NJ), preliminary pH 7.0, and supplemented with 33 mM trisodium citrate (LBC). Erythromycin was added, when suitable, inside a 5 g ml?1 concentration. Development was supervised by ...
Genetic Mutations & Gene Therapy
What is the current status of gene therapy research?. The Food and Drug Administration (FDA) has not yet approved any human gene therapy product for sale. Current gene therapy is experimental and has not proven very successful in clinical trials. Little progress has been made since the first gene therapy clinical trial began in 1990. In 1999, gene therapy suffered a major setback with the death of 18-year-old Jesse Gelsinger. Jesse was participating in a gene therapy trial for ornithine transcarboxylase deficiency (OTCD). He died from multiple organ failures 4 days after starting the treatment. His death is believed to have been triggered by a severe immune response to the adenovirus carrier.. Another major blow came in January 2003, when the FDA placed a temporary halt on all gene therapy trials using retroviral vectors in blood stem cells. FDA took this action after it learned that a second child treated in a French gene therapy trial had developed a leukemia-like condition. Both this child ...
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NASPA Word of the Day
Definition: SOLON*SOLONS n a wise lawgiver Anagrams: loons nolos snool. Hooks: solonS. Ana-hooks: Bolson Colons Consol loGons loosEn oRlons sAloon snoolS solAno solIon sTolon. Typos: colon salon solan solos. Blana-grams: Bolos Boons Boson Clons Cools Coons Enols Fools Goons Holos Kolos lEnos lInos lIons loAns loBos loCos loGon loGos loIns lonGs looFs looKs looMs loonY looPs loosE looTs loTos Monos Mools Moons noEls noIls noMos nooKs nooNs noosE oBols olEos olIos oRlon osMol Polos Pools Poons sHool sHoon sloMo slooP snooD snooK snooP snooT soKol solDo sonlY soTol sPool sPoon sTool sWoon Tools Toons Wools Zoons. Extensions: solonETS solonETZ solonCHAK solonCHAKS solonETSES solonETZES solonETZIC PREDNIsolonE PREDNIsolonES solonISATION# solonIZATION#. Sub-anagrams: lo loo loon loos no nolo noo nos on ono onos ons os so sol solo son soon ...
RCSB PDB - 3GLK: The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2)
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
CP001022.PE450 Location/Qualifiers FT CDS_pept 483692..484267 FT /codon_start=1 FT /transl_table=11 FT /locus_tag=Exig_0456 FT /product=phosphoribosylglycinamide formyltransferase FT /note=TIGRFAM: phosphoribosylglycinamide FT formyltransferase; PFAM: formyl transferase domain protein; FT KEGG: bcy:Bcer98_0276 phosphoribosylglycinamide FT formyltransferase FT /db_xref=EnsemblGenomes-Gn:Exig_0456 FT /db_xref=EnsemblGenomes-Tr:ACB59938 FT /db_xref=GOA:B1YJ08 FT /db_xref=InterPro:IPR002376 FT /db_xref=InterPro:IPR004607 FT /db_xref=InterPro:IPR036477 FT /db_xref=UniProtKB/TrEMBL:B1YJ08 FT /protein_id=ACB59938.1 FT /translation=MKIACFASGSGSNVEALFEAVETGRLQATIELVVCDQKQAKVIER FT AQARGCDIFVFTAKDYPDKPSFEREIVAELERRGVERIILAGYMRLIGDVLLSHYAGRI FT VNIHPSLLPAFPGKDAIGQAFRGGVKITGVTIHIVDEGMDTGPIIAQEAVRITEDMTRE FT TLQQAIQQVEHRLYPQVIEEWMKEEANV atgaagattg cctgttttgc ctcgggaagt ggcagtaatg tcgaagcttt attcgaagca 60 gttgaaacag gacgtctgca ggctacgatt gaactcgtcg tctgtgatca aaaacaagca 120 aaagtgattg ...
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SOA? That was just a fad. Cloud Computing? Now that is the real deal. So says Springs Rod Johnson
Sadly, its not just VMWare. Even supposedly independent research organizations like Gartner are trumpeting the cloud as loudly as they can these days. Then again, these are the very same people that were at the forefront of the SOA, etc hype too :-).. The technology industry overall seems to hold the unfortunate belief that overblown marketing is an essential tool to sell anything -- even things that do indeed have technical merit. Guess thats where TSS steps in to separate the reality from the hype :-). Fortunately rank-and-file developers in general seem to grasp the concept of the hype cycle. Its the higher-ups in the technology organizations that often dont seem to get it.... ...
List of MeSH codes (D08)
... carboxyl and carbamoyl transferases MeSH D08.811.913.555.275.200 - aspartate carbamoyltransferase MeSH D08.811.913.555.275.600 ... glutathione transferase MeSH D08.811.913.225.500.500 - glutathione S-transferase pi MeSH D08.811.913.225.575 - ... carbamoyl-phosphate synthase (ammonia) MeSH D08.811.464.259.400 - carbon-nitrogen ligases with glutamine as amide-n-donor MeSH ... adp ribose transferases MeSH D08.811.913.400.725.115.180 - cholera toxin MeSH D08.811.913.400.725.115.220 - diphtheria toxin ...
Orotate is covalently linked with phosphoribosyl pyrophosphate (PRPP) by orotate phosphoribysol-transferase yielding orotidine ... A carboxyl group is attached to AIR by N5-CAIR synthetase to form N5-Carboxyaminoimidazole ribonucleotide (N5-CAIR), which is ... ring begins with the conversion of Aspartate to N-Carbamoylaspartate by undergoing a condensation reaction with carbamoyl ...
... aspartate carbamoyltransferase catalyzes a condensation reaction between aspartate and carbamoyl phosphate to form carbamoyl ... Next, a glycine is incorporated fueled by ATP hydrolysis, and the carboxyl group forms an amine bond to the NH2 previously ... Orotate phosphoribosyltransferase (PRPP transferase) catalyzes the net reaction yielding orotidine monophosphate (OMP): Orotate ... The synthesis of the pyrimidines CTP and UTP occurs in the cytoplasm and starts with the formation of carbamoyl phosphate from ...
List of EC numbers (EC 6)
... biotin carboxyl-carrier protein] ligase EC 184.108.40.206: carbamoyl-phosphate synthase (ammonia) EC 220.127.116.11: formate-dihydrofolate ... several ubiquitin transferases and finally by EC 18.104.22.168 [ubiquitin transferase RING E3 (calmodulin-selective)] EC 22.214.171.124: ... carbamoyl-phosphate synthase (glutamine-hydrolysing) EC 126.96.36.199: asparaginyl-tRNA synthase (glutamine-hydrolysing) EC 188.8.131.52: ... long-chain fatty acid adenylase/transferase FadD23 * EC 184.108.40.206: isophthalate-CoA ligase * EC 220.127.116.11: long-chain fatty acid ...
List of EC numbers (EC 2)
... oxalate CoA-transferase EC 18.104.22.168: malonate CoA-transferase EC 22.214.171.124: deleted EC 126.96.36.199: 3-oxoacid CoA-transferase EC 2.8. ... carbamoyl-phosphate synthase (ammonia) EC 188.8.131.52: formate kinase EC 184.108.40.206: butyrate kinase EC 220.127.116.11: acetylglutamate ... gibberellin A4 carboxyl methyltransferase EC 18.104.22.1687: anthranilate O-methyltransferase EC 22.214.171.1248: indole-3-acetate O- ... oxalate CoA-transferase EC 126.96.36.199: malonate CoA-transferase EC 188.8.131.52: deleted EC 184.108.40.206: 3-oxoacid CoA-transferase EC 2.8. ...
DeCS 2008 - versión 17 de Marzo de 2008
Transferase, Carbamoyl. Transferase, Carboxyl. Transferases, Carbamoyl. Transferases, Carboxyl. Tree number(s):. D08.811. ... Carbamoyl Transferase Carbamoyl Transferases Carbamoyltransferase Transferase, Carbamoyl Transferases, Carbamoyl ... Carbamoyl Transferases. Carbamoyltransferase. Carbamoyltransferases. Carboxyl Transferase. Carboxyl Transferases. Carboxyl and ... Carboxyl and carbamoyl transferases Entry term(s):. Carbamoyl Transferase. ...
activity, and inhibition of the Carboxyltransferase -subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium...
Methyltransferases | Profiles RNS
Glycosyl transferase family 4, Phospho-N-acetylmuramoyl-pentapeptide-transferase signature 1 [Interproscan].","protein_coding ... ","Biotin carboxyl carrier protein of acetyl-CoA carboxylase [Ensembl]. Biotin-requiring enzyme [Interproscan].","protein_ ... ","biotin carboxylase [Ensembl]. Carbamoyl-phosphate synthase L chain, Biotin carboxylase C-terminal domain [Interproscan]."," ... ","glycosyl transferase, group 4 family protein [Ensembl]. Glycosyl transferase [Interproscan].","protein_coding" "AKI50640"," ...
Carbamoyl-phosphate synthase L chain, ATP binding domain. 2.8E-80. 153. 361. ... Carboxyl_trans. Carboxyl transferase domain. 7.1E-184. 1623. 2175. © 2022 - Robin Ohm - Utrecht University - The Netherlands ... Carbamoyl-phosphate synthase L chain, ATP binding domain. 2.0E-74. 136. 346. ... Carbamoyl-phosphate synthase L chain, ATP binding domain. 9.3E-53. 234. 416. ...
KEGG T08195: CLAFUR5 06324
YOR184W 2167.216480 INESSENTIAL SER1 phosphoserine transaminase,phosphoserine aminotransferase
1.514166 INESSENTIAL KTR6 mannosylphosphate transferase, cell wall organization and biogenesis*, mannosylphosphate transferase ... YER098W 0.630747 INESSENTIAL UBP9 ubiquitin carboxyl-terminal hydrolase, deubiquitylation, ubiquitin-specific protease, ... carbamoyl-phosphate synthase (glutamine-hydrolyzing), cytosol YDR158W 1459.133859 INESSENTIAL HOM2 aspartic beta semi-aldehyde ... 7.324323 INESSENTIAL GTT2 Glutathione transferase, glutathione metabolism, glutathione transferase, YJR048W 7.324312 ...
Carbamoyl phosphate synthetase-1 (CPS1) is the first key enzyme involved in the urea cycle. Functionally, we demonstrated that ... Two arginine residues, unique among plant SSATs, hold the carboxyl group of amino acid substrates. The most abundant acetylated ... lysine and ornithine acetylation catalyzed by spermine/spermidine N-acetyl transferase in moss and maize. ...
Domain IPR003439:ABC transporter-like
Acetyl-CoA carboxylase carboxyl transferase, beta subunit 31 Conserved_site IPR000385:MoaA/nifB/pqqE, iron-sulphur binding, ... Glutathione S-transferase, N-terminal 142 Family IPR002781:Transmembrane protein TauE-like 142 Domain IPR005479:Carbamoyl- ... Glycosyl transferase, family 51 87 Domain IPR023631:Amidase signature domain 86 Family IPR004165:Coenzyme A transferase family ... Glycosyl transferase, family 4 63 Domain IPR002539:MaoC-like domain 63 Family IPR002201:Glycosyl transferase, family 9 62 ...
HOMD :: SEQF1911
carboxyl transferase domain protein. 162. SEQF1911,AEHJ01000035.1. EFO76790.1 jb [NA] [AA] 699/232. 115086-115784. putative ... Carbamoyl-phosphate synthase L chain%2C ATP binding domain protein. 143. SEQF1911,AEHJ01000035.1. EFO76771.1 jb [NA] [AA] 120/ ... phosphopantetheine--protein transferase domain protein. 150. SEQF1911,AEHJ01000035.1. EFO76778.1 jb [NA] [AA] 1089/362. 196948- ...
The reaction is catalyzed by carbamoyl phosphate synthetase. The carbamoyl moiety of carbamoyl phosphate (NH2CO−) is ... The α-carbon is the one closest to the carboxyl [−COOH] group of a fatty acid; the next closest is the β-, and so on to the end ... 6. The enzyme peptidyl transferase, which is part of the larger of the two ribosomal subunits, catalyzes the transfer of ... and carbamoyl phosphate (derived from carbon dioxide, ATP, and ammonia via reaction [30->]) condense to form N- ...
HOMD :: SEQF2888
putative acetyl-CoA carboxylase%2C carboxyl transferase%2C beta subunit. 18. SEQF2888,AENP01000032.1. EFR32157.1 jb [NA] [AA] ... carbamoyl-phosphate synthase%2C large subunit. 69. SEQF2888,AENP01000032.1. EFR32208.1 jb [NA] [AA] 420/139. 968-549. putative ... polysaccharide pyruvyl transferase CsaB. 22. SEQF2888,AENP01000032.1. EFR32161.1 jb [NA] [AA] 1029/342. 58866-57838. peptidase ... acyl transferase domain protein. 17. SEQF2888,AENP01000032.1. EFR32156.1 jb [NA] [AA] 861/286. 8241-7381. ...
HOMD :: SEQF3533
carbamoyl phosphate synthase large subunit. 197. SEQF3533,CP024697.1. ATV54151.1 jb [NA] [AA] 759/252. 252369-253127. ... acetyl-CoA carboxylase biotin carboxyl carrier protein subunit. 68. SEQF3533,CP024697.1. ATV54022.1 jb [NA] [AA] 351/116. 96364 ... glycosyl transferase family 2. 14. SEQF3533,CP024697.1. ATV53968.1 jb [NA] [AA] 462/153. 20118-19657. hypothetical protein. ... carbamoyl-phosphate synthase (glutamine-hydrolyzing) small subunit. 196. SEQF3533,CP024697.1. ATV54150.1 jb [NA] [AA] 3225/1074 ...
Carbon dioxide (YMDB00912) - Yeast Metabolome Database
ATP + biotin-[carboxyl-carrier-protein] + CO(2) → ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].. ... Involved in transferase activity. Specific function:. Fatty acid synthetase catalyzes the formation of long- chain fatty acids ... acetyl-CoA carboxylase and carbamoyl- phosphate synthetase. Involved in protection against oxidative damage. Encodes a ... ATP + biotin-[carboxyl-carrier-protein] + CO(2) → ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].. ...
Model Search | BioModels
Carbamoyl-phosphate synthase arginine-specific small chain (3) * Cytochrome b-c1 complex subunit 1, mitochondrial (3) ... Ubiquitin carboxyl-terminal hydrolase RPN11 (1) * Type 1 phosphatases regulator YPI1 (1) ... L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (3) * V-type proton ATPase subunit D (3) ...
Advances in Separations Technology for the "OMICs" and Clarification of Therapeutic Targets | Leaders in Pharmaceutical...
The modular BRCA1 carboxyl-terminal (BRCT) domain is frequently present in proteins involved in the DDR, can exist either as an ... ADP in the y-glutamyl transferase reaction that is catalyzed by glutamine synthetase.. M Dowton, IR Kennedy. Purification of ... Substrate the endogenous Upβ substrate, N-carbamoyl-β-alanine. *Substrate mimicry of an ABPP probe. ...
Seed Viewer - Organism
Acetyl-coenzyme A carboxyl transferase alpha chain (EC 220.127.116.11)@^fig,[email protected]~Fatty Acids, Lipids, and [email protected]^ ... Carbamoyl-phosphate synthase small chain (EC 18.104.22.168)@^fig,[email protected]~Cell Division and Cell [email protected]^Cell Division and ... Acetyl-coenzyme A carboxyl transferase beta chain (EC 22.214.171.124)@^fig,[email protected]~Fatty Acids, Lipids, and [email protected]^ ... Acetyl-coenzyme A carboxyl transferase alpha chain (EC 126.96.36.199)@^fig,[email protected]~Predictions based on plant-prokaryote ...
No data available that match "carboxyl and carbamoyl transferases"
- A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (childrensmercy.org)
- Asp/Orn binding domain, carbamoyl-P binding domain [InterProScan]. (ntu.edu.sg)