Acetoin Dehydrogenase: An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.Acetoin: A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.ButanonesButylene Glycols: 4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.L-Lactate Dehydrogenase: A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.Alcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.Dissertations, Academic as Topic: Dissertations embodying results of original research and especially substantiating a specific view, e.g., substantial papers written by candidates for an academic degree under the individual direction of a professor or papers written by undergraduates desirous of achieving honors or distinction.Gastropoda: A class in the phylum MOLLUSCA comprised of SNAILS and slugs. The former have coiled external shells and the latter usually lack shells.Triploidy: Polyploidy with three sets of chromosomes. Triploidy in humans are 69XXX, 69XXY, and 69XYY. It is associated with HOLOPROSENCEPHALY; ABNORMALITIES, MULTIPLE; PARTIAL HYDATIDIFORM MOLE; and MISCARRAGES.Academic DissertationsLibraries, Digital: Libraries in which a major proportion of the resources are available in machine-readable format, rather than on paper or MICROFORM.Mollusca: A phylum of the kingdom Metazoa. Mollusca have soft, unsegmented bodies with an anterior head, a dorsal visceral mass, and a ventral foot. Most are encased in a protective calcareous shell. It includes the classes GASTROPODA; BIVALVIA; CEPHALOPODA; Aplacophora; Scaphopoda; Polyplacophora; and Monoplacophora.Nursing Research: Research carried out by nurses, generally in clinical settings, in the areas of clinical practice, evaluation, nursing education, nursing administration, and methodology.MercaptoethanolAlcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Succimer: A mercaptodicarboxylic acid used as an antidote to heavy metal poisoning because it forms strong chelates with them.Methanosarcina 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.Urease: An enzyme that catalyzes the conversion of urea and water to carbon dioxide and ammonia. EC 3.5.1.5.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.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.Hexosaminidases: Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.Man-Machine Systems: A system in which the functions of the man and the machine are interrelated and necessary for the operation of the system.5,10-Methylenetetrahydrofolate Reductase (FADH2): An FAD-dependent oxidoreductase found primarily in BACTERIA. It is specific for the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. This enzyme was formerly listed as EC 1.1.1.68 and 1.1.99.15.Pterygoid Muscles: Two of the masticatory muscles: the internal, or medial, pterygoid muscle and external, or lateral, pterygoid muscle. Action of the former is closing the jaws and that of the latter is opening the jaws, protruding the mandible, and moving the mandible from side to side.Neurospora crassa: A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies.Leuconostocaceae: A family of gram-positive bacteria in the order Lactobacillales. Lactic acid is the main product of their carbohydrate metabolism.Lactobacillales: An order of gram-positive bacteria in the class Bacilli, that have the ability to ferment sugars to lactic acid. They are widespread in nature and commonly used to produce fermented foods.Glutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Genomics: The systematic study of the complete DNA sequences (GENOME) of organisms.Sodium-Hydrogen Antiporter: A plasma membrane exchange glycoprotein transporter that functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens.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.Genome, Bacterial: The genetic complement of a BACTERIA as represented in its DNA.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.Software: Sequential operating programs and data which instruct the functioning of a digital computer.Deltaproteobacteria: A group of PROTEOBACTERIA represented by morphologically diverse, anaerobic sulfidogens. Some members of this group are considered bacterial predators, having bacteriolytic properties.Desulfuromonas: A genus of gram-negative, anaerobic, nonsporeforming bacteria in the family Desulfuromonadaceae. It is found in anoxic marine sediments.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Cytochrome c Group: A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)HSP40 Heat-Shock Proteins: A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.Barth Syndrome: Rare congenital X-linked disorder of lipid metabolism. Barth syndrome is transmitted in an X-linked recessive pattern. The syndrome is characterized by muscular weakness, growth retardation, DILATED CARDIOMYOPATHY, variable NEUTROPENIA, 3-methylglutaconic aciduria (type II) and decreases in mitochondrial CARDIOLIPIN level. Other biochemical and morphological mitochondrial abnormalities also exist.Tripterygium: A plant genus of the family CELASTRACEAE that is a source of triterpenoids and diterpene epoxides such as triptolide.Medication Adherence: Voluntary cooperation of the patient in taking drugs or medicine as prescribed. This includes timing, dosage, and frequency.Peer Group: Group composed of associates of same species, approximately the same age, and usually of similar rank or social status.Video Games: A form of interactive entertainment in which the player controls electronically generated images that appear on a video display screen. This includes video games played in the home on special machines or home computers, and those played in arcades.Videotape Recording: Recording of visual and sometimes sound signals on magnetic tape.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.Peer Review, Research: The evaluation by experts of the quality and pertinence of research or research proposals of other experts in the same field. Peer review is used by editors in deciding which submissions warrant publication, by granting agencies to determine which proposals should be funded, and by academic institutions in tenure decisions.Peer Review: An organized procedure carried out by a select committee of professionals in evaluating the performance of other professionals in meeting the standards of their specialty. Review by peers is used by editors in the evaluation of articles and other papers submitted for publication. Peer review is used also in the evaluation of grant applications. It is applied also in evaluating the quality of health care provided to patients.

Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. (1/20)

A recent study indicated that Bacillus subtilis catabolizes acetoin by enzymes encoded by the acu gene cluster (F. J. Grundy, D. A. Waters, T. Y. Takova, and T. M. Henkin, Mol. Microbiol. 10:259-271, 1993) that are completely different from those in the multicomponent acetoin dehydrogenase enzyme system (AoDH ES) encoded by aco gene clusters found before in all other bacteria capable of utilizing acetoin as the sole carbon source for growth. By hybridization with a DNA probe covering acoA and acoB of the AoDH ES from Clostridium magnum, genomic fragments from B. subtilis harboring acoA, acoB, acoC, acoL, and acoR homologous genes were identified, and some of them were functionally expressed in E. coli. Furthermore, acoA was inactivated in B. subtilis by disruptive mutagenesis; these mutants were impaired to express PPi-dependent AoDH E1 activity to remove acetoin from the medium and to grow with acetoin as the carbon source. Therefore, acetoin is catabolized in B. subtilis by the same mechanism as all other bacteria investigated so far, leaving the function of the previously described acu genes obscure.  (+info)

Interplay of organic and biological chemistry in understanding coenzyme mechanisms: example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids. (2/20)

With the publication of the three-dimensional structures of several thiamin diphosphate-dependent enzymes, the chemical mechanism of their non-oxidative and oxidative decarboxylation reactions is better understood. Chemical models for these reactions serve a useful purpose to help evaluate the additional catalytic rate acceleration provided by the protein component. The ability to generate, and spectroscopically observe, the two key zwitterionic intermediates invoked in such reactions allowed progress to be made in elucidating the rates and mechanisms of the elementary steps leading to and from these intermediates. The need remains to develop chemical models, which accurately reflect the enzyme-bound conformation of this coenzyme.  (+info)

Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. (3/20)

Bacillus subtilis grown in media containing amino acids or glucose secretes acetate, pyruvate, and large quantities of acetoin into the growth medium. Acetoin can be reused by the bacteria during stationary phase when other carbon sources have been depleted. The acoABCL operon encodes the E1alpha, E1beta, E2, and E3 subunits of the acetoin dehydrogenase complex in B. subtilis. Expression of this operon is induced by acetoin and repressed by glucose in the growth medium. The acoR gene is located downstream from the acoABCL operon and encodes a positive regulator which stimulates the transcription of the operon. The product of acoR has similarities to transcriptional activators of sigma 54-dependent promoters. The four genes of the operon are transcribed from a -12, -24 promoter, and transcription is abolished in acoR and sigL mutants. Deletion analysis showed that DNA sequences more than 85 bp upstream from the transcriptional start site are necessary for full induction of the operon. These upstream activating sequences are probably the targets of AcoR. Analysis of an acoR'-'lacZ strain of B. subtilis showed that the expression of acoR is not induced by acetoin and is repressed by the presence of glucose in the growth medium. Transcription of acoR is also negatively controlled by CcpA, a global regulator of carbon catabolite repression. A specific interaction of CcpA in the upstream region of acoR was demonstrated by DNase I footprinting experiments, suggesting that repression of transcription of acoR is mediated by the binding of CcpA to the promoter region of acoR.  (+info)

Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney. (4/20)

In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lung-specific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for alpha-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and l-xylulose, and were inhibited competitively by n-butyric acid. Therefore, the proteins are designated as dicarbonyl/l-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and l-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC ) are identical to l-xylulose reductase (EC ), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.  (+info)

Effect of substrates on acetoin production by Torulopsis colliculosa and Enterobacter species. (5/20)

Under optimal conditions, Torulopsis colliculosa NRRL 172 and Enterobacter B-87 (ATCC 27613) produced 50 to 500 mg of acetoin per g of substrate. Whereas cane molasses, gur, glucose, and sucrose were suitable substrates for acetoin production, lactose and mannitol supported very good growth but yielded little or no acetoin. Production of acetoin increased with increases in the concentration of glucose, yeast extract, and peptone. Combination of substrates and intermittent feeding of substrate failed to increase the yields.  (+info)

Plasmid-encoded diacetyl (acetoin) reductase in Leuconostoc pseudomesenteroides. (6/20)

A plasmid-borne diacetyl (acetoin) reductase (butA) from Leuconostoc pseudomesenteroides CHCC2114 was sequenced and cloned. Nucleotide sequence analysis revealed an open reading frame encoding a protein of 257 amino acids which had high identity at the amino acid level to diacetyl (acetoin) reductases reported previously. Downstream of the butA gene of L. pseudomesenteroides, but coding in the opposite orientation, a putative DNA recombinase was identified. A two-step PCR approach was used to construct FPR02, a butA mutant of the wild-type strain, CHCC2114. FPR02 had significantly reduced diacetyl (acetoin) reductase activity with NADH as coenzyme, but not with NADPH as coenzyme, suggesting the presence of another diacetyl (acetoin)-reducing activity in L. pseudomesenteroides. Plasmid-curing experiments demonstrated that the butA gene is carried on a 20-kb plasmid in L. pseudomesenteroides.  (+info)

Alpha,beta-dicarbonyl reduction by Saccharomyces D-arabinose dehydrogenase. (7/20)

An alpha,beta-dicarbonyl reductase activity was purified from Saccharomyces cerevisiae and identified as the cytosolic enzyme D-Arabinose dehydrogenase (ARA1) by MALDI-TOF/TOF. Size exclusion chromatography analysis of recombinant Ara1p revealed that this protein formed a homodimer. Ara1p catalyzed the reduction of the reactive alpha,beta-dicarbonyl compounds methylglyoxal, diacetyl, and pentanedione in a NADPH dependant manner. Ara1p had apparent Km values of approximately 14 mM, 7 mM and 4 mM for methylglyoxal, diacetyl and pentanedione respectively, with corresponding turnover rates of 4.4, 6.9 and 5.9 s(-1) at pH 7.0. pH profiling showed that Ara1p had a pH optimum of 4.5 for the diacetyl reduction reaction. Ara1p also catalyzed the NADP+ dependant oxidation of acetoin; however this back reaction only occurred at alkaline pH values. That Ara1p was important for degradation of alpha,beta-dicarbonyl substrates was further supported by the observation that ara1-Delta knockout yeast mutants exhibited a decreased growth rate phenotype in media containing diacetyl.  (+info)

Purification and characterization of acetoin:2,6-dichlorophenolindophenol oxidoreductase, dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase enzyme system. (8/20)

Dihydrolipoamide dehydrogenase (DHLDH), dihydrolipoamide acetyltransferase (DHLTA), and acetoin: 2,6-dichlorophenolindophenol oxidoreductase (Ao:DCPIP OR) were purified from acetoin-grown cells of Pelobacter carbinolicus. DHLDH had a native Mr of 110,000, consisted of two identical subunits of Mr 54,000, and reacted only with NAD(H) as a coenzyme. The N-terminal amino acid sequence included the flavin adenine dinucleotide-binding site and exhibited a high degree of homology to other DHLDHs. DHLTA had a native Mr of greater than 500,000 and consisted of subunits identical in size (Mr 60,000). The enzyme was highly sensitive to proteolytic attack. During limited tryptic digestion, two major fragments of Mr 32,500 and 25,500 were formed. Ao:DCPIP OR consisted of two different subunits of Mr 37,500 and 38,500 and had a native Mr in the range of 143,000 to 177,000. In vitro in the presence of DCPIP, it catalyzed a thiamine pyrophosphate-dependent oxidative-hydrolytic cleavage of acetoin, methylacetoin, and diacetyl. The combination of purified Ao:DCPIP OR, DHLTA, and DHLDH in the presence of thiamine pyrophosphate and the substrate acetoin or methylacetoin resulted in a coenzyme A-dependent reduction of NAD. In the strictly anaerobic acetoin-utilizing bacteria P. carbinolicus, Pelobacter venetianus, Pelobacter acetylenicus, Pelobacter propionicus, Acetobacterium carbinolicum, and Clostridium magnum, the enzymes Ao:DCPIP OR, DHLTA, and DHLDH were induced during growth on acetoin, whereas they were absent or scarcely present in cells grown on a nonacetoinogenic substrate.  (+info)

One research study found that in the past, c-type cytochromes in Pelobacter species had not been detected even though close relatives in the Geobacteraceae family have many c-type cytochromes present. Careful study of the entire completed genome sequence of Pelobacter carbinolicus found 14 open reading frames that encode for c-type cytochromes. It was found that three c-type cytochrome genes were expressed during iron reduction, which suggests that these particular proteins may play a role in electron transfer to iron. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels of acetoin-fermenting Pelobacter carbinolicus protein cells showed three heme-staining bands. In addition, many of the c-type cytochromes that genetic studies have realized are required for optimal iron reduction in G. sulfurreducens were not present in the P. carbinolicus genome. The results from this study suggest more in depth studies of the functions of c-type cytochromes may possibly be beneficial for further ...
Leuconostoc pseudomesenteroides is an intrinsically vancomycin-resistant, Gram-positive, coccus-shaped bacterium, with type strain NCDO 768. Farrow, J. A. E.; Facklam, R. R.; Collins, M. D. (1989). "Nucleic Acid Homologies of Some Vancomycin-Resistant Leuconostocs and Description of Leuconostoc citreum sp. nov. and Leuconostoc pseudomesenteroides sp. nov". International Journal of Systematic Bacteriology. 39 (3): 279-283. doi:10.1099/00207713-39-3-279. ISSN 0020-7713. Jofré M, Leonor; Sakurada Z, Andrea; Ulloa F, M. Teresa; Hormázabal O, J. Carlos; Godoy M, Viviana; Fernández O, Jorge; Gutiérrez M, Marcela; Monteverde O, M. Pilar; Castillo G, Marcela; Canales P, Ana (2006). "Infección por Leuconostoc en pacientes con síndrome de intestino corto, nutrición parenteral y alimentación enteral continua". Revista chilena de infectología. 23 (4). doi:10.4067/S0716-10182006000400008. ISSN 0716-1018. Cappelli, Elisabete A., et al. "Leuconostoc pseudomesenteroides as a cause of nosocomial urinary ...
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Acorda Therapeutics, Inc. (Nasdaq: ACOR) today announced its financial results for the second quarter ended June 30, 2012....ACOR
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Acorda Therapeutics, Inc. (Nasdaq: ACOR) today announced that the MILESTONE clinical study did not show sufficient efficacy to support further development of dalfampridine to improve post-stroke walking difficulties (PSWD)....ACOR
Leuconostoc citreum is a vancomycin-resistant, Gram-positive, coccus-shaped bacterium, with type strain NCDO 1837. Its genome has been sequenced. Farrow, J. A. E.; Facklam, R. R.; Collins, M. D. (1989). "Nucleic Acid Homologies of Some Vancomycin-Resistant Leuconostocs and Description of Leuconostoc citreum sp. nov. and Leuconostoc pseudomesenteroides sp. nov". International Journal of Systematic Bacteriology. 39 (3): 279-283. doi:10.1099/00207713-39-3-279. ISSN 0020-7713. Kim, J. F.; Jeong, H.; Lee, J.-S.; Choi, S.-H.; Ha, M.; Hur, C.-G.; Kim, J.-S.; Lee, S.; Park, H.-S.; Park, Y.-H.; Oh, T. K. (2008). "Complete Genome Sequence of Leuconostoc citreum KM20". Journal of Bacteriology. 190 (8): 3093-3094. doi:10.1128/JB.01862-07. ISSN 0021-9193. PMC 2293239 . PMID 18281406. Weng, P.F.; Wu, Z.F.; Lei, L.L. (2013). "Predictive Models for Growth ofLeuconostoc citreumand Its Dynamics in Pickled Vegetables with Low Salinity". Journal of Food Process Engineering. 36 (3): 284-291. ...
NAD-dependent (R,R)-butanediol dehydrogenase, catalyzes oxidation of (R,R)-2,3-butanediol to (3R)-acetoin, oxidation of meso-butanediol to (3S)-acetoin, and reduction of ...
The ability of Pelobacter carbinolicus to oxidize electron donors with electron transfer to the anodes of microbial fuel cells was evaluated because microorganisms closely related to Pelobacter species are generally abundant on the anodes of microbial fuel cells harvesting electricity from aquatic sediments. P. carbinolicus could not produce current in a microbial fuel cell with electron donors which support Fe(III) oxide reduction by this organism. Current was produced using a coculture of P. carbinolicus and Geobacter sulfurreducens with ethanol as the fuel. Ethanol consumption was associated with the transitory accumulation of acetate and hydrogen. G. sulfurreducens alone could not metabolize ethanol, suggesting that P. carbinolicus grew in the fuel cell by converting ethanol to hydrogen and acetate, which G. sulfurreducens oxidized with electron transfer to the anode. Up to 83% of the electrons available in ethanol were recovered as electricity and in the metabolic intermediate acetate. ...
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pyruvate decarboxylase ^ CO2. a-acetolactate/acetaldehyde-TPP. ,CO2. CO2 diacetyl reductase diacetyl -^ ^ ► acetoin reductase / % . NADH+H NAD. acetoin reductase c. NADH+H. NAD 2,3-butanediol catalyzed by a-acetolactate synthase and requiring high concentrations of pyruvate. The a-acetolactate is unstable in the presence of oxygen and is finally decarboxylated, nonenzy-matically, to form diacetyl. It is important to note that diacetyl is not necessarily the terminal end-product of the pathway. Further reduction of diacetyl can also occur, forming acetoin and 2,3-butanediol, compounds that contribute no flavor or aroma to the product.. Following the addition of the culture, the mix is incubated at 21°C to 22°C for twelve to sixteen hours. At the end of the fermentation, when the titratable acidity has reached 0.85% to 0.90% and the pH has decreased to about 4.5, the product is cooled to 2°C and agitated to break up the coagulum. Salt is usually added, and, if desired, butter granules or ...
DCXR antibody [4H10] (dicarbonyl/L-xylulose reductase) for FACS, IHC-P, WB. Anti-DCXR mAb (GTX84624) is tested in Human samples. 100% Ab-Assurance.
DCXR antibody [9C9] (dicarbonyl/L-xylulose reductase) for IHC-P, WB. Anti-DCXR mAb (GTX84626) is tested in Human samples. 100% Ab-Assurance.
Described as the mother of the Adult Children of Alcoholics movement, Dr. Woititz was a pioneer in the ACOA movement. The site offers insights into ACOA as well as information on Woititz books. ...
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Literatūras apskatā apkopota informācija par 2-alkilaizvietotu karbociklisko1,3-diketonu iegūšanas metodēm no 1952. līdz 2015. gadam, izmantojot datubāzes Reaxys, SciFinder, ScienceDirect un Espacenet. Bakalaura darba eksperimentālās daļas ietvaros sintezēti 2-arilmetil-cikloheksān-1,3-dioni, 9-aril-3,4,5,6,7,9-heksahidro-1H-ksantēn-1,8-(2H)-dioni, kā arī bis-2-arilmetilcikloheksān-1,3-dioni. Sintezētajiem savienojumiem veikti antiradikāļu aktivitātes pētījumi, izmantojot DPPH un GO testus; daži no savienojumiem uzrāda augstu antiradikāļu aktivitāti un salīdzinājumā ar komerciāli plaši izmantoto BHT izrāda gandrīz 3 reizes augstāku aktivitāti. Bakalaura darbs uzrakstīts latviešu valodā, tā apjoms 72 lpp. Darbs satur 11 attēlus, 6 tabulas, 35 shēmas, izmantoti 49 literatūras avoti ...
Acetoin (AC) and 2,3-butanediol (2,3-BD) as highly promising bio-based platform chemicals have received more attentions due to their wide range of applications. However, the non-efficient substrate conversion and mutually transition between AC and 2,3-BD in their natural producing strains not only led to a low selectivity but also increase the difficulty of downstream purification. Therefore, synthetic engineering of more suitable strains should be a reliable strategy to selectively produce AC and 2,3-BD, respectively. In this study, the respective AC (alsS and alsD) and 2,3-BD biosynthesis pathway genes (alsS, alsD, and bdhA) derived from Bacillus subtilis 168 were successfully expressed in non-natural AC and 2,3-BD producing Corynebacterium crenatum, and generated recombinant strains, C. crenatum SD and C. crenatum SDA, were proved to produce 9.86 g L−1 of AC and 17.08 g L−1 of 2,3-BD, respectively. To further increase AC and 2,3-BD selectivity, the AC reducing gene (butA) and lactic acid
Climacteric C2H4 biosynthesis includes (1) conversion of Asp to Met, (2) conversion of Met to C2H4, and (3) the Met recycling pathway (Yang and Hoffman, 1984). Conversion of Met to C2H4 is, at least in part, governed via transcriptional regulation of SAM, ACS, and ACO gene family members; however, these genes are regulated by different mechanisms. SAM1 transcripts accumulate preferentially in tomato pericarp during fruit maturation, while ACS2, ACS4, and ACO1 transcripts accumulate concomitantly with C2H4 biosynthesis and pericarp ripening. Based on the expression data presented here, it is apparent that transcriptional regulation may govern other stages of the C2H4 biosynthetic pathway as well. For example, TS expression decreases throughout pericarp development, while CGS expression increases during the transition from a mature green fruit to a ripening fruit in an Nr-dependent manner. These transcriptional changes could influence TS and CGS and shift carbon flux from the Thr pathway to the ...
Climacteric C2H4 biosynthesis includes (1) conversion of Asp to Met, (2) conversion of Met to C2H4, and (3) the Met recycling pathway (Yang and Hoffman, 1984). Conversion of Met to C2H4 is, at least in part, governed via transcriptional regulation of SAM, ACS, and ACO gene family members; however, these genes are regulated by different mechanisms. SAM1 transcripts accumulate preferentially in tomato pericarp during fruit maturation, while ACS2, ACS4, and ACO1 transcripts accumulate concomitantly with C2H4 biosynthesis and pericarp ripening. Based on the expression data presented here, it is apparent that transcriptional regulation may govern other stages of the C2H4 biosynthetic pathway as well. For example, TS expression decreases throughout pericarp development, while CGS expression increases during the transition from a mature green fruit to a ripening fruit in an Nr-dependent manner. These transcriptional changes could influence TS and CGS and shift carbon flux from the Thr pathway to the ...
Role of cerebrospinal fluid, creatine kinase and lactate dehydrogenase enzyme levels in diagnostic and prognostic evaluation of tubercular and pyogenic meningitis
tr:Q4C2L7_CROWT] Biotin/lipoyl attachment:Catalytic domain of components of various dehydrogenase complexes:E3 binding; K00627 pyruvate dehydrogenase E2 component (dihydrolipoamide acetyltransferase) [EC:2.3.1.12] ...
K00627 pyruvate dehydrogenase E2 component (dihydrolipoamide acetyltransferase) [EC:2.3.1.12] , (GenBank) Dihydrolipoyllysine-residue ...
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As long as your yeast is healthy and abundant and youre not cold-crashing the beer as soon as fermentation tails off, youll be fine. Ive fermented with a number of Saison and Belgian strains (though I cant remember which off the top of my head) and Ive never had any problems with diacetyl. Also, basically any strain thats known to produce diacetyl in over-abundance will say so on its spec sheet.. The elevated temperature many Belgians ferment at is actually a boon to yeasts reduction of diacetyl to flavor-neutral compounds after primary. Also, most Belgians are medium to medium-low flocculators (highly flocculent yeast tends to leave more diacetyl around). More yeast in suspension = more power to reduce diacetyl post-fermentation. To be safe, theres really no reason not to just let your beers sit for a week at primary temperature after fermentation is done to make extra sure all the D is gone. A small, virtually risk-free step you can take to ensure good beer.. As far as Im concerned ...
Four π-expanded α,β-unsaturated 1,3-diketones have been prepared via attaching strong electron-donating and electron-withdrawing groups at positions 9 and 10 of the anthracene scaffold. The strategic incorporation of (C12H25)2N groups at the periphery of these D-π-A molecules resulted in dyes with excellent Celebrating 175 years of the Royal Society of Chemistry
Following treatment with the mutagen N-methyl-N-nitro-N-nitrosoguanidine, three mutants of Lactococcus lactis subsp. lactis biovar diacetylactis CNRZ 483 that produced diacetyl and acetoin from glucose were isolated. The lactate dehydrogenase activity of these mutants was strongly attenuated, and the mutants produced less lactate than the parental strain. The kinetic properties of lactate dehydrogenase of strain CNRZ 483 and the mutants revealed differences in the affinity of the enzyme for pyruvate, NADH, and fructose-1,6-diphosphate. When cultured aerobically, strain CNRZ 483 transformed 2.3% of glucose to acetoin and produced no diacetyl or 2,3-butanediol. Under the same conditions, mutants 483L1, 483L2, and 483L3 transformed 42.0, 78.9, and 75.8%, respectively, of glucose to C4 compounds (diacetyl, acetoin, and 2,3-butanediol). Anaerobically, strain CNRZ 483 produced no C4 compounds, while mutants 483L1, 483L2, and 483L3 transformed 2.0, 37.0, and 25.8% of glucose to acetoin and 2,3-butanediol. In
Maybe you thought a lot of genome papers provide "insights" - and youd be right. But did you know that even more genome papers "reveal" stuff? Its true! Heres a list of nearly 500 examples.. Abe, A., et al. (2012). "Genome sequencing reveals agronomically important loci in rice using MutMap." Nature Biotechnology 30(2): 174-178.. Acarkan, A., et al. (2000). "Comparative genome analysis reveals extensive conservation of genome organisation for Arabidopsis thaliana and Capsella rubella." Plant Journal 23(1): 55-62.. Ahola, V., et al. (2014). "The Glanville fritillary genome retains an ancient karyotype and reveals selective chromosomal fusions in Lepidoptera." Nature Communications 5.. Aklujkar, M., et al. (2012). "The genome of Pelobacter carbinolicus reveals surprising metabolic capabilities and physiological features." Bmc Genomics 13.. Alcaraz, L. D., et al. (2008). "The genome of Bacillus coahuilensis reveals adaptations essential for survival in the relic of an ancient marine ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Trifluoroaeetylated proteins (CF3CO-proteins), elicited in animals or humans exposed to halothane, were recognized by anti-CF3CO antibody, monospecific N6-trifluoroacetyl-L-lysine (CF3CO-Lys). Anti-CF
Five new tremulane-type sesquiterpenes, 11,12-dihydroxy-1-tremulen-5-one (1), 11,12-epoxy-12 beta-hydroxy-1-tremulen-5-one (2), 5 alpha, 12-dihydroxy-1-tremulen-11-yl 2(S)-pyroglutamate (3), 2 alpha, 11-dihydroxy-1(10)-tremulen-5,12-olide (4), and 10 beta,11-dihydroxy-5,6-seco-1,6(13)-tremuladien-5,12-olide (5), as well as three new aliphatic diketones, 2,3-dihydroxydodecane-4,7-dione (9 and 10) and 1-hydroxydecane-2,5-dione (11), together with three known sesquiterpene analogues, tremulenediol A (6), conocenol B (7), and conocenolide A (8), were isolated from cultures of the basidiomycete Conocybe siliginea ...
Popcorn lung disease lawyers are busy defending cases of many microwave popcorn workers across the US. The lawsuits involve the manufacturers use of a poisonous flavoring additive called diacetyl. Manufacturers quickly ceased use of diacetyl in favor of an alternative ingredient, 2,3-pentanedione, or PD. Recent reports, however, reveal that PD is just as toxic as diacetyl. … ...
This model represents one of several closely related clades of the dihydrolipoamide acetyltransferase subunit of the pyruvate dehydrogenase complex. It includes sequences from mitochondria and from alpha and beta branches of the proteobacteria, as well as from some other bacteria. Sequences from Gram-positive bacteria are not included. The non-enzymatic homolog protein X, which serves as an E3 component binding protein, falls within the clade phylogenetically but is rejected by its low score ...
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Date: Tue, 10 Nov 92 08:58:50 -0500 From: bradley at adx.adelphi.edu (Rob Bradley) Subject: racking after respiration I posted the following on Monday morning; it seems to have ended up in Tumbolia: B followed A, therefore A caused B. This fallacious form of reasoning is very common, and I plead guilty your honor, with an explanation. Peter Maxwell and I have had the following back-and-forth in #1007 & #1008: ,, ....then I got a ,, batch with an INCREDIBLE, UNDRINKABLE amount of diacetyl. End of ,, experiment. Back to racking on day 4. , ,Was this diacetyl produced BECAUSE you racked off earlier? What happened? ,How could racking earlier than day 4 result in this? I never claimed a causal connection, although I had hoped to get some evidence one way or another from other HBDers. Id love to find the time and patience to test scientifically the effect of racking at 24 hours on diacetyl production. My 1990 experiment came to an end based on laziness, not scientific method. Brewing a batch of ...
Methanol is an attractive alternative non-food feedstock for industrial fermentations that can be used instead of sugar-based raw materials. Here, the thermophilic and methylotrophic bacterium Bacillus methanolicus MGA3 was metabolically engineered to produce the platform chemical (R)-acetoin from methanol at 50 °C
EC 1.8.1.4; other names: lipoamide reductase (NADH); lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; diaphorase; the E3 component of α‐ketoacid dehydrogenase complexes, an FAD‐flavoprotein enzyme that catalyses the oxidation by NAD+ of dihydrolipoamide ... ...
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... serves as co-factor to the acetoin dehydrogenase complex catalyzing the conversion of acetoin (3-hydroxy-2-butanone ... complex the acetoin dehydrogenase complex. The most-studied of these is the pyruvate dehydrogenase complex. These complexes ... the pyruvate dehydrogenase complex the α-ketoglutarate dehydrogenase or 2-oxoglutarate dehydrogenase complex the branched-chain ... and methylamine group in the glycine cleavage complex or glycine dehydrogenase. 2-Oxoacid dehydrogenase transfer reactions ...
... acetoin dehydrogenase EC 2.3.1.191: UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase EC 2.3.1.192: glycine N- ... 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) kinase EC 2.7.11.5: (isocitrate dehydrogenase (NADP+)) kinase EC ... acetoin-ribose-5-phosphate transaldolase EC 2.2.1.5: 2-hydroxy-3-oxoadipate synthase EC 2.2.1.6: acetolactate synthase EC 2.2. ... pyruvate dehydrogenase (acetyl-transferring)) kinase EC 2.7.11.3: dephospho-(reductase kinase) kinase EC 2.7.11.4: ( ...
... acetoin dehydrogenase MeSH D08.811.682.047.070 --- alcohol dehydrogenase MeSH D08.811.682.047.150 --- carbohydrate ... acyl-coa dehydrogenases MeSH D08.811.682.660.150.100 --- acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 --- acyl-coa ... l-iditol 2-dehydrogenase MeSH D08.811.682.047.150.700.649 --- mannitol dehydrogenase MeSH D08.811.682.047.150.900 --- uridine ... 11-beta-hydroxysteroid dehydrogenase type 1 MeSH D08.811.682.047.436.174.600 --- 11-beta-hydroxysteroid dehydrogenase type 2 ...
In some bacteria, acetoin can also be reduced to 2,3-butanediol by acetoin reductase/2,3-butanediol dehydrogenase. The Voges- ... The conversion of acetoin into acetyl-CoA is catalysed by the acetoin dehydrogenase complex, following a mechanism largely ... Acetoin is a chiral molecule. The form produced by bacteria is (R)-acetoin. Acetoin is a neutral, four-carbon molecule used as ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ...
Taylor MB; Juni E (1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenase". Biochim. Biophys. Acta. 39 (3): 448- ... In enzymology, an acetoin racemase (EC 5.1.2.4) is an enzyme that catalyzes the chemical reaction (S)-acetoin ⇌ {\displaystyle ... The systematic name of this enzyme class is acetoin racemase. This enzyme is also called acetylmethylcarbinol racemase. This ... rightleftharpoons } (R)-acetoin This enzyme belongs to the family of isomerases, specifically those racemases and epimerases ...
... (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme ... Acetoin dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... "Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system". J. Bacteriol. 176 ( ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ...
Bertagnolli, B.L.; Hager, L.P. (1993). "Role of flavin in acetoin production by two bacterial pyruvate oxidases". Arch. Biochem ... Pyruvate dehydrogenase (quinone) (EC 1.2.5.1, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) ... Pyruvate dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ... dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate: ...
Other names in common use include L-butanediol dehydrogenase, L-BDH, and L(+)-2,3-butanediol dehydrogenase (L-acetoin forming ... In enzymology, a (S,S)-butanediol dehydrogenase (EC 1.1.1.76) is an enzyme that catalyzes the chemical reaction (S,S)-butane-2, ... Taylor MB; Juni E (1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenase". Biochim. Biophys. Acta. 39 (3): 448- ... whereas its 3 products are acetoin, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those ...
... (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)- ... "Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella ... acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction (S)-acetoin + NAD+ ⇌ {\displaystyle \ ... Different from EC 1.1.1.303, diacetyl reductase ((R)-acetoin forming). Giovannini, P.P.; Medici, A.; Bergamini, C.M.; Rippa, M ...
... (EC 1.1.1.303, (R)-acetoin dehydrogenase) is an enzyme with systematic name (R)- ... acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction (R)-acetoin + NAD+ ⇌ {\displaystyle \ ... This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol ... This enzyme is different from EC 1.1.1.304, diacetyl reductase ((S)-acetoin forming). Heidlas, J.; Tressl, R. (1990). " ...
D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D- ... aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1 ... 2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ oxidoreductase, 1 ... In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction (R,R)-butane-2,3 ...
... acetoin dehydrogenase EC 1.1.1.304: (S)-acetoin dehydrogenase EC 1.1.1.305: UDP-glucuronic acid dehydrogenase EC 1.1.1.306: S-( ... EC 1.1.1.1: alcohol dehydrogenase EC 1.1.1.2: alcohol dehydrogenase (NADP+) EC 1.1.1.3: homoserine dehydrogenase EC 1.1.1.4: (R ... L-arabinitol 4-dehydrogenase EC 1.1.1.13: L-arabinitol 2-dehydrogenase EC 1.1.1.14: L-iditol 2-dehydrogenase EC 1.1.1.15: D- ... glutaryl-CoA dehydrogenase EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase EC 1.3.8.8: long-chain acyl-CoA dehydrogenase EC 1.3 ...
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme ... Acetoin dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... "Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system". J. Bacteriol. 176 ( ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ...
2.3.1.190 acetoin dehydrogenase 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase ...
Other name(s): acetoin dehydrogenase complex;acetoin dehydrogenase enzyme system;AoDH ES. Systematic name: acetyl-CoA:acetoin O ... Accepted name: acetoin dehydrogenase. Reaction: acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+. ... Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. J. Bacteriol. 176 ( ... Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ...
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional. Pssm-ID: 184875 [Multi-domain] Cd ...
Putative acetoin dehydrogenase (TPP-dependent), E1 component beta. 0.256. 0.0015098. SMU.1744. Putative 3-oxoacyl-(acyl-carrier ... Putative dehydrogenase. 13.452. 0.000102. SMU.934. Putative amino acid ABC transporter, permease protein. 12.95. 0.0005141. 3.6 ... Putative pyruvate dehydrogenase E1 component beta subunit. 4.835. 0.0028314. SMU.179. Conserved hypothetical protein. 4.762. ... Sorbitol-6-phosphate 2-dehydrogenase. 4.196. 0.0010415. SMU.1187. Glucosamine-fructose-6-phosphate aminotransferase. 4.037. ...
Other name(s): acetoin dehydrogenase complex;acetoin dehydrogenase enzyme system;AoDH ES. Systematic name: acetyl-CoA:acetoin O ... Accepted name: acetoin dehydrogenase. Reaction: acetoin + CoA + NAD+ = acetaldehyde + acetyl-CoA + NADH + H+. ... EC 2.3.1.190 acetoin dehydrogenase. EC 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase EC 2.3.1.192 glycine ... Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the ...
EC 1.1.1.3 homoserine dehydrogenase. EC 1.1.1.4 (R,R)-butanediol dehydrogenase. EC 1.1.1.5 acetoin dehydrogenase. EC 1.1.1.5 ... lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD- ... Other name(s): malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent ... acetoin) reductase; D-aminopropanol dehydrogenase; 1-amino-2-propanol dehydrogenase; 2,3-butanediol dehydrogenase; D-1-amino-2- ...
TTHA0829 putative acetoin FT utilization protein, acetoin dehydrogenase; PFAM: CBS FT domain containing protein; SMART: CBS ...
acetoin/pyruvate dehydrogenase complex, E3 component, dihydrolipoamide dehydrogenase [KO:K00382] [EC:1.8.1.4] ... acetoin dehydrogenase complex, E1 component subunit alpha [KO:K00161] [EC:1.2.4.1] ... acetoin dehydrogenase complex, E1 component subunit beta [KO:K00162] [EC:1.2.4.1] ...
Overexpression of α-acetolactate decarboxylase and acetoin reductase/2,3-butanediol dehydrogenase in Arabidopsis thaliana ...
Transcription activator of acetoin dehydrogenase operon. 3. 30 (25). H69581. Bacillus subtilis. Transcription. ... Formate dehydrogenase homolog. 3. 40 (26). A27286. Bacillus subtilis. Formate dehydrogenase. Probable Ni/Fe hydrogenase small ... Formate dehydrogenase, nitrate inducible. 3. 29 (27). P24183. Escherichia coli. Formate dehydrogenase. ... Histidinol dehydrogenase. 4. 17 (16). Q9PM77. Campylobacter jejuni. Amino acid biosynthesis. Carbamate kinase-like protein. 4. ...
DEMPERS D. Overexpression of α-acetolactate decarboxylase and acetoin reductase/2,3-butanediol dehydrogenase in Arabidopsis ... The development of an in situ hybridisation technique to determine the gene expression patterns of UDP-glucose dehydrogenase, ... VAN DER MERWE J. Isolation and evaluation of the sugarcane UDP-glucose dehydrogenase gene and promoter. PhD, 2006. http:// ...
3-butanediol dehydrogenase to reduce acetoin formation by glycerol-overproducing, low-alcohol Saccharomyces cerevisiae. Appl. ... which encode for an alcohol dehydrogenase III and a glycerol-3-phosphate dehydrogenase, respectively (Young and Pilgrim, 1985; ... de Smidt, O., Du Preez, J. C., and Albertyn, J. (2008). The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive ... Alternatively, the overexpression of GPD1 complemented by the overexpression of BDH1 increases acetoin reduction to produce 2,3 ...
In some bacteria, acetoin can also be reduced to 2,3-butanediol by acetoin reductase/2,3-butanediol dehydrogenase. The Voges- ... The conversion of acetoin into acetyl-CoA is catalysed by the acetoin dehydrogenase complex, following a mechanism largely ... Acetoin is a chiral molecule. The form produced by bacteria is (R)-acetoin. Acetoin is a neutral, four-carbon molecule used as ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ...
3-butanediol dehydrogenase. In the next step, a multimeric acetoin dehydrogenase oxidizes and cleaves acetoin into acetyl-CoA ... The architecture of the acetoin dehydrogenase of A. woodii resembles bacterial pyruvate dehydrogenase or α-ketoglutarate ... dihydrolipoamide dehydrogenase, and dihydrolipoamide acetyltransferase of the Pelobacter carbinolicus acetoin dehydrogenase ... Purification and characterization of the E1 component of the Clostridium magnum acetoin dehydrogenase enzyme system. Antonie ...
3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral ... ACETOIN REDUCTASE A, B, C..., D, E, F, G, HA, B, C, D, E, F, G, H. 256 Klebsiella pneumoniae EC#: 1.1.1.304 IUBMB Gene Name(s): ... CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE. *DOI: 10.2210/pdb1geg/pdb ...
seb:STM474_2260 acetoin dehydrogenase 260 100 ( -) 29 0.329 73 -, 1 sed:SeD_A2517 oxidoreductase, short chain dehydrogenase 260 ... sphn:BV902_04220 succinate dehydrogenase flavoprotein s K00239 644 108 ( -) 30 0.307 114 -, 1 tbn:TBH_C0536 proton-dependent ... vbl:L21SP4_02010 Inositol 2-dehydrogenase 436 105 ( -) 30 0.322 90 -, 1 aaa:Acav_1599 Asp/Glu/hydantoin racemase 259 104 ( -) ... sht:KO02_02595 succinate dehydrogenase K00239 644 101 ( -) 29 0.307 114 -, 1 sth:STH1244 orotidine-5-phosphate decarboxylase ...
sil:SPO3790 acetoin dehydrogenase complex, E2 component K00627 366 116 ( -) 32 0.347 95 -, 1 cceu:CBR64_14525 Na+/H+ antiporter ... azc:AZC_1907 acetoin dehydrogenase complex E2 component K00627 371 100 ( -) 29 0.308 117 -, 1 bcew:DM40_1642 voltage gated ... chel:AL346_22565 acetoin dehydrogenase K00627 372 124 ( -) 34 0.365 96 -, 1 cet:B8281_16805 Na+/H+ antiporter NhaA 471 123 ... ara:Arad_3395 2-oxoisovalerate dehydrogenase beta subun K11381 1107 103 ( -) 29 0.314 121 -, 1 ato:CIW82_17465 acetoin ...
Other names in common use include L-butanediol dehydrogenase, L-BDH, and L(+)-2,3-butanediol dehydrogenase (L-acetoin forming ... In enzymology, a (S,S)-butanediol dehydrogenase (EC 1.1.1.76) is an enzyme that catalyzes the chemical reaction (S,S)-butane-2, ... Taylor MB; Juni E (1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenase". Biochim. Biophys. Acta. 39 (3): 448- ... whereas its 3 products are acetoin, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those ...
Nicholson WL: The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase. Appl Environ ... Glu dehydrogenase (gdh; [31, 32]), 3-hydroxybutyrate dehydrogenase (bdh[33, 34]), high affinity (HA) and low affinity (LA) ... Glutamine SynthetaseGlutamate DehydrogenaseAconitate HydrataseClass BacillusFutile Cycling. Background. The assimilation and re ... Other associations that were conserved included that with the gdh gene (encoding glutamate dehydrogenase) and the citBZ-icd ...
Diacetyl reductase ((S)-acetoin forming) (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)- ... "Sequence analysis of the gene for and characterization of D-acetoin forming meso-2,3-butanediol dehydrogenase of Klebsiella ... acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction (S)-acetoin + NAD+ ⇌ {\displaystyle \ ... Different from EC 1.1.1.303, diacetyl reductase ((R)-acetoin forming). Giovannini, P.P.; Medici, A.; Bergamini, C.M.; Rippa, M ...
Diacetyl reductase ((R)-acetoin forming) (EC 1.1.1.303, (R)-acetoin dehydrogenase) is an enzyme with systematic name (R)- ... acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction (R)-acetoin + NAD+ ⇌ {\displaystyle \ ... This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol ... This enzyme is different from EC 1.1.1.304, diacetyl reductase ((S)-acetoin forming). Heidlas, J.; Tressl, R. (1990). " ...
ova:OBV_21370 acetoin dehydrogenase E2 component K00627 446 100 ( -) 29 0.302 126 -, 1 pcon:B0A89_13190 flagellum-specific ATP ... prp:M062_03205 short-chain dehydrogenase K07124 266 108 ( -) 30 0.302 116 -, 1 pseh:XF36_09515 aldehyde dehydrogenase K13821 ... bhm:D558_3485 acyl-CoA dehydrogenase, N-terminal domain K00249 379 101 ( -) 29 0.302 126 -, 1 bho:D560_3516 acyl-CoA ... paeu:BN889_00745 putative short-chain dehydrogenase K07124 266 108 ( -) 30 0.302 116 -, 1 pag:PLES_06371 probable short-chain ...
Additionally, genes for acetoin dehydrogenase (ECAG_02019 to ECAG_02022), which converts acetoin to acetaldehyde and acetyl ... Probes targeting c-di-GMP signaling (see data set S3 in the supplemental material) and acetoin dehydrogenase genes (E. ... Transmembrane modulator-dependent bacterial tyrosine kinase activates UDP-glucose dehydrogenases. EMBO J. 22:4709-4718. ... encoding a previously characterized branched-chain α-keto acid dehydrogenase complex (53). The eutBC genes (EF1629 and EF1627, ...
... acetoin dehydrogenase enzyme system normally encoded by aco gene clusters found in all the other bacteria able to use acetoin ... Another recent study found that the organism Bacillus subtilis catabolized acetoin using the acu gene cluster enzymes that are ... Research in Pelobacter carbinolicus will help us to further understand the mechanisms of other types of acetoin system ... deduced showed very important similarities to the amino acid sequences of Pelobacter carbinolicus acetoin dehydrogenase enzyme ...
  • High fluorescence levels were obtained in a glycerol 3-phosphate dehydrogenase double deletion strain ( gpd1Δgpd2Δ ), which is deficient in the ability to regenerate NAD + via glycerol formation. (springeropen.com)
  • In S. cerevisiae , the cytosolic enzyme glycerol-3-phosphate dehydrogenase (GPD) 2 encoded by the GPD2 gene plays a central role in redox metabolism. (springeropen.com)
  • 1997 ]). A similar approach has been applied for S. cerevisiae where mannitol-1-phosphate 5-dehydrogenase (M1PDH) was introduced and the cytosolic free NADH/NAD + ratio was determined by the ratio between fructose-6-phosphate (F6P) and mannitol-1-phosphate (M1P) and the equilibrium constant for the reaction M1P + NAD ↔ F6P + NADH + H + (Canelas et al. (springeropen.com)
  • 5. Huang, M., Oppermann-Sanio, F.B. and Steinbuchel, A. Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway. (qmul.ac.uk)
  • The genome of the important industrial host Bacillus subtilis does not encode the glyoxylate shunt, which is necessary to utilize overflow metabolites, like acetate or acetoin, as carbon source. (biomedcentral.com)
  • In terms of Bacillus subtilis such conditions include aerobic growth with excess glucose or anaerobic nitrate respiration [ 2 , 3 ] and lead to the formation of acetate as well as acetoin and 2,3-butanediol. (biomedcentral.com)
  • The gene encoding a putative ( R , R )-butane-2,3-diol dehydrogenase ( bdhA ) from Bacillus clausii DSM 8716 T was isolated, sequenced and expressed in Escherichia coli . (megazyme.com)
  • In order to synthesize ( R )-3,5-BTPE efficiently, Lk CR was coexpressed with glucose dehydrogenase from Bacillus subtilis ( Bs GDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L ( R )-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). (biomedcentral.com)
  • This enzyme, which belongs to the family of 2-oxo acid dehydrogenase complexes, catalyses the oxidative-hydrolytic cleavage of acetoin to acetaldehyde and acetyl-CoA in many bacterial strains, both aerobic and anaerobic. (qmul.ac.uk)
  • This study confirmed that two (2R,3R)-2,3-butanediol dehydrogenases (BDHs) from industrial (denoted Y)/laboratory (denoted B) strains of S. cerevisiae , Bdh1p(Y)/Bdh1p(B) and Bdh2p(Y)/Bdh2p(B), were members of the PDH subfamily with an NAD(P)H binding domain and a catalytic zinc binding domain, and exhibited reductive activities towards lignocellulosic aldehyde inhibitors, such as acetaldehyde, glycolaldehyde, and furfural. (springer.com)
  • Lipoic acid serves as co-factor to the acetoin dehydrogenase complex catalyzing the conversion of acetoin (3-hydroxy-2-butanone) to acetaldehyde and acetyl coenzyme A, in some bacteria, allowing acetoin to be used as the sole carbon source. (wikipedia.org)
  • Xylitol and also glycerol by-product formation would be prevented if enzymatic activities for phosphoketolase, phosphate acetyl transferase and acetaldehyde dehydrogenase (acylating) were introduced in S. cerevisiae. (lu.se)
  • Addition of acetoin during cell proliferation under oxygen-limited conditions resulted in a more than 2-fold decrease in mean fluorescence intensity as compared to the control experiment. (springeropen.com)
  • Funciton: Acetoin dehydrogenase E1 component beta-subunit (EC 1.2.4. (lbl.gov)
  • Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of ( R , R )- and meso -butane-2,3-diol, while the enzyme reduced butane-2,3-dione ( V max 74 U/mg) solely to ( R , R )-butane-2,3-diol via ( R )-acetoin. (megazyme.com)
  • High purity recombinant Formate dehydrogenase ( Candida boidinii ) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. (megazyme.com)
  • In this study, CcpA mutants defective in transcriptional activation of the alsSD operon, which is involved in acetoin biosynthesis, were identified. (asm.org)
  • Exogenous application of racemic mixture of (RR) and (SS) isomers of 2,3-butanediol was found to trigger ISR and transgenic lines of B. subtilis that emitted reduced levels of 2,3-butanediol and acetoin conferred reduced Arabidopsis protection to pathogen infection compared with seedlings exposed to VOCs from wild-type bacterial lines. (plantphysiol.org)
  • The isolated enzyme catalyzed the ( R )-specific oxidation of ( R , R )- and meso -butane-2,3-diol to ( R )- and ( S )-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. (megazyme.com)
  • This is curious in view of the reported absolute stereospecificity of C. glutamicum BDH for (S)-acetoin (Takusagawa et al. (unl.pt)
  • We conclude that C. glutamicum BDH is not absolutely specific for (S)-acetoin, though this is the preferred substrate. (unl.pt)
  • Importantly, the low activity of BDH with (R)-acetoin was sufficient to support high yields of meso-2,3-BD in the engineered strain C. glutamicum ΔaceEΔpqoΔldhA(pEKEx2-als,aldB,butA Cg ). (unl.pt)
  • The enzymes that catalyze these conversions are glutamine synthetase, glutaminase, glutamate dehydrogenase and glutamine alpha-ketoglutarate aminotransferase. (biomedcentral.com)
  • The assimilation and re-distribution of nitrogen within a cell is essentially controlled within the central metabolic conversions between alpha-ketoglutarate, glutamate and glutamine (Figure 1 A). The enzymes that catalyze these conversions are glutamine synthetase (GS), glutaminase (G), glutamate dehydrogenase (GDH) and glutamine alpha-ketoglutarate aminotransferase (GOGAT). (biomedcentral.com)
  • In addition less-conserved associations were found with, for instance, glutamate dehydrogenase in Streptococcaceae, purine catabolism and the reduction of nitrite in Bacillaceae, and aspartate/asparagine deamination in Lactobacillaceae. (biomedcentral.com)
  • Kinetic parameters for (S)-acetoin, (R)-acetoin, meso-2,3-BD and (2S,3S)-BD were determined by spectrophotometric assays. (unl.pt)