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.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.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.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.Bacteriophage PRD1: Bacteriophage and type species in the genus Tectivirus, family TECTIVIRIDAE. They are specific for Gram-negative bacteria.Bridged Compounds: Cyclic hydrocarbons that contain multiple rings and share one or more atoms.Nitrogen Oxides: Inorganic oxides that contain nitrogen.Benzoic Acid: A fungistatic compound that is widely used as a food preservative. It is conjugated to GLYCINE in the liver and excreted as hippuric acid.Transition Temperature: The temperature at which a substance changes from one state or conformation of matter to another.Benzoates: Derivatives of BENZOIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxybenzene structure.Nitrobenzoates: Benzoic acid or benzoic acid esters substituted with one or more nitro groups.Hippurates: Salts and esters of hippuric acid.Fermentation: Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.Molecular Weight: The sum of the weight of all the atoms in a molecule.Physicochemical Phenomena: The physical phenomena describing the structure and properties of atoms and molecules, and their reaction and interaction processes.Metalloporphyrins: Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Nicotinamide N-Methyltransferase: An enzyme found primarily in the LIVER that catalyzes the N-methylation of NICOTINAMIDE and other structurally related compounds.Guanidinoacetate N-Methyltransferase: This enzyme catalyzes the last step of CREATINE biosynthesis by catalyzing the METHYLATION of guanidinoacetate to CREATINE.Histamine N-Methyltransferase: An enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to histamine, forming N-methylhistamine, the major metabolite of histamine in man. EC 2.1.1.8.Glycine N-Methyltransferase: An enzyme that catalyzes the METHYLATION of GLYCINE using S-ADENOSYLMETHIONINE to form SARCOSINE with the concomitant production of S-ADENOSYLHOMOCYSTEINE.Phosphatidylethanolamine N-Methyltransferase: An enzyme that catalyses three sequential METHYLATION reactions for conversion of phosphatidylethanolamine to PHOSPHATIDYLCHOLINE.Betaine-Homocysteine S-Methyltransferase: A ZINC metalloenzyme that catalyzes the transfer of a methyl group from BETAINE to HOMOCYSTEINE to produce dimethylglycine and METHIONINE, respectively. This enzyme is a member of a family of ZINC-dependent METHYLTRANSFERASES that use THIOLS or selenols as methyl acceptors.Methyltransferases: A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.Catechol O-Methyltransferase: Enzyme that catalyzes the movement of a methyl group from S-adenosylmethionone to a catechol or a catecholamine.Acetylserotonin O-Methyltransferase: An enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to N-acetylserotonin to form N-acetyl-5-methoxytryptamine (MELATONIN).Phenylethanolamine N-Methyltransferase: A methyltransferase that catalyzes the reaction of S-adenosyl-L-methionine and phenylethanolamine to yield S-adenosyl-L-homocysteine and N-methylphenylethanolamine. It can act on various phenylethanolamines and converts norepinephrine into epinephrine. (From Enzyme Nomenclature, 1992) EC 2.1.1.28.
(1/20) Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway.

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

*  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 ...
*  Acetoin
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 ...
*  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). " ...
*  Lipoic acid
... 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 ...
*  List of EC numbers (EC 2)
... 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: ( ...
*  List of MeSH codes (D08)
... 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 ...
*  S,S)-butanediol dehydrogenase
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 ...
*  Acetoin racemase
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 ...
*  Pyruvate dehydrogenase (quinone)
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: ...
*  List of EC numbers (EC 1)
... 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 ...
*  R,R)-butanediol dehydrogenase
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 - Wikipedia  Acetoin dehydrogenase - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Acetoin_dehydrogenase
EC 2.3.1.190  EC 2.3.1.190
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 ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/3/1/190.html
KEGG BRITE: Enzymes - Mycobacterium tuberculosis H37Rv  KEGG BRITE: Enzymes - Mycobacterium tuberculosis H37Rv
2.3.1.190 acetoin dehydrogenase 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase ...
more infohttp://www.genome.jp/kegg-bin/get_htext?mtu01000+Rv2243
NCBI Conserved Domain Search  NCBI Conserved Domain Search
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional. Pssm-ID: 184875 [Multi-domain] Cd ...
more infohttps://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi?SEQUENCE=AAO24581
EC 2.3.1.151-2.3.1.200  EC 2.3.1.151-2.3.1.200
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 ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/0301d.html
KEGG PATHWAY: lca00020  KEGG PATHWAY: lca00020
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] ...
more infohttp://www.genome.jp/dbget-bin/www_bget?pathway+lca00020
Diverse protein regulations on PHA formation in Ralstonia eutropha on short chain organic acids  Diverse protein regulations on PHA formation in Ralstonia eutropha on short chain organic acids
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. ...
more infohttp://www.ijbs.com/v05p0215.htm
KEGG SSDB Best Search Result: ure:UREG 00168  KEGG SSDB Best Search Result: ure:UREG 00168
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 ...
more infohttp://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=ure:UREG_00168
KEGG SSDB Best Search Result: bna:111207313  KEGG SSDB Best Search Result: bna:111207313
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 ...
more infohttps://www.kegg.jp/ssdb-bin/ssdb_best?org_gene=bna:111207313
Energetics and Application of Heterotrophy in Acetogenic Bacteria | Applied and Environmental Microbiology  Energetics and Application of Heterotrophy in Acetogenic Bacteria | Applied and Environmental Microbiology
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 ...
more infohttps://aem.asm.org/content/82/14/4056.full
Acetoin - Wikipedia  Acetoin - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Acetoin
Comparative Genomics of Enterococci: Variation in Enterococcus faecalis, Clade Structure in E. faecium, and Defining...  Comparative Genomics of Enterococci: Variation in Enterococcus faecalis, Clade Structure in E. faecium, and Defining...
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, ...
more infohttps://mbio.asm.org/content/3/1/e00318-11?ijkey=8ae947f20790543ea8798a37cc48f29699872300&keytype2=tf_ipsecsha
拳皇命运官方论坛:
	Benzoic acid | 65-85 - 拳皇命运图片  拳皇命运官方论坛: Benzoic acid | 65-85 - 拳皇命运图片
... acetoin dehydrogenase; mandelonitrile lyase; carbonyl reductase; esterase; peroxidase; pyrophosphatase.or inorganic ... lactate dehydrogenase, weakly inhibited; glucose dehydrogenase, weakly inhibited; γ-butyrobetaine dioxygenase, gbutyrobetaine ...
more infohttp://www.ljntc.icu/ChemicalProductProperty_EN_CB8698780.htm
Analysis of growth-phase regulated genes in Streptococcus agalactiaeby global transcript profiling | BMC Microbiology | Full...  Analysis of growth-phase regulated genes in Streptococcus agalactiaeby global transcript profiling | BMC Microbiology | Full...
... pyruvate dehydrogenase (acoAB), and L-lactate dehydrogenase (gbs0947) (Table 1). This finding is similar to the results ... glyceraldehyde 3P-dehydrogenase (gbs1811), phosphoglycerate kinase (gbs1809), enolase (gbs0608), ...
more infohttps://bmcmicrobiol.biomedcentral.com/articles/10.1186/1471-2180-9-32
Regulon of CcpA in Streptococcus mutans UA159  Regulon of CcpA in Streptococcus mutans UA159
Funciton: Dihydrolipoamide acetyltransferase component (E2) of acetoin dehydrogenase complex (EC 2.3.1.-) ... Funciton: Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NADP+] (EC 1.2.1.16) ... Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NADP+] (EC 1.2.1.16) ...
more infohttp://regprecise.lbl.gov/RegPrecise/regulon.jsp?regulon_id=35145
Network Portal - Gene BSU27980  Network Portal - Gene BSU27980
acetoin dehydrogenase E1 component (TPP-dependent beta subunit) (RefSeq). 17, 277. BSU08080. acoC. branched-chain alpha-keto ...
more infohttp://networks.systemsbiology.net/bsu/gene/BSU27980
Network Portal - Gene BSU18600  Network Portal - Gene BSU18600
acetoin dehydrogenase E1 component (TPP-dependent alpha subunit) (RefSeq). 17, 55. BSU08120. yfjF. hypothetical protein (RefSeq ...
more infohttp://networks.systemsbiology.net/bsu/gene/BSU18600
Regulon of CcpA in Streptococcus gallolyticus UCN34  Regulon of CcpA in Streptococcus gallolyticus UCN34
2,3-butanediol dehydrogenase, S-alcohol forming, (R)-acetoin-specific (EC 1.1.1.4) / Acetoin (diacetyl) reductase (EC 1.1.1.5) ... Funciton: 2,3-butanediol dehydrogenase, S-alcohol forming, (R)-acetoin-specific (EC 1.1.1.4) / Acetoin (diacetyl) reductase (EC ... Funciton: Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NADP+] (EC 1.2.1.16) ... Succinate-semialdehyde dehydrogenase [NAD] (EC 1.2.1.24); Succinate-semialdehyde dehydrogenase [NADP+] (EC 1.2.1.16) ...
more infohttp://regprecise.lbl.gov/RegPrecise/regulon.jsp?regulon_id=35142
Evolution from a respiratory ancestor to fill syntrophic and fermentative niches: comparative genomics of six Geobacteraceae...  Evolution from a respiratory ancestor to fill syntrophic and fermentative niches: comparative genomics of six Geobacteraceae...
Enzymes acquired by lateral gene transfer are shown in red: 1) butanediol dehydrogenase, 2) acetoin dehydrogenase, 3) pyruvate: ... Enzymes acquired by lateral gene transfer are shown in red: 1) butanediol dehydrogenase, 2) acetoin dehydrogenase, 3) ... the butanediol dehydrogenase and acetoin dehydrogenase appear to have been acquired by lateral gene transfer. NAD+ is ... The butanediol dehydrogenase (Bdh, Pcar_0330) and acetoin dehydrogenase (AcoABCL, Pcar_0343-Pcar0346), which catalyze the ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-10-103
EzCatDB


M00188  EzCatDB M00188
Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system. ... E2 component of pyruvate dehydrogenase complex.. The pyruvate dehydrogenase complex is composed of pyruvate dehydrogenaes (E1 ... and lipoamide dehydrogenase (E3 component; E.C. 1.8.1.4). (The E3 component corresponds to the entry T00017 in EzCatDB.). This ... Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex. Pfam. PF00198 (2-oxoacid_dh). PF00364 (Biotin_ ...
more infohttp://ezcatdb.cbrc.jp/EzCatDB/search/get.do?dbcode=M00188
Lipoic acid  Lipoic acid
the acetoin dehydrogenase complex.. The most-studied of these is the pyruvate dehydrogenase complex. These complexes have three ... Lipoic acid serves as co-factor to the acetoin dehydrogenase complex catalyzing the conversion of acetoin (3-hydroxy-2-butanone ... the α-ketoglutarate dehydrogenase or 2-oxoglutarate dehydrogenase complex. * the branched-chain oxoacid dehydrogenase (BCDH) ... One of the most studied roles of RLA is as a cofactor of the pyruvate dehydrogenase complex (PDC or PDHC), though it is a ...
more infohttps://ipfs.io/ipfs/QmXoypizjW3WknFiJnKLwHCnL72vedxjQkDDP1mXWo6uco/wiki/Alpha-Lipoic_acid.html
ENZYME: 2.3.1.  ENZYME: 2.3.1.
Acetoin dehydrogenase 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase 2.3.1.192 Glycine N- ...
more infohttps://enzyme.expasy.org/EC/2.3.1.-
ENZYME: 2.-.-.  ENZYME: 2.-.-.
Acetoin dehydrogenase 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase 2.3.1.192 Glycine N- ... 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase 2.7.11.5 [Isocitrate dehydrogenase (NADP(+))] kinase 2.7. ... Acetoin--ribose-5-phosphate transaldolase 2.2.1.5 2-hydroxy-3-oxoadipate synthase 2.2.1.6 Acetolactate synthase 2.2.1.7 1-deoxy ... Pyruvate dehydrogenase (acetyl-transferring)] kinase 2.7.11.3 Dephospho-[reductase kinase] kinase 2.7.11.4 [ ...
more infohttps://enzyme.expasy.org/EC/2.-.-.-
Frontiers | GPD1 and ADH3 Natural Variants Underlie Glycerol Yield Differences in Wine Fermentation | Microbiology  Frontiers | GPD1 and ADH3 Natural Variants Underlie Glycerol Yield Differences in Wine Fermentation | Microbiology
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 ...
more infohttps://www.frontiersin.org/articles/10.3389/fmicb.2018.01460/full
  • Because of this, manufacturers of partially hydrogenated oils typically add artificial butter flavor - acetoin and diacetyl - (along with beta carotene for the yellow color) to the final product, which would otherwise be tasteless. (wikipedia.org)