Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Acetate-CoA Ligase: An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Coenzyme A Ligases: Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.Antibody Formation: The production of ANTIBODIES by proliferating and differentiated B-LYMPHOCYTES under stimulation by ANTIGENS.Antibodies, Neutralizing: Antibodies that reduce or abolish some biological activity of a soluble antigen or infectious agent, usually a virus.Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Methylmalonyl-CoA Decarboxylase: A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism.Metabolome: The dynamic collection of metabolites which represent a cell's or organism's net metabolic response to current conditions.Propionates: Derivatives of propionic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxyethane structure.Metabolomics: The systematic identification and quantitation of all the metabolic products of a cell, tissue, organ, or organism under varying conditions. The METABOLOME of a cell or organism is a dynamic collection of metabolites which represent its net response to current conditions.Acetyl-CoA Carboxylase: A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.Carbon-Carbon Ligases: Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.Acyl Coenzyme A: S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.Carboxy-Lyases: Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.EthylenediaminesMethanosarcina barkeri: A species of halophilic archaea whose organisms are nonmotile. Habitats include freshwater and marine mud, animal-waste lagoons, and the rumens of ungulates.Search Engine: Software used to locate data or information stored in machine-readable form locally or at a distance such as an INTERNET site.Chelating Agents: Chemicals that bind to and remove ions from solutions. Many chelating agents function through the formation of COORDINATION COMPLEXES with METALS.Information Storage and Retrieval: Organized activities related to the storage, location, search, and retrieval of information.Semiconductors: Materials that have a limited and usually variable electrical conductivity. They are particularly useful for the production of solid-state electronic devices.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Aspergillus oryzae: An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Bacillus subtilis: A species of gram-positive bacteria that is a common soil and water saprophyte.Acetyl Coenzyme A: Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.Acetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Phosphate Acetyltransferase: An enzyme that catalyzes the synthesis of acetylphosphate from acetyl-CoA and inorganic phosphate. Acetylphosphate serves as a high-energy phosphate compound. EC 2.3.1.8.Coenzyme ASirtuin 3: A sirtuin family member found primarily in MITOCHONDRIA. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.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.Pseudomonas syringae: A species of gram-negative, fluorescent, phytopathogenic bacteria in the genus PSEUDOMONAS. It is differentiated into approximately 50 pathovars with different plant pathogenicities and host specificities.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Siderophores: Low-molecular-weight compounds produced by microorganisms that aid in the transport and sequestration of ferric iron. (The Encyclopedia of Molecular Biology, 1994)Pigments, Biological: Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms.Plant Diseases: Diseases of plants.Sigma Factor: A protein which is a subunit of RNA polymerase. It effects initiation of specific RNA chains from DNA.ATP-Binding Cassette Transporters: A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.Bacterial Proteins: Proteins found in any species of bacterium.Pseudomonas aeruginosa: A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.Indenes: A family of fused-ring hydrocarbons isolated from coal tar that act as intermediates in various chemical reactions and are used in the production of coumarone-indene resins.Desulfitobacterium: A genus of anaerobic, gram-positive bacteria in the family Peptococcaceae, that reductively dechlorinates CHLOROPHENOLS.Oxidoreductases, O-Demethylating: Drug metabolizing enzymes which oxidize methyl ethers. Usually found in liver microsomes.Corrinoids: Cyclic TETRAPYRROLES based on the corrin skeleton.Tetrachloroethylene: A chlorinated hydrocarbon used as an industrial solvent and cooling liquid in electrical transformers. It is a potential carcinogen.Halogens: A family of nonmetallic, generally electronegative, elements that form group 17 (formerly group VIIa) of the periodic table.Clostridium bifermentans: A species of gram-positive bacteria in the family Clostridiaceae that ferments both CARBOHYDRATES and AMINO ACIDS.Chlorophenols: Phenols substituted with one or more chlorine atoms in any position.Pentachlorophenol: An insecticide and herbicide that has also been used as a wood preservative. Pentachlorphenol is a widespread environmental pollutant. Both chronic and acute pentachlorophenol poisoning are medical concerns. The range of its biological actions is still being actively explored, but it is clearly a potent enzyme inhibitor and has been used as such as an experimental tool.Dichloroethylenes: Toxic chlorinated unsaturated hydrocarbons. Include both the 1,1- and 1,2-dichloro isomers. Both isomers are toxic, but 1,1-dichloroethylene is the more potent CNS depressant and hepatotoxin. It is used in the manufacture of thermoplastic polymers.IndolizinesAttentional Blink: Temporary visual deficit or impaired visual processing occurring in a rapid serial visual presentation task. After a person identifies the first of two visual targets, the ability to detect the second target is impaired for the next few hundred milliseconds. This phenomenon is called attentional blink.Williams Syndrome: A disorder caused by hemizygous microdeletion of about 28 genes on chromosome 7q11.23, including the ELASTIN gene. Clinical manifestations include SUPRAVALVULAR AORTIC STENOSIS; MENTAL RETARDATION; elfin facies; impaired visuospatial constructive abilities; and transient HYPERCALCEMIA in infancy. The condition affects both sexes, with onset at birth or in early infancy.Cholestasis, Intrahepatic: Impairment of bile flow due to injury to the HEPATOCYTES; BILE CANALICULI; or the intrahepatic bile ducts (BILE DUCTS, INTRAHEPATIC).MississippiDrugs, Chinese Herbal: Chinese herbal or plant extracts which are used as drugs to treat diseases or promote general well-being. The concept does not include synthesized compounds manufactured in China.Receptor-Interacting Protein Serine-Threonine Kinase 2: A RIP serine-theonine kinase that contains a C-terminal caspase activation and recruitment domain. It can signal by associating with other CARD-signaling adaptor proteins and INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.Retroelements: Elements that are transcribed into RNA, reverse-transcribed into DNA and then inserted into a new site in the genome. Long terminal repeats (LTRs) similar to those from retroviruses are contained in retrotransposons and retrovirus-like elements. Retroposons, such as LONG INTERSPERSED NUCLEOTIDE ELEMENTS and SHORT INTERSPERSED NUCLEOTIDE ELEMENTS do not contain LTRs.Nobel PrizeGenetic Drift: The fluctuation of the ALLELE FREQUENCY from one generation to the next.History, 19th Century: Time period from 1801 through 1900 of the common era.Methanococcus: A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.ArchivesBiological Science Disciplines: All of the divisions of the natural sciences dealing with the various aspects of the phenomena of life and vital processes. The concept includes anatomy and physiology, biochemistry and biophysics, and the biology of animals, plants, and microorganisms. It should be differentiated from BIOLOGY, one of its subdivisions, concerned specifically with the origin and life processes of living organisms.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Gene Expression Regulation, Archaeal: Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in archaea.Genes, Archaeal: The functional genetic units of ARCHAEA.Directories as Topic: Lists of persons or organizations, systematically arranged, usually in alphabetic or classed order, giving address, affiliations, etc., for individuals, and giving address, officers, functions, and similar data for organizations. (ALA Glossary of Library and Information Science, 1983)Archaeal Proteins: Proteins found in any species of archaeon.Methanococcales: An order of anaerobic methanogens in the kingdom EURYARCHAEOTA. They are pseudosarcina, coccoid or sheathed rod-shaped and catabolize methyl groups. The cell wall is composed of protein. The order includes one family, METHANOCOCCACEAE. (From Bergey's Manual of Systemic Bacteriology, 1989)
(1/150) The Cryptosporidium "mouse" genotype is conserved across geographic areas.

A 298-bp region of the Cryptosporidium parvum 18S rRNA gene and a 390-bp region of the acetyl coenzyme A synthetase gene were sequenced for a range of Cryptosporidium isolates from wild house mice (Mus domesticus), a bat (Myotus adversus), and cattle from different geographical areas. Previous research has identified a distinct genotype, referred to as the "mouse"-derived Cryptosporidium genotype, common to isolates from Australian mice. Comparison of a wider range of Australian mouse isolates with United Kingdom and Spanish isolates from mice and cattle and also an Australian bat-derived Cryptosporidium isolate revealed that the "mouse" genotype is conserved across geographic areas. Mice are also susceptible to infection with the "cattle" Cryptosporidium genotype, which has important implications for their role as reservoirs of infection for humans and domestic animals.  (+info)

(2/150) The role of an iron-sulfur cluster in an enzymatic methylation reaction. Methylation of CO dehydrogenase/acetyl-CoA synthase by the methylated corrinoid iron-sulfur protein.

This paper focuses on how a methyl group is transferred from a methyl-cobalt(III) species on one protein (the corrinoid iron-sulfur protein (CFeSP)) to a nickel iron-sulfur cluster on another protein (carbon monoxide dehydrogenase/acetyl-CoA synthase). This is an essential step in the Wood-Ljungdahl pathway of anaerobic CO and CO2 fixation. The results described here strongly indicate that transfer of methyl group to carbon monoxide dehydrogenase/acetyl-CoA synthase occurs by an SN2 pathway. They also provide convincing evidence that oxidative inactivation of Co(I) competes with methylation. Under the conditions of our anaerobic assay, Co(I) escapes from the catalytic cycle one in every 100 turnover cycles. Reductive activation of the CFeSP is required to regenerate Co(I) and recruit the protein back into the catalytic cycle. Our results strongly indicate that the [4Fe-4S] cluster of the CFeSP is required for reductive activation. They support the hypothesis that the [4Fe-4S] cluster of the CFeSP does not participate directly in the methyl transfer step but provides a conduit for electron flow from physiological reductants to the cobalt center.  (+info)

(3/150) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri.

Methanosarcina barkeri has recently been shown to produce a multisubunit membrane-bound [NiFe] hydrogenase designated Ech (Escherichia coli hydrogenase 3) hydrogenase. In the present study Ech hydrogenase was purified to apparent homogeneity in a high yield. The enzyme preparation obtained only contained the six polypeptides which had previously been shown to be encoded by the ech operon. The purified enzyme was found to contain 0.9 mol of Ni, 11.3 mol of nonheme-iron and 10.8 mol of acid-labile sulfur per mol of enzyme. Using the purified enzyme the kinetic parameters were determined. The enzyme catalyzed the H2 dependent reduction of a M. barkeri 2[4Fe-4S] ferredoxin with a specific activity of 50 U x mg protein-1 at pH 7.0 and exhibited an apparent Km for the ferredoxin of 1 microM. The enzyme also catalyzed hydrogen formation with the reduced ferredoxin as electron donor at a rate of 90 U x mg protein-1 at pH 7.0. The apparent Km for the reduced ferredoxin was 7.5 microM. Reduction or oxidation of the ferredoxin proceeded at similar rates as the reduction or oxidation of oxidized or reduced methylviologen, respectively. The apparent Km for H2 was 5 microM. The kinetic data strongly indicate that the ferredoxin is the physiological electron donor or acceptor of Ech hydrogenase. Ech hydrogenase amounts to about 3% of the total cell protein in acetate-grown, methanol-grown or H2/CO2-grown cells of M. barkeri, as calculated from quantitative Western blot experiments. The function of Ech hydrogenase is ascribed to ferredoxin-linked H2 production coupled to the oxidation of the carbonyl-group of acetyl-CoA to CO2 during growth on acetate, and to ferredoxin-linked H2 uptake coupled to the reduction of CO2 to the redox state of CO during growth on H2/CO2 or methanol.  (+info)

(4/150) Molecular cloning and cell-cycle-dependent expression of the acetyl-CoA synthetase gene in Tetrahymena cells.

To identify transcriptionally regulated mediators associated with the cell cycle, we adopted the differential mRNA display technique for cell cultures of Tetrahymena pyriformis synchronized by cyclic heat treatment. One cDNA fragment that was expressed differently during synchronous cell division had a greatly decreased expression at 30 min after the end of heat treatment (EHT). Using this fragment as a probe, we isolated the full-length cDNA for T. pyriformis acetyl-CoA synthetase (TpAcs) which encodes a 651 amino acid polypeptide with a predicted molecular mass of 72.8 kDa. The deduced amino acid sequence of T. pyriformis ACS shows 42% sequence identity compared with that of Lysobacter sp. acetyl-CoA synthetase (ACS), an enzyme which catalyses the formation of acetyl-CoA from acetate via an acetyl-adenylate intermediate. The deduced sequence is also 41% and 40% identical compared with those of Pseudomonas putida and Coprinus cinereus ACS, respectively. The deduced sequence of T. pyriformis ACS also shares similar characteristics of the conserved motifs I and II in the ACS family. To further investigate the actions of the gene encoding this enzyme, mRNA expression was determined during the course of synchronized cell division in T. pyriformis. Northern blot results show that the mRNA level was dramatically decreased at 30 min after EHT prior to entering synchronous cell division (which occurs 75 min after EHT), suggesting that mRNA expression of the TpAcs was associated with the cell cycle and that the down-regulated expression of TpAcs at 30 min after EHT would be required for the initiation of the oncoming synchronous cell division in T. pyriformis.  (+info)

(5/150) Oxalic acid production by Aspergillus niger: an oxalate-non-producing mutant produces citric acid at pH 5 and in the presence of manganese.

The external pH appeared to be the main factor governing oxalic acid production by Aspergillus niger. A glucose-oxidase-negative mutant produced substantial amounts of oxalic acid as long as the pH of the culture was 3 or higher. When pH was decreased below 2, no oxalic acid was formed. The activity of oxaloacetate acetylhydrolase (OAH), the enzyme believed to be responsible for oxalate formation in A. niger, correlated with oxalate production. OAH was purified from A. niger and characterized. OAH cleaves oxaloacetate to oxalate and acetate, but A. niger never accumulated any acetate in the culture broth. Since an A. niger acuA mutant, which lacks acetyl-CoA synthase, did produce some acetate, wild-type A. niger is apparently able to catabolize acetate sufficiently fast to prevent its production. An A. niger mutant, prtF28, previously isolated in a screen for strains deficient in extracellular protease expression, was shown here to be oxalate non-producing. The prtF28 mutant lacked OAH, implying that OAH is the only enzyme involved in oxalate production in A. niger. In a traditional citric acid fermentation low pH and absence of Mn2+ are prerequisites. Remarkably, a strain lacking both glucose oxidase (goxC) and OAH (prtF) produced citric acid from sugar substrates in a regular synthetic medium at pH 5 and under these conditions production was completely insensitive to Mn2+.  (+info)

(6/150) sigma(70) is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli.

Cells of Escherichia coli undergo a metabolic switch associated with the production and utilization of acetate. During exponential growth on tryptone broth, these cells excrete acetate via the phosphotransacetylase-acetate kinase (Pta-AckA) pathway. As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively. This metabolic switch depends upon the induction of Acs. As part of our effort to dissect the mechanism(s) underlying induction and to identify the signal(s) that triggers that induction, we sought the sigma factor most responsible for acs expression. Using isogenic strains that carry a temperature sensitivity allele of the gene that encodes sigma(70) and either a wild-type or null allele of the gene that encodes sigma(S), we determined by immunoblotting, reverse transcriptase PCR, and acs::lacZ transcriptional fusion analyses that sigma(70) is the sigma factor primarily responsible for the acs transcription that cells induce during mid-exponential phase. In contrast, sigma(S) partially inhibits that transcription as cells enter stationary phase.  (+info)

(7/150) Evidence for intersubunit communication during acetyl-CoA cleavage by the multienzyme CO dehydrogenase/acetyl-CoA synthase complex from Methanosarcina thermophila. Evidence that the beta subunit catalyzes C-C and C-S bond cleavage.

The carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) from Methanosarcina thermophila is part of a five-subunit complex consisting of alpha, beta, gamma, delta, and epsilon subunits. The multienzyme complex catalyzes the reversible oxidation of CO to CO(2), transfer of the methyl group of acetyl-CoA to tetrahydromethanopterin (H(4)MPT), and acetyl-CoA synthesis from CO, CoA, and methyl-H(4)MPT. The alpha and epsilon subunits are required for CO oxidation. The gamma and delta subunits constitute a corrinoid iron-sulfur protein that is involved in the transmethylation reaction. This work focuses on the beta subunit. The isolated beta subunit contains significant amounts of nickel. When proteases truncate the beta subunit, causing the CODH/ACS complex to dissociate, the amount of intact beta subunit correlates directly with the EPR signal intensity of Cluster A and the activity of the CO/acetyl-CoA exchange reaction. Our results strongly indicate that the beta subunit harbors Cluster A, a NiFeS cluster, that is the active site of acetyl-CoA cleavage and assembly. Although the beta subunit is necessary, it is not sufficient for acetyl-CoA synthesis; interactions between the CODH and the ACS subunits are required for cleavage or synthesis of the C-C bond of acetyl-CoA. We propose that these interactions include intramolecular electron transfer reactions between the CODH and ACS subunits.  (+info)

(8/150) Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (Nucleoside diphosphate-forming).

The gene coding for the acetyl-CoA synthetase (ADP-forming) from the amitochondriate eukaryote Giardia lamblia has been expressed in Escherichia coli. The recombinant enzyme exhibited the same substrate specificity as the native enzyme, utilizing acetyl-CoA and adenine nucleotides as preferred substrates and less efficiently, propionyl- and succinyl-CoA. N- and C-terminal parts of the G. lamblia acetyl-CoA synthetase sequence were found to be homologous to the alpha- and beta-subunits, respectively, of succinyl-CoA synthetase. Sequence analysis of homologous enzymes from various bacteria, archaea, and the eukaryote, Plasmodium falciparum, identified conserved features in their organization, which allowed us to delineate a new superfamily of acyl-CoA synthetases (nucleoside diphosphate-forming) and its signature motifs. The representatives of this new superfamily of thiokinases vary in their domain arrangement, some consisting of separate alpha- and beta-subunits and others comprising fusion proteins in alpha-beta or beta-alpha orientation. The presence of homologs of acetyl-CoA synthetase (ADP-forming) in such human pathogens as G. lamblia, Yersinia pestis, Bordetella pertussis, Pseudomonas aeruginosa, Vibrio cholerae, Salmonella typhi, Porphyromonas gingivalis, and the malaria agent P. falciparum suggests that they might be used as potential drug targets.  (+info)

*  Acetate-CoA ligase (ADP-forming)
... an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + acetate + CoA ⇌ {\ ... The systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ... acetate, and CoA, whereas its 3 products are ADP, phosphate, and acetyl-CoA. This enzyme belongs to the family of ligases, ... Reeves RE, Warren LG, Susskind B, Lo HS (1977). "An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. ...
*  Methionine gamma-lyase
2-oxobutyrate is ultimately decomposed by acetate-CoA ligase and produces ATP, thus contributing to ATP metabolism. MGL also ...
*  Acetyl-CoA synthetase
... or Acetate-CoA ligase is an enzyme (EC 6.2.1.1) involved in metabolism of acetate. It is in the ligase ... Acetate + CoA <=> AMP + Pyrophosphate + Acetyl-CoA Once acetyl-CoA is formed it can be used in the TCA cycle in aerobic ... Co-A then rotates in the active site into the position where acetate can covalently bind to CoA. The covalent bond is formed ... The two molecules joined together that make up Acetyl CoA synthetase are acetate and coenzyme A (CoA). The complete reaction ...
*  List of EC numbers (EC 6)
... lactate ligase EC 6.2.1.1: acetate-CoA ligase EC 6.2.1.2: butyrate-CoA ligase EC 6.2.1.3: long-chain-fatty-acid-CoA ligase EC ... acid-CoA ligase (GDP-forming) EC 6.2.1.11: biotin-CoA ligase EC 6.2.1.12: 4-coumarate-CoA ligase EC 6.2.1.13: acetate-CoA ... glutarate-CoA ligase EC 6.2.1.7: cholate-CoA ligase EC 6.2.1.8: oxalate-CoA ligase EC 6.2.1.9: malate-CoA ligase EC 6.2.1.10: ... arachidonate-CoA ligase EC 6.2.1.16: acetoacetate-CoA ligase EC 6.2.1.17: propionate-CoA ligase EC 6.2.1.18: citrate-CoA ligase ...
*  Thiokinase
Types include: Acetate-CoA ligase (ADP-forming) Butyrate-CoA ligase Citrate-CoA ligase Malate-CoA ligase Succinate-CoA ligase ( ... A Thiokinase is a ligase that synthesizes CoA Thioesters. They are classified under EC number 6.2, but often have primary names ... ADP-forming) Succinate-CoA ligase (GDP-forming) Molecular and Cellular Biology portal. ...
*  CO-methylating acetyl-CoA synthase
Acetyl-CoA Synthase (ACS), not to be confused with Acetyl-CoA Synthetase or Acetate-CoA Ligase (ADP forming), is a Nickel ... the Wood-Ljungdahl pathway allows for the anaerobic oxidation of acetate where ATP is used to convert acetate into acetyl-CoA, ... For example, acetate-forming bacteria use acetyl-CoA for their autotrophic growth processes, and methanogenic archae such as ... In addition to acetyl-CoA production, the reverse can occur with ACS producing acetate, CO and returning the methyl piece back ...
*  2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase
... acetate:CoA ligase (AMP-forming). This enzyme catalyses the following chemical reaction [(1R)-2,2,3-trimethyl-5-oxocyclopent-3- ... 2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase (EC 6.2.1.38, 2-oxo-Delta3-4,5,5-trimethylcyclopentenylacetyl-CoA ... enyl]acetate + ATP + CoA ⇌ {\displaystyle \rightleftharpoons } AMP + diphosphate + [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl] ... 2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase at the US National Library of Medicine Medical Subject Headings (MeSH ...
*  List of MeSH codes (D08)
... coenzyme a ligases MeSH D08.811.464.267.500.200 --- acetate-coa ligase MeSH D08.811.464.267.500.600 --- succinate-coa ligases ... isoleucine-trna ligase MeSH D08.811.464.263.200.500 --- leucine-trna ligase MeSH D08.811.464.263.200.550 --- lysine-trna ligase ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 --- arginine-tRNA ligase MeSH D08.811.464.263.200.150 --- aspartate-tRNA ...
*  Citric acid cycle
... succinyl-CoA:acetate CoA-transferase. This specialized enzyme links the TCA cycle with acetate metabolism in these organisms. ... Most organisms utilize EC 6.2.1.5, succinate-CoA ligase (ADP-forming) (despite its name, the enzyme operates in the pathway in ... The cycle consumes acetate (in the form of acetyl-CoA) and water, reduces NAD+ to NADH, and produces carbon dioxide as a waste ... It is the oxidation of the acetate portion of acetyl-CoA that produces CO2 and water, with the energy thus released captured in ...
*  Eugenol
... which is in turn converted to feruloyl-CoA by the enzyme 4-hydroxycinnamoyl-CoA ligase (4CL). Next, feruloyl-CoA is reduced to ... forming coniferyl acetate. Finally, coniferyl acetate is converted to eugenol via the enzyme eugenol synthase 1 and the use of ... coniferaldehyde by cinnamoyl-CoA reductase (CCR). Coniferaldeyhyde is then further reduced to coniferyl alcohol by cinnamyl- ...
*  Fatty acid metabolism
Once inside the cell long-chain-fatty-acid-CoA ligase catalyzes the reaction between a fatty acid molecule with ATP (which is ... acetate) units, which, combined with co-enzyme A, form molecules of acetyl CoA, which condense with oxaloacetate to form ... Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into the fatty ... acetyl-CoA and 1 molecule of propionyl-CoA per molecule of fatty acid. Each beta oxidative cut of the acyl-CoA molecule yields ...
*  Oxalyl-CoA decarboxylase
Oxalate-CoA ligase Formyl-CoA transferase Oxalate CoA-transferase Baetz, A.L. and Allison, M.J. "Purification and ... a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon ... The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). Other names in common use include ... This addition is followed by the decarboxylation of oxalyl-CoA, and then the oxidation and removal of formyl-CoA to regenerate ...
*  Biosynthesis
These may be metal ions, vitamin derivatives such as NADH and acetyl CoA, or non-vitamin derivatives such as ATP. In the case ... Okazaki fragments are covalently joined by DNA ligase to form a continuous strand. Then, to complete DNA replication, RNA ... Organisms that use ethanol and acetate as the major carbon source utilize the glyconeogenic pathway to synthesize glycine. The ... Cholesterol is synthesized from acetyl CoA. The pathway is shown below: More generally, this synthesis occurs in three stages, ...
*  Citrate synthase
The enzyme is inhibited by high ratios of ATP:ADP, acetyl-CoA:CoA, and NADH:NAD, as high concentrations of ATP, acetyl-CoA, and ... Citrate synthase catalyzes the condensation reaction of the two-carbon acetate residue from acetyl coenzyme A and a molecule of ... These experiments have revealed that this single site alternates between two forms, which participate in ligase and hydrolase ... This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citroyl-CoA ...
*  List of EC numbers (EC 3)
... acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA ... glutamate-ammonia ligase) hydrolase EC 3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase EC 3.1.4.17: 3',5'-cyclic- ... methylumbelliferyl-acetate deacetylase EC 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase EC 3.1.1.58: N- ... bile-acid-CoA hydrolase EC 3.1.2.27: choloyl-CoA hydrolase EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase EC 3.1.2.29: ...
*  List of EC numbers (EC 2)
3-oxoadipate CoA-transferase EC 2.8.3.7: succinate-citramalate CoA-transferase EC 2.8.3.8: acetate CoA-transferase EC 2.8.3.9: ... protein ligase EC 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase EC 2.7.7.65: diguanylate cyclase EC 2.7.7.66: ... succinyl-CoA:(R)-benzylsuccinate CoA-transferase EC 2.8.3.16: formyl-CoA transferase EC 2.8.3.17: cinnamoyl-CoA:phenyllactate ... oxalate CoA-transferase EC 2.8.3.3: malonate CoA-transferase EC 2.8.3.4: deleted EC 2.8.3.5: 3-oxoacid CoA-transferase EC 2.8. ...
Human Metabolome Database: Showing metabocard for Propionyl-CoA (HMDB0001275)  Human Metabolome Database: Showing metabocard for Propionyl-CoA (HMDB0001275)
Involved in acetate-CoA ligase activity. Specific function:. Not Available. Gene Name:. ACSS2. Uniprot ID:. Q96FY7 Molecular ... Propionyl-CoA + Acetyl-CoA → Coenzyme A + 2-Methylacetoacetyl-CoA. details. Propionyl-CoA + Chenodeoxycholoyl-CoA → Coenzyme A ... Propionyl-CoA + Acetyl-CoA → Coenzyme A + 2-Methylacetoacetyl-CoA. details. Propionyl-CoA + Chenodeoxycholoyl-CoA → Coenzyme A ... Involved in acetate-CoA ligase activity. Specific function:. Important for maintaining normal body temperature during fasting ...
more infohttp://www.hmdb.ca/metabolites/HMDB0001275
Acetate-CoA ligase (ADP-forming) - Wikipedia  Acetate-CoA ligase (ADP-forming) - Wikipedia
... an acetate-CoA ligase (ADP-forming) (EC 6.2.1.13) is an enzyme that catalyzes the chemical reaction ATP + acetate + CoA ⇌ {\ ... The systematic name of this enzyme class is acetate:CoA ligase (ADP-forming). Other names in common use include acetyl-CoA ... acetate, and CoA, whereas its 3 products are ADP, phosphate, and acetyl-CoA. This enzyme belongs to the family of ligases, ... Reeves RE, Warren LG, Susskind B, Lo HS (1977). "An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica. ...
more infohttps://en.wikipedia.org/wiki/Acetate%E2%80%94CoA_ligase_(ADP-forming)
Acetate-CoA Ligase (Acetyl-CoA Synthetase) from yeast, lyophilizate  Acetate-CoA Ligase (Acetyl-CoA Synthetase) from yeast, lyophilizate
Acetate-CoA Ligase (Acetyl-CoA Synthetase) material number and pack size: Material Number. Pack Size. ... Use Acetate-CoA Ligase (Acetyl-CoA Synthetase) in diagnostic tests for the determination of acetic acid in combination with ... Ligase that catalyzes the synthesis of acetyl-CoA from acetate and coenzyme A.. +- ... Specific activity (+37°C, acetate): ≥4 U/mg protein. Protein (Biuret): ≤0.25 mg/mg lyophilizate. Acetate (enzymatic): ≤0.1%. ...
more infohttps://custombiotech.roche.com/home/Product_Details/3_1_1_5_7_1.html
Ac CoA synth (MF 01123) | InterPro | EMBL-EBI  Ac CoA synth (MF 01123) | InterPro | EMBL-EBI
Ac_CoA_synth (MF_01123). Accession MF_01123 Integration. Acetate-CoA ligase (IPR011904) Member database. HAMAP. HAMAP stands ...
more infohttp://www.ebi.ac.uk/interpro/ISignatureOverview?sig=MF_01123&query=Q
Anti-ACSS2 antibody KO Tested (ab66038) | Abcam  Anti-ACSS2 antibody KO Tested (ab66038) | Abcam
Acetate thiokinase antibody. *Acetate--CoA ligase antibody. *Acetyl CoA synthetase antibody. *Acetyl Coenzyme A synthetase 2 ( ... Activates acetate so that it can be used for lipid synthesis or for energy generation. ... Decreased expression of acetyl-CoA synthase 2 promotes metastasis and predicts poor prognosis in hepatocellular carcinoma.. ... Acetate CoA ligase antibody. * ... Acyl CoA synthetase short chain family member 2 antibody. *Acyl ...
more infohttps://www.abcam.com/acss2-antibody-ab66038.html
acs - Acetyl-coenzyme A synthetase - Escherichia coli (strain K12) - acs gene & protein  acs - Acetyl-coenzyme A synthetase - Escherichia coli (strain K12) - acs gene & protein
In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the ... In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. ... Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and ... acetate-CoA ligase activity Source: CACAO ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the function ...
more infohttp://www.uniprot.org/uniprot/P27550
acsA1 - Acetyl-coenzyme A synthetase 1 - Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440) - acsA1 gene ...  acsA1 - Acetyl-coenzyme A synthetase 1 - Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440) - acsA1 gene ...
In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the ... In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. ... Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and ... Acetate--CoA ligase 1UniRule annotation. Manual assertion according to rulesi ...
more infohttps://www.uniprot.org/uniprot/Q88EH6
Expression of ACSS3 in cancer - Summary - The Human Protein Atlas  Expression of ACSS3 in cancer - Summary - The Human Protein Atlas
GO:0003987 [acetate-CoA ligase activity]. GO:0005524 [ATP binding]. GO:0005739 [mitochondrion]. GO:0005759 [mitochondrial ... Acyl-CoA synthetase short-chain family member 3. Protein classi. Protein class the gene product belongs to according to ... Ligase. Predicted membrane proteins. Prediction method-based. Membrane proteins predicted by MDM. MEMSAT3 predicted membrane ... Acyl-CoA synthetase short-chain family member 3, mitochondrial; FLJ21963 protein, isoform CRA_b ...
more infohttp://www.proteinatlas.org/ENSG00000111058-ACSS3/pathology
EC 6.2.1  EC 6.2.1
Accepted name: acetate CoA ligase. Reaction: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. Other name(s): acetyl-CoA ... EC 6.2.1.6 glutarate CoA ligase. EC 6.2.1.7 cholate CoA ligase. EC 6.2.1.8 oxalate CoA ligase. EC 6.2.1.9 malate CoA ligase. EC ... CoA ligase; p-coumaryl-CoA ligase; p-hydroxycinnamic acid:CoA ligase; 4CL Systematic name: 4-coumarate:CoA ligase (AMP-forming) ... phenylacetyl-CoA ligase; PA-CoA ligase; phenylacetyl-CoA ligase (AMP-forming). Systematic name: phenylacetate:CoA ligase (AMP- ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC6/0201.html
S cerevisiae.fasta  S cerevisiae.fasta
GO:0003824,catalytic activity,IEA; GO:0003987,acetate-CoA ligase activity,IDA; GO:0003987,acetate-CoA ligase activity,IEA; GO: ... GO:0004812,tRNA ligase activity,IEA; GO:0004814,arginine-tRNA ligase activity,IEA; GO:0004814,arginine-tRNA ligase activity,IMP ... aspartate-tRNA ligase activity,IEA; GO:0004816,asparagine-tRNA ligase activity,IDA; GO:0004816,asparagine-tRNA ligase activity, ... GO:0000151,ubiquitin ligase complex,IEA; GO:0004842,ubiquitin-protein ligase activity,IEA; GO:0005624,membrane fraction,IDA; GO ...
more infohttp://megasun.bch.umontreal.ca/Software/Scerevisiae_PEDANT/S_cerevisiae.fasta.html
Human Metabolome Database: Showing metabocard for Phosphoric acid (HMDB0002142)  Human Metabolome Database: Showing metabocard for Phosphoric acid (HMDB0002142)
Involved in acetate-CoA ligase activity. Specific function:. Important for maintaining normal body temperature during fasting ... 7. Acetyl-CoA carboxylase 2. General function:. Involved in acetyl-CoA carboxylase activity. Specific function:. ACC-beta may ... Essential for energy expenditure under ketogenic conditions (By similarity). Converts acetate to acetyl-CoA so that it can be ... Acetyl-CoA carboxylase 1. General function:. Involved in acetyl-CoA carboxylase activity. Specific function:. Catalyzes the ...
more infohttp://www.hmdb.ca/metabolites/HMDB0002142
Metatranscriptomic Analysis of Arctic Peat Soil Microbiota | Applied and Environmental Microbiology  Metatranscriptomic Analysis of Arctic Peat Soil Microbiota | Applied and Environmental Microbiology
... acetate-CoA ligase (AMP forming); 2.7.2.1, acetate kinase; 2.3.1.8, phosphate acetyltransferase; 1.2.99.2, carbon monoxide ... the transcripts for AMP-forming acetate-coenzyme A ligase (EC 6.2.1.1), a key enzyme for acetoclastic methanogenesis by ... and methylamines in addition to acetate. Particularly, transcripts for methanogenesis from acetate and formate were abundant in ... However, whether this is due to homoacetogenic competition for H2 or to formate and acetate being major fermentation products ...
more infohttps://aem.asm.org/content/80/18/5761
Gene Ontology  Gene Ontology
acetate-CoA ligase (ADP-forming) activity. Molecular Function. GO:0047676. arachidonate-CoA ligase activity. ... acyl-CoA synthetase long-chain family member 1:. Biological Process. GO:0001676. long-chain fatty acid metabolic process. ... phytanate-CoA ligase activity. Molecular Function. GO:0102391. decanoate-CoA ligase activity. ...
more infohttps://www.komp.org/GO.php?geneid=18183
KEGG SSDB Best Search Result: tpe:Tpen 1227  KEGG SSDB Best Search Result: tpe:Tpen 1227
bgd:bgla_1g28680 Acetate--CoA ligase K01895 660 105 ( 1) 30 0.388 49 -, 2 bgo:BM43_321 acetate--CoA ligase K01895 660 105 ( 1) ... bgl:bglu_1g25360 Acetate--CoA ligase K01895 660 106 ( -) 30 0.420 50 -, 1 bgp:BGL_1c27120 acetate-CoA ligase K01895 660 106 ( 4 ... bmu:Bmul_1085 acetate--CoA ligase K01895 660 105 ( 0) 30 0.388 49 -, 3 bmul:NP80_2307 acetate--CoA ligase K01895 660 105 ( 0) ... bpd:BURPS668_A0628 acetate--CoA ligase K01895 660 105 ( 3) 30 0.388 49 -, 2 bpk:BBK_5595 acetate--CoA ligase K01895 660 105 ( 3 ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=tpe:Tpen_1227
Acetyl-CoA synthetase from Bacillus subtilis, Recombinant(EC 6.2.1.1) - Creative Enzymes  Acetyl-CoA synthetase from Bacillus subtilis, Recombinant(EC 6.2.1.1) - Creative Enzymes
... involved in metabolism of acetate. It is in the ligase class of enzymes, meaning that it catalyzes t ... Acetyl-CoA synthetase or Acetate-CoA ligase is an enzyme (EC 6.2.1.1) ... Acetyl-CoA synthetase or Acetate-CoA ligase is an enzyme (EC 6.2.1.1) involved in metabolism of acetate. It is in the ligase ... Acetyl-CoA synthetase; Acetate-CoA ligase; EC 6.2.1.1; Acetate thiokinase; Acetyl-activating enzyme; Acetyl-CoA synthase; Acyl- ...
more infohttps://www.creative-enzymes.com/product/AcetylCoA-Synthetase-From-Bacillus-Subtilis-Recombinant_1733.html
Find Research Outputs
             - University of Texas Southwestern Medical Center  Find Research Outputs - University of Texas Southwestern Medical Center
Acetate-CoA Ligase Lipid Metabolism Fats Genes Acetyl Coenzyme A ACTG2-Associated Visceral Myopathy With Chronic Intestinal ...
more infohttps://utsouthwestern.influuent.utsystem.edu/en/publications/?format=&page=1
Carbon metabolic pathways of D. hafniense DCB-2. The pa | Open-i  Carbon metabolic pathways of D. hafniense DCB-2. The pa | Open-i
acetate-CoA ligase; Dhaf_0467. 11b. acetyl-CoA hydrolase/transferase; Dhaf_0603, Dhaf_2858, Dhaf_4529. 12. aldehyde ... acetate-CoA ligase; Dhaf_0467. 11b. acetyl-CoA hydrolase/transferase; Dhaf_0603, Dhaf_2858, Dhaf_4529. 12. aldehyde ... succinate-CoA ligase (ADP-forming); Dhaf_0192, Dhaf_2066. 17. alcohol dehydrogenase; Dhaf_2180, Dhaf_0588. 18. succinate ... succinate-CoA ligase (ADP-forming); Dhaf_0192, Dhaf_2066. 17. alcohol dehydrogenase; Dhaf_2180, Dhaf_0588. 18. succinate ...
more infohttps://openi.nlm.nih.gov/detailedresult.php?img=PMC3306737_1471-2180-12-21-2&req=4
Journal: Applied microbiology and biotechnology / Publication Year: 2013 / Source: 2013 v.97 no.14 - PubAg Search Results  Journal: Applied microbiology and biotechnology / Publication Year: 2013 / Source: 2013 v.97 no.14 - PubAg Search Results
Candida utilis; Clostridium acetobutylicum; Clostridium beijerinckii; acetate-CoA ligase; acetates; acetyl-CoA ... Because the engineered strain accumulated acetate, isopropanol ti .... DOI:. 10.1007/s00253-013-4964-0. PubMed:. 23674152. http ... A genetically-engineered strain of the yeast Candida utilis harboring genes encoding (1) an acetoacetyl-CoA transferase from ... Clostridium butyricum; Enterococcus faecium; acetyl-CoA carboxylase; average daily intake; breast muscle; broiler chickens; ...
more infohttps://pubag.nal.usda.gov/?f%5Bjournal_name%5D%5B%5D=Applied+microbiology+and+biotechnology&f%5Bpublication_year_rev%5D%5B%5D=7987-2013&f%5Bsource%5D%5B%5D=2013+v.97+no.14&per_page=100
人Acetyl CoA synthetase多肽| Abcam中国  人Acetyl CoA synthetase多肽| Abcam中国
购买Abcam人Acetyl CoA synthetase多肽(ab71894),提供28,000多种信号蛋白、细胞因子、趋化因子 ... Acetate CoA ligase. *Acetate thiokinase. *Acetate--CoA ligase. *Acetyl CoA synthetase. *Acetyl Coenzyme A synthetase 2 (ADP ... 人Acetyl CoA synthetase多肽. 参阅全部 Acetyl CoA synthetase 蛋白酶. ... Activates acetate so that it can be used for lipid
more infohttp://www.abcam.cn/human-acetyl-coa-synthetase-peptide-ab71894.html
Sequence Similarity Search - BLAST  Sequence Similarity Search - BLAST
ban:BA_4915 K01895 acetyl-CoA synthetase [EC:6.2.1.1] , (RefSeq) acsA; acetate--CoA ligase (A) ...
more infohttp://www.genome.jp/tools-bin/search_sequence?prog=blast&seqid=ban:BA_4915+aa
Panoply™ Human ACSS2 Knockdown Stable Cell Line - Creative Biogene  Panoply™ Human ACSS2 Knockdown Stable Cell Line - Creative Biogene
This gene encodes a cytosolic enzyme that catalyzes the activation of acetate for use in lipid synthesis and energy generation ... AMP binding; ATP binding; acetate-CoA ligase activity;. Related Products. *Transfected Stable Cell Lines ...
more infohttps://www.creative-biogene.com/Panoply-Human-ACSS2-Knockdown-Stable-Cell-Line-CSC-DC000181-1253200-14.html
SA2402 - AureoWiki  SA2402 - AureoWiki
product: acetate-CoA ligase. ⊟Genome View[edit source , edit]. Meta Function Gene Functional Class (TIGRFam Main Role) Color ... dicarboxylate--CoA ligase PimA (TIGR03205; EC 6.2.1.23; HMM-score: 176.4) acyl-CoA ligase (AMP-forming), exosortase A- ... Acetate--CoA ligaseATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. *TIGRFAM: benzoate-CoA ligase family (TIGR02262; HMM- ... propionate--CoA ligase (TIGR02316; EC 6.2.1.17; HMM-score: 160.6) Cell structureCell envelopeBiosynthesis and degradation of ...
more infohttp://aureowiki.med.uni-greifswald.de/SA2402
Methionine gamma-lyase - Wikipedia  Methionine gamma-lyase - Wikipedia
2-oxobutyrate is ultimately decomposed by acetate-CoA ligase and produces ATP, thus contributing to ATP metabolism. MGL also ...
more infohttps://en.wikipedia.org/wiki/Methionine_gamma-lyase
  • Oxalyl-CoA decarboxylase is extremely important for the elimination of ingested oxalates found in human foodstuffs like coffee, tea, and chocolate, and the ingestion of such foods in the absence of Oxalobacter formigenes in the gut can result in kidney disease or even death as a result of oxalate poisoning. (wikipedia.org)
  • Beta oxidation, in the mitochondrial matrix, then cuts the long carbon chains of the fatty acids (in the form of acyl-CoA molecules) into a series of two-carbon (acetate) units, which, combined with co-enzyme A, form molecules of acetyl CoA, which condense with oxaloacetate to form citrate at the "beginning" of the citric acid cycle. (wikipedia.org)
  • In addition to acetyl-CoA production, the reverse can occur with ACS producing acetate, CO and returning the methyl piece back to the corrinoid protein. (wikipedia.org)
  • Coniferyl alcohol is then converted to an ester in the presence of the substrate CH3COSCoA, forming coniferyl acetate. (wikipedia.org)
  • The liberated carnitine is shuttled back to the cytosol, as an acyl-CoA is shuttled into the matrix. (wikipedia.org)
  • The acetyl-CoA degradation and related genes are shown in more detail (boxed). (nih.gov)