An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD.
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
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.
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.
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.
Butanones, also known as methyl ethyl ketone or MEK, are organic compounds consisting of a four-carbon chain with a ketone functional group located at the second carbon atom, classified as dimethyl ketones, and commonly used in industrial and laboratory settings as solvents and chemical intermediates.
4-carbon straight chain aliphatic hydrocarbons substituted with two hydroxyl groups. The hydroxyl groups cannot be on the same carbon atom.
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.
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.

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)

Acetoin dehydrogenase is an enzyme complex that plays a role in the metabolism of certain organic compounds. It is responsible for catalyzing the oxidation of acetoin to diacetyl, which is then further oxidized to acetate. This enzyme complex is found in many different types of bacteria and is involved in their energy metabolism. Acetoin dehydrogenase is a multi-enzyme complex that consists of several different subunits, including an acetoin reductase, a diacetyl reductase, and a dihydrolipoyl dehydrogenase. These subunits work together to catalyze the oxidation of acetoin in a series of steps. The overall reaction is:

Acetoin + NAD+ -> Diacetyl + NADH + H+

Diacetyl + 2NADH + 2H+ -> 2Acetate + 2NAD+

The overall equation for the conversion of acetoin to acetate by acetoin dehydrogenase is:

Acetoin + NAD+ -> 2Acetate + NADH + H+

This reaction is important in the metabolism of certain types of bacteria, as it allows them to generate energy and reduce power for their growth and survival.

Acetoin is a chemical compound that is produced as a metabolic byproduct in certain types of bacteria, including some species of streptococcus and lactobacillus. It is a colorless liquid with a sweet, buttery odor and is used as a flavoring agent in the food industry. In addition to its use as a flavoring, acetoin has been studied for its potential antibacterial properties and its possible role in the development of biofilms. However, more research is needed to fully understand the potential uses and implications of this compound.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Dihydrolipoyllysine-residue acetyltransferase is a type of enzyme that plays a crucial role in the cellular process of energy production, specifically in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle). This enzyme is responsible for transferring an acetyl group from acetyl-CoA to a specific residue on another protein called dihydrolipoyl dehydrogenase.

The reaction catalyzed by this enzyme can be summarized as follows:
Acetyl-CoA + dihydrolipoyl dehydrogenase (E3-DHLA) -> CoA + acetylated-dihydrolipoyl dehydrogenase (E3-DHLAA)

The acetylation of the dihydrolipoyl dehydrogenase protein is a necessary step in the citric acid cycle, which helps generate energy in the form of ATP through a series of oxidation-reduction reactions. Defects or mutations in this enzyme can lead to various metabolic disorders and diseases.

Multienzyme complexes are specialized protein structures that consist of multiple enzymes closely associated or bound together, often with other cofactors and regulatory subunits. These complexes facilitate the sequential transfer of substrates along a series of enzymatic reactions, also known as a metabolic pathway. By keeping the enzymes in close proximity, multienzyme complexes enhance reaction efficiency, improve substrate specificity, and maintain proper stoichiometry between different enzymes involved in the pathway. Examples of multienzyme complexes include the pyruvate dehydrogenase complex, the citrate synthase complex, and the fatty acid synthetase complex.

Butanones are a group of chemical compounds that contain a ketone functional group and have the molecular formula C4H8O. They are also known as methyl ethyl ketones or MEKs. The simplest butanone is called methyl ethyl ketone (MEK) or 2-butanone, which has a chain of four carbon atoms with a ketone group in the second position. Other butanones include diethyl ketone (3-pentanone), which has a ketone group in the third position, and methyl isobutyl ketone (MIBK) or 4-methyl-2-pentanone, which has a branched chain with a ketone group in the second position.

Butanones are commonly used as solvents in various industrial applications, such as paint thinners, adhesives, and cleaning agents. They have a characteristic odor and can be harmful if ingested or inhaled in large quantities. Exposure to butanones can cause irritation of the eyes, skin, and respiratory tract, and prolonged exposure may lead to neurological symptoms such as dizziness, headache, and nausea.

Butylene glycols are a type of organic compounds that belong to the class of diols, which are chemical compounds containing two hydroxyl groups. Specifically, butylene glycols are composed of a four-carbon chain with two hydroxyl groups located on adjacent carbon atoms.

There are two isomeric forms of butylene glycol: 1,2-butanediol and 1,3-butanediol.

* 1,2-Butanediol (also known as 1,2-butylene glycol) has the hydroxyl groups on the first and second carbon atoms of the chain. It is a colorless, viscous liquid that is used as a solvent, humectant, and antifreeze in various industrial and cosmetic applications.
* 1,3-Butanediol (also known as 1,3-butylene glycol) has the hydroxyl groups on the first and third carbon atoms of the chain. It is also a colorless, viscous liquid that is used as a solvent, humectant, and antifreeze in various industrial and cosmetic applications.

Butylene glycols are generally considered to be safe for use in cosmetics and other consumer products, although they may cause skin irritation or allergic reactions in some individuals. They are also used as intermediates in the synthesis of other chemicals, such as polyesters and polyurethanes.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

... (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme ... Acetoin+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ... "Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system". Journal of ...
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 ... The form produced by bacteria is (R)-acetoin. Acetoin is a neutral, four-carbon molecule used as an external energy store by a ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin 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 (April 1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenases". Biochimica et Biophysica Acta ... 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). "Purification ...
... homoserine dehydrogenase EC 1.1.1.4: (R,R)-butanediol dehydrogenase EC 1.1.1.5: acetoin dehydrogenase. Now EC 1.1.1.303, ... acetoin forming] EC 1.1.1.304: diacetyl reductase [(S)-acetoin forming] EC 1.1.1.305: UDP-glucuronic acid dehydrogenase (UDP-4- ... acetoin forming] EC 1.1.1.6: glycerol dehydrogenase EC 1.1.1.7: propanediol-phosphate dehydrogenase EC 1.1.1.8: glycerol-3- ... 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- ...
... acetoin dehydrogenase EC 2.3.1.191: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase EC 2.3.1.192: glycine N- ... 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) kinase EC 2.7.1.116: Now EC 2.7.11.5, [isocitrate dehydrogenase ( ... 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. ...
... acetoin dehydrogenase MeSH D08.811.682.047.070 - alcohol dehydrogenase MeSH D08.811.682.047.150 - carbohydrate dehydrogenases ... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ... acyl-coa dehydrogenase MeSH D08.811.682.660.150.150 - acyl-coa dehydrogenase, long-chain MeSH D08.811.682.660.150.200 - acyl- ... glycine dehydrogenase MeSH D08.811.682.664.500.677 - l-amino acid oxidase MeSH D08.811.682.664.500.724 - leucine dehydrogenase ...
Taylor MB, Juni E (April 1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenases". Biochimica et Biophysica Acta ... 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 ...
Bertagnolli BL, Hager LP (January 1993). "Role of flavin in acetoin production by two bacterial pyruvate oxidases". Archives of ... Pyruvate dehydrogenase (quinone) (EC 1.2.5.1, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) ... dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate: ...
... 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 ... Lipoic acid is a cofactor for five enzymes or classes of enzymes: pyruvate dehydrogenase, a-ketoglutarate dehydrogenase, the ...
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 racemase EC 5.1.2.5: tartrate epimerase EC 5.1.2.6: isocitrate epimerase EC 5.1.2.7: tagaturonate epimerase * *No ... 11-cis-retinol dehydrogenase. EC 5.2.1.4: maleylpyruvate isomerase EC 5.2.1.5: linoleate isomerase EC 5.2.1.6: furylfuramide ... NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine-retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase ...
Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme ... Acetoin+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ... "Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase ... "Biochemical and molecular characterization of the Clostridium magnum acetoin dehydrogenase enzyme system". Journal of ...
1987) Isolated tumoral pyruvate dehydrogenase can synthesize acetoin which inhibits pyruvate oxidation as well as other ...
The activity of acetoin reduction was 7.7 times higher than that of (2R,3R)-2,3-butanediol oxidation when ReBDH was assayed at ... The enzyme was NAD(H)-specific and its optimal activity for acetoin reduction was observed at pH 6.5 and 55 °C. The optimal pH ... The enzyme displayed absolute stereospecificity in the reduction of diacetyl to (2R,3R)-2,3-butanediol via (R)-acetoin, ... belonging to the family of the zinc-containing alcohol dehydrogenases. ...
acetoin dehydrogenase e3 component-like protein 0.0032. 0.0218. 0.1101. Mycobacterium ulcerans. UDP-N-acetylglucosamine 1- ... DIHYDROLIPOAMIDE DEHYDROGENASE LPD (LIPOAMIDE REDUCTASE (NADH)) (LIPOYL DEHYDROGENASE) (DIHYDROLIPOYL DEHYDROGENASE) ( ... Dihydrolipoamide dehydrogenase LpdC (lipoamide reductase (NADH)) (lipoyl dehydrogenase) (dihydrolipoyl dehydrogenase) ( ... Probable dehydrogenase 0.021. 0.3163. 0.4283. Toxoplasma gondii. pyruvate dehydrogenase complex subunit PDH-E3II 0.0032. 0.0218 ...
Ortholog function: Acetoin dehydrogenase E1 component alpha-subunit (EC 1.2.4.-) Bacillus subtilis subsp. subtilis str. 168 ...
Dihydrolipoamide acetyltransferase component of acetoin dehydrogenase complex (NCBI ptt file). 355, 407. ...
acetoin dehydrogenase activity. GO:0030955. F. 63%. potassium ion binding. GO:0016616. F. 62%. oxidoreductase activity acting ... 3-methyl-2-oxobutanoate dehydrogenase 2-methylpropanoyl-transferring activity. GO:0004739. F. 89%. pyruvate dehydrogenase ... GOPET predicts for our Protein multiple exclusive categories of dehydrogenases so we would assume that the protein in fact has ... GOPET predicts for our Protein multiple exclusive categories of dehydrogenases so we would assume that the protein in fact has ...
For the first time, 2,3-butanediol production was achieved with promising titer, rate and yield and no acetoin formation from ... Optimizing oxygen supply and elimination of acetoin and by-product formation improved the 2,3-butanediol titer to 68 g& ... and acetoin reductase/butanediol dehydrogenase (budC). alsS indicates that acetolactate synthase of B. subtilis was combined ... Concentrations of 2,3-butanediol and acetoin obtained for the individual constructs are given as one bar (solid area = 2,3- ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
E7.945.750.40 Acetoin Dehydrogenase D8.811.682.47.50 D8.811.682.47.820.200 Acetyl-CoA Carboxylase D8.811.641.249 Acid-Base ... D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ...
... diolivorans strain overexpressing the endogenous alcohol dehydrogenase pduQ. The two-step cultivation process based on the ... 3-BTD catalysed by different acetoin reductases (or 2,3-BTD dehydrogenases). The ratio between the different isoforms for 2,3- ... In the next step, alpha-acetolactate decarboxylase decarboxylates alpha-acetolactate to acetoin. Acetoin is then used as a ... For S. cerevisiae, it has been already shown that the overexpression of a secondary alcohol dehydrogenase in combination with ...
It did not associate tightly with the E1 and E2 components of either acetoin dehydrogenase or 2-oxoglutarate dehydrogenase to ... The acoD gene, which encodes a dihydrolipoamide dehydrogenase component of the acetoin dehydrogenase enzyme system of ... acetoin dissimilation enzymes, pyruvate dehydrogenase complex, 2-oxoglutarate dehydrogenase complex, and branched-chain 2-oxo ... characterization of the acoD gene encoding a dihydrolipoamide dehydrogenase of the Klebsiella pneumoniae acetoin dehydrogenase ...
Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper). budC ... GRDH_DAUCA / Q5KTS5 Glucose and ribitol dehydrogenase; Carrot ABA-induced in somatic embryos 5 protein; EC 1.1.1.- from Daucus ... 3ay6B / P39485 Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose ... 5u2wA / B4E730 Crystal structure of a short chain dehydrogenase from burkho cenocepacia j2315 in complex with NADP. 52% ...
3-Hydroxyacyl CoA Dehydrogenases. *3-Isopropylmalate Dehydrogenase. *Acetoin Dehydrogenase. *Alcohol Dehydrogenase. * ...
... acetoin, meso-2,3-BD and (2S,3S)-BD were determined by spectrophotometric assays. V max values for (S)-acetoin and (R)-acetoin ... acetoin, meso-2,3-BD and (2S,3S)-BD were determined by spectrophotometric assays. V max values for (S)-acetoin and (R)-acetoin ... acetoin, meso-2,3-BD and (2S,3S)-BD were determined by spectrophotometric assays. V max values for (S)-acetoin and (R)-acetoin ... acetoin is a substrate for endogenous 2,3-butanediol dehydrogenase (BDH) activity. This is curious in view of the reported ...
Acetoin Dehydrogenase [D08.811.682.047.820.200] * Alcohol Dehydrogenase [D08.811.682.047.820.250] * Aldo-Keto Reductases [ ... beta-Isopropylmalate Dehydrogenase Term UI T106383. LexicalTag NON. ThesaurusID NLM (2006). beta-IPM Dehydrogenase Term UI ... 3-Hydroxyacyl CoA Dehydrogenases [D08.811.682.047.820.150] * 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) [D08.811.682.047 ... beta-IPM Dehydrogenase beta-Isopropylmalate Dehydrogenase Registry Number. EC 1.1.1.85. Related Numbers. 9030-97-1. Public MeSH ...
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They ... Acetoin Dehydrogenase. *acetol dehydrogenase. *acetylacetoin reductase. *Acinetobacter calcoaceticus QuiA protein. *acyclic ... A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They ...
Acetoin Dehydrogenase [D08.811.682.047.820.200] * Alcohol Dehydrogenase [D08.811.682.047.820.250] * Aldo-Keto Reductases [ ... Alcohol Dehydrogenase I Alcohol Dehydrogenase II Alcohol-NAD+ Oxidoreductase Yeast Alcohol Dehydrogenase Registry Number. EC ... Alcohol Dehydrogenase I Narrower Concept UI. M0000644. Registry Number. 0. Terms. Alcohol Dehydrogenase I Preferred Term Term ... Alcohol Dehydrogenase II Narrower Concept UI. M0000645. Registry Number. 0. Terms. Alcohol Dehydrogenase II Preferred Term Term ...
... acetoin from meso‐2,3‐butanediol using 2,3‐butanediol dehydrogenase and NADH oxidase. J. Chem. Technol. Biotechnol. 2019, 94, 8 ... Entner-Doudoroff pathway and pyruvate dehydrogenase complex to improve poly(3-hydroxybutyrate) production in Escherichia coli. ...
Catabolic glutamate dehydrogenases were discovered, implying that the tricarboxylic acid (TCA) cycle can function catabolically ... RESULTS: Pathways were predicted for catabolism of known substrates: 2,3-butanediol, acetoin, glycerol, 1,2-ethanediol, ... Multiple isozymes of 2,3-butanediol dehydrogenase, ATP synthase and [FeFe]-hydrogenase were differentiated and assigned roles ...
... acetoin dehydrogenase, thymine PPi ... 253 1e-65 gi,29840688,ref,NP_829794.1, 2-oxo acid dehydrogenase, E3 compon... 253 1e-65 ... acetoin dehydrogenase 228 3e-58 gi,13540930,ref,NP_110618.1, Dihydrolipoamide dehydrogenase [The... 228 3e-58 gi,46445785,ref, ... JC4793 dihydrolipoamide dehydrogenase (EC 1.8.1.... 248 2e-64 gi,15614388,ref,NP_242691.1, acetoin dehydrogenase E3 component ... dihydrolipoamide dehydrogenase [Bac... 234 3e-60 gi,16077876,ref,NP_388690.1, acetoin dehydrogenase E3 component ... 234 4e-60 ...
succinate dehydrogenase (ubiquinone) activity GO:0008177 * diacetyl reductase ((S)-acetoin forming) activity ...
5-exo-hydroxycamphor dehydrogenase activity 2-hydroxytetrahydrofuran dehydrogenase activity acetoin dehydrogenase activity ... isocitrate dehydrogenase activity mevaldate reductase activity gluconate dehydrogenase activity steroid dehydrogenase activity ... dihydrotestosterone 17-beta-dehydrogenase activity (R)-2-hydroxyisocaproate dehydrogenase activity L-arabinose 1-dehydrogenase ... steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor steroid dehydrogenase activity, ...
2-oxoglutarate dehydrogenase system, EC 1.2.1.104, pyruvate dehydrogenase system, and EC 2.3.1.190, acetoin dehydrogenase ... glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H- ... Other name(s): NAD(P)+-L-tryptophan dehydrogenase; L-tryptophan dehydrogenase; L-Trp-dehydrogenase; TDH. Systematic name: L- ... EC 1.4.1.3 glutamate dehydrogenase [NAD(P)+]. EC 1.4.1.4 glutamate dehydrogenase (NADP+). EC 1.4.1.5 L-amino-acid dehydrogenase ...
keywords = "2,3-butanediol, Acetolactate decarboxylase, Acetolactate synthase, Butantediol dehydrogenase, Metabolic flux ... and the budC gene enzyme catalyzed the reversible conversion of acetoin to 2,3-BDO and regulated the intracellular NAD+/NADH ... and butanediol dehydrogenase, which are encoded by the budA, budB, and budC genes, respectively. The mechanisms of the three ... and butanediol dehydrogenase, which are encoded by the budA, budB, and budC genes, respectively. The mechanisms of the three ...
  • Searching for up to 100 curated homologs for 201943 SO2813 oxidoreductase, short chain dehydrogenase/reductase family (NCBI ptt file) (254 a.a. (lbl.gov)
  • The gene encoding a (2 R ,3 R )-2,3-butanediol dehydrogenase from Rhodococcus erythropolis WZ010 (ReBDH) was over-expressed in Escherichia coli and the resulting recombinant ReBDH was successfully purified by Ni-affinity chromatography. (mdpi.com)
  • dissolvens DSM 16657) represent gene donors for acetolactate synthase ( budB ), acetolactate decarboxylase ( budA ) and acetoin reductase/butanediol dehydrogenase ( budC ). (biomedcentral.com)
  • In this work, we showed that Corynebacterium glutamicum endowed with the Lactococcus lactis genes encoding α-acetolactate synthase and decarboxylase activities produced meso-2,3-BD as the major end product, meaning that (R)-acetoin is a substrate for endogenous 2,3-butanediol dehydrogenase (BDH) activity. (uni-stuttgart.de)
  • Multiple isozymes of 2,3-butanediol dehydrogenase, ATP synthase and [FeFe]-hydrogenase were differentiated and assigned roles according to their structural properties and genomic contexts. (umass.edu)
  • In the central carbon metabolism of K. pneumoniae, the 2,3-BDO synthesis pathway is dominated by three essential enzymes, namely acetolactate decarboxylase, acetolactate synthase, and butanediol dehydrogenase, which are encoded by the budA, budB, and budC genes, respectively. (korea.ac.kr)
  • This enzyme catalyses the following chemical reaction acetoin + CoA + NAD+ ⇌ {\displaystyle \rightleftharpoons } acetaldehyde + acetyl-CoA + NADH + H+ This enzyme requires thiamine diphosphate. (wikipedia.org)
  • Activity assays monitored online by 1H-NMR using racemic acetoin and an excess of NADH showed an initial, fast production of (2S,3S)-2,3-BD, followed by a slow (∼20-fold lower apparent rate) formation of meso-2,3-BD. (uni-stuttgart.de)
  • While the enzyme encoded by the budA gene produced branched-chain amino acids which were favorable for cell growth, the budB gene enzyme rapidly enhanced the conversion of acetolactate to acetoin in an oxygen-dependent manner, and the budC gene enzyme catalyzed the reversible conversion of acetoin to 2,3-BDO and regulated the intracellular NAD + /NADH balance. (korea.ac.kr)
  • Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. (wikipedia.org)
  • The enzyme was NAD(H)-specific and its optimal activity for acetoin reduction was observed at pH 6.5 and 55 °C. The optimal pH and temperature for 2,3-butanediol oxidation were pH 10 and 45 °C, respectively. (mdpi.com)
  • 3. Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. (qmul.ac.uk)
  • For example, the limiting step and the control point for alginate biosynthesis is the activity of the GDP-mannose dehydrogenase enzyme, which is involved in the irreversible oxidation of GDP-mannose to GDP-mannuronic acid [ 24 ], and is NAD + -dependent [ 25 ]. (biomedcentral.com)
  • 1987 ) Isolated tumoral pyruvate dehydrogenase can synthesize acetoin which inhibits pyruvate oxidation as well as other aldehydes. (academictree.org)
  • This gene encodes a protein which contains 2 WW domains and a short-chain dehydrogenase/reductase domain (SRD). (thermofisher.com)
  • T23632 dihydrolipoamide dehydrogenase (EC 1.8.1. (nig.ac.jp)
  • dihydrolipoamide dehydrogenase (52. (nig.ac.jp)
  • dihydrolipoamide dehydrogenase precur. (nig.ac.jp)
  • dihydrolipoamide dehydrogenase [Danio. (nig.ac.jp)
  • A Chain A, Dihydrolipoamide Dehydrogenase Of. (nig.ac.jp)
  • S22384 dihydrolipoamide dehydrogenase (EC 1.8.1.4. (nig.ac.jp)
  • Kinetic parameters for (S)-acetoin, (R)-acetoin, meso-2,3-BD and (2S,3S)-BD were determined by spectrophotometric assays. (uni-stuttgart.de)
  • Catabolic glutamate dehydrogenases were discovered, implying that the tricarboxylic acid (TCA) cycle can function catabolically. (umass.edu)
  • 1. Frieden, C. L -Glutamate dehydrogenase. (qmul.ac.uk)
  • A further improvement of the maximum butanol titer was achieved using an engineered L. diolivorans strain overexpressing the endogenous alcohol dehydrogenase pduQ. (biomedcentral.com)
  • 1. Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L -glutamic acid dehydrogenase. (qmul.ac.uk)
  • BFV are a complex mixture of volatile agents containing of diacetyl and butyric acid, two components of BFV, and to develop a hybrid computational fluid dynamic-physiologically diacetyl (2,3-butanedione), acetoin, 2-nonanone, acetic acid, based pharmacokinetic model (CFD-PBPK) to describe these and butyric acid, among other vapors (Boylstein et al. (cdc.gov)
  • We conclude that C. glutamicum BDH is not absolutely specific for (S)-acetoin, though this is the preferred substrate. (uni-stuttgart.de)
  • 1. O'Connor, R.J. and Halvorson, H. The substrate specificity of L -alanine dehydrogenase. (qmul.ac.uk)
  • A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. (curehunter.com)
  • The purified ReBDH in the native form was found to exist as a monomer with a calculated subunit size of 37180, belonging to the family of the zinc-containing alcohol dehydrogenases. (mdpi.com)
  • Acetoin dehydrogenase E1 component alpha-subunit (EC 1.2.4. (lbl.gov)
  • 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. (nih.gov)
  • An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD . (nih.gov)
  • Here the authors demonstrate that a model of pyruvate distribution in Lactococcus lactis based on enzyme kinetics in combination with metabolic control analysis clearly indicates the key control points in the flux to acetoin and diacetyl, important flavour compounds. (nih.gov)
  • BFV are a complex mixture of volatile agents containing of diacetyl and butyric acid, two components of BFV, and to develop a hybrid computational fluid dynamic-physiologically diacetyl (2,3-butanedione), acetoin, 2-nonanone, acetic acid, based pharmacokinetic model (CFD-PBPK) to describe these and butyric acid, among other vapors (Boylstein et al. (cdc.gov)
  • The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. (nih.gov)
  • In its diphosphate form (also known as TDP, thiamine pyrophosphate, TPP, or cocarboxylase), it serves as a cofactor for enzymes involved in carbohydrate metabolism, including transketolase, α-ketoglutarate dehydrogenase, pyruvate dehydrogenase, and branched chain α-keto acid dehydrogenase. (ferienwohnung-gluecksburg.net)
  • Acetoin dehydrogenase (EC 2.3.1.190, acetoin dehydrogenase complex, acetoin dehydrogenase enzyme system, AoDH ES) is an enzyme with systematic name acetyl-CoA:acetoin O-acetyltransferase. (wikipedia.org)
  • This gene encodes a member of the alcohol dehydrogenase family. (thermofisher.com)
  • Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. (embl.de)
  • The structure of inosine-5'-monophosphate dehydrogenase (IMPDH) in complex with IMP and mycophenolic acid (MPA) has been determined by X-ray diffraction. (embl.de)
  • The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. (nih.gov)
  • Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure [3]. (embl.de)