'Ketosis' is a metabolic state characterized by an elevated concentration of ketone bodies in the blood, typically occurring during fasting, carbohydrate restriction, or in uncontrolled diabetes, and can lead to a shift in the body's primary energy source from glucose to fatty acids and ketones.
Polyhydric alcohols having no more than one hydroxy group attached to each carbon atom. They are formed by the reduction of the carbonyl group of a sugar to a hydroxyl group.(From Dorland, 28th ed)
An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.
Enzymes that catalyze the interconversion of aldose and ketose compounds.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
Compounds based on reduced IMIDAZOLINES which contain no double bonds in the ring.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
A polyhydric alcohol with about half the sweetness of sucrose. Sorbitol occurs naturally and is also produced synthetically from glucose. It was formerly used as a diuretic and may still be used as a laxative and in irrigating solutions for some surgical procedures. It is also used in many manufacturing processes, as a pharmaceutical aid, and in several research applications.

Cobalt proteins. (1/391)

In the form of vitamin B12, cobalt plays a number of crucial roles in many biological functions. However, recent studies have provided information on the biochemistry and bioinorganic chemistry of several proteins containing cobalt in a form other than that in the corrin ring of vitamin B12. To date, eight noncorrin-cobalt-containing enzymes (methionine aminopeptidase, prolidase, nitrile hydratase, glucose isomerase, methylmalonyl-CoA carboxytransferase, aldehyde decarbonylase, lysine-2,3-aminomutase, and bromoperoxidase) have been isolated and characterized. A cobalt transporter is involved in the metallocenter biosynthesis of the host cobalt-containing enzyme, nitrile hydratase. Understanding the differences between cobalt and nickel transporters might lead to drug development for gastritis and peptic ulceration.  (+info)

Construction and characterization of Escherichia coli disruptants defective in the yaeM gene. (2/391)

Escherichia coli disruptants defective in the yaeM gene, which is located at 4.2 min on the chromosome map, were constructed and characterized. The disruptants showed auxotrophy for 2-C-methylerythritol, a free alcohol of 2-C-methyl-D-erythritol 4-phosphate that is a biosynthetic precursor in the nonmevalonate pathway. This result clearly shows that the yaeM gene is indeed involved in this pathway in E. coli.  (+info)

Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. (3/391)

Enzymes from hyperthermophiles can be efficiently purified after expression in mesophilic hosts and are well-suited for crystallisation attempts. Two enzymes of histidine biosynthesis from Thermotoga maritima, N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase and the cyclase moiety of imidazoleglycerol phosphate synthase, were overexpressed in Escherichia coli, both in their native and seleno-methionine-labelled forms, purified by heat precipitation of host proteins and crystallised. N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase crystallised in four different forms, all suitable for X-ray structure solution, and the cyclase moiety of imidazoleglycerol phosphate synthase yielded one crystal form that diffracted to atomic resolution. The obtained crystals will enable the determination of the first three-dimensional structures of enzymes from the histidine biosynthetic pathway.  (+info)

Cloning and heterologous expression of a cDNA encoding 1-deoxy-D-xylulose-5-phosphate reductoisomerase of Arabidopsis thaliana. (4/391)

Various plant isoprenoids are synthesized via the non-mevalonate pathway of isopentenyl diphosphate formation. In this pathway, 1-deoxy-D-xylulose 5-phosphate (DOXP), the first intermediate, is transformed to 2-C-methyl-D-erythritol 4-phosphate (MEP) by an enzyme which was recently cloned from Escherichia coli. In order to find a plant homologue of this 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) we cloned a cDNA fragment from Arabidopsis thaliana which has high homology to the E. coli DXR. By expression of this fragment in E. coli we could demonstrate that it encodes a protein which transforms DOXP to MEP. The antibiotic fosmidomycin specifically inhibits this DXR enzyme activity.  (+info)

A molecular sensor that allows a gut commensal to control its nutrient foundation in a competitive ecosystem. (5/391)

Little is known about how members of the indigenous microflora interact with their mammalian hosts to establish mutually beneficial relationships. We have used a gnotobiotic mouse model to show that Bacteroides thetaiotaomicron, a component of the intestinal microflora of mice and humans, uses a repressor, FucR, as a molecular sensor of L-fucose availability. FucR coordinates expression of an operon encoding enzymes in the L-fucose metabolic pathway with expression of another locus that regulates production of fucosylated glycans in intestinal enterocytes. Genetic and biochemical studies indicate that FucR does this by using fucose as an inducer at one locus and as a corepressor at the other locus. Coordinating this commensal's immediate nutritional requirements with production of a host-derived energy source is consistent with its need to enter and persist within a competitive ecosystem.  (+info)

Gene silencing: Maintaining methylation patterns. (6/391)

Recent studies of an Arabidopsis gene family have shown that inverted repeats can be potent silencers of other identical sequences in the genome, causing them to become stably methylated at cytosine residues. From mutations affecting this process we are beginning to understand how methylation patterns are maintained.  (+info)

Increasing the thermostability of D-xylose isomerase by introduction of a proline into the turn of a random coil. (7/391)

Thermostability can be increased by introducing prolines at suitable sites in target proteins. Two single (G138P, G247D) mutants and one double (G138P/G247D) mutant of xylose isomerase from Streptomyces diastaticus No.7, strain M1033 have been constructed by site-directed mutagenesis. With respect to the wild-type enzyme, G138P showed about a 100% increase in thermostability, and G247D showed an increased catalytic activity. Significantly, the double mutant, G138P/G247D displayed even higher activity than G247D and better heat stability than G138P. Its half life was about 2.5-fold greater than the wild-type enzyme, using xylose as a substrate. Molecular modelling suggested that the introduction of a proline residue in the turn of a random coil may cause the surrounding conformation to be tightened by reducing the backbone flexibility. The change in thermostability can, therefore, be explained based on changes in the molecular rigidity. Furthermore, the improvements in the properties of the double mutant indicated that the advantages of two single mutants can be combined effectively.  (+info)

Arabidopsis PAI gene arrangements, cytosine methylation and expression. (8/391)

Previous analysis of the PAI tryptophan biosynthetic gene family in Arabidopsis thaliana revealed that the Wassilewskija (WS) ecotype has four PAI genes at three unlinked sites: a tail-to-tail inverted repeat at one locus (PAI1-PAI4) plus singlet genes at two other loci (PAI2 and PAI3). The four WS PAI genes are densely cytosine methylated over their regions of DNA identity. In contrast, the Columbia (Col) ecotype has three singlet PAI genes at the analogous loci (PAI1, PAI2, and PAI3) and no cytosine methylation. To understand the mechanism of PAI gene duplication at the polymorphic PAI1 locus, and to investigate the relationship between PAI gene arrangement and PAI gene methylation, we analyzed 39 additional ecotypes of Arabidopsis. Six ecotypes had PAI arrangements similar to WS, with an inverted repeat and dense PAI methylation. All other ecotypes had PAI arrangements similar to Col, with no PAI methylation. The novel PAI-methylated ecotypes provide insights into the mechanisms underlying PAI gene duplication and methylation, as well as the relationship between methylation and gene expression.  (+info)

Ketosis is a metabolic state characterized by elevated levels of ketone bodies in the blood or urine. Ketone bodies are molecules produced from fatty acids during the breakdown of fats for energy, particularly when carbohydrate intake is low. This process occurs naturally in our body, and it's a part of normal metabolism. However, ketosis becomes significant under certain conditions such as:

1. Diabetic ketoacidosis (DKA): A serious complication in people with diabetes, typically type 1 diabetes, which happens when there are extremely high levels of ketones and blood sugar due to insulin deficiency or a severe infection. DKA is a medical emergency that requires immediate treatment.
2. Starvation or fasting: When the body doesn't receive enough carbohydrates from food, it starts breaking down fats for energy, leading to ketosis. This can occur during prolonged fasting or starvation.
3. Low-carbohydrate diets (LCDs) or ketogenic diets: Diets that restrict carbohydrate intake and emphasize high fat and protein consumption can induce a state of nutritional ketosis, where ketone bodies are used as the primary energy source. This type of ketosis is not harmful and can be beneficial for weight loss and managing certain medical conditions like epilepsy.

It's important to note that there is a difference between diabetic ketoacidosis (DKA), which is a dangerous condition, and nutritional ketosis, which is a normal metabolic process and can be achieved through dietary means without negative health consequences for most individuals.

Sugar alcohols, also known as polyols, are carbohydrates that are chemically similar to sugar but have a different molecular structure. They occur naturally in some fruits and vegetables, but most sugar alcohols used in food products are manufactured.

The chemical structure of sugar alcohols contains a hydroxyl group (-OH) instead of a hydrogen and a ketone or aldehyde group, which makes them less sweet than sugar and have fewer calories. They are not completely absorbed by the body, so they do not cause a rapid increase in blood glucose levels, making them a popular sweetener for people with diabetes.

Common sugar alcohols used in food products include xylitol, sorbitol, mannitol, erythritol, and maltitol. They are often used as sweeteners in sugar-free and low-sugar foods such as candy, chewing gum, baked goods, and beverages.

However, consuming large amounts of sugar alcohols can cause digestive symptoms such as bloating, gas, and diarrhea, due to their partial absorption in the gut. Therefore, it is recommended to consume them in moderation.

Aldehyde reductase is an enzyme that belongs to the family of alcohol dehydrogenases. Its primary function is to catalyze the reduction of a wide variety of aldehydes into their corresponding alcohols, using NADPH as a cofactor. This enzyme plays a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. It is widely distributed in different tissues, including the liver, kidney, and brain. In addition to its detoxifying function, aldehyde reductase has been implicated in several physiological and pathophysiological processes, such as neuroprotection, cancer, and diabetes.

Aldose-ketose isomerases are a group of enzymes that catalyze the interconversion between aldoses and ketoses, which are different forms of sugars. These enzymes play an essential role in carbohydrate metabolism by facilitating the reversible conversion of aldoses to ketoses and vice versa.

Aldoses are sugars that contain a carbonyl group (a functional group consisting of a carbon atom double-bonded to an oxygen atom) at the end of the carbon chain, while ketoses have their carbonyl group located in the middle of the chain. The isomerization process catalyzed by aldose-ketose isomerases helps maintain the balance between these two forms of sugars and enables cells to utilize them more efficiently for energy production and other metabolic processes.

There are several types of aldose-ketose isomerases, including:

1. Triose phosphate isomerase (TPI): This enzyme catalyzes the interconversion between dihydroxyacetone phosphate (a ketose) and D-glyceraldehyde 3-phosphate (an aldose), which are both trioses (three-carbon sugars). TPI plays a crucial role in glycolysis, the metabolic pathway that breaks down glucose to produce energy.
2. Xylulose kinase: This enzyme is involved in the pentose phosphate pathway, which is a metabolic route that generates reducing equivalents (NADPH) and pentoses for nucleic acid synthesis. Xylulose kinase catalyzes the conversion of D-xylulose (a ketose) to D-xylulose 5-phosphate, an important intermediate in the pentose phosphate pathway.
3. Ribulose-5-phosphate 3-epimerase: This enzyme is also part of the pentose phosphate pathway and catalyzes the interconversion between D-ribulose 5-phosphate (an aldose) and D-xylulose 5-phosphate (a ketose).
4. Phosphoglucomutase: This enzyme catalyzes the reversible conversion of glucose 1-phosphate (an aldose) to glucose 6-phosphate (an aldose), which is an important intermediate in both glycolysis and gluconeogenesis.
5. Phosphomannomutase: This enzyme catalyzes the reversible conversion of mannose 1-phosphate (a ketose) to mannose 6-phosphate (an aldose), which is involved in the biosynthesis of complex carbohydrates.

These are just a few examples of enzymes that catalyze the interconversion between aldoses and ketoses, highlighting their importance in various metabolic pathways.

Isomerases are a class of enzymes that catalyze the interconversion of isomers of a single molecule. They do this by rearranging atoms within a molecule to form a new structural arrangement or isomer. Isomerases can act on various types of chemical bonds, including carbon-carbon and carbon-oxygen bonds.

There are several subclasses of isomerases, including:

1. Racemases and epimerases: These enzymes interconvert stereoisomers, which are molecules that have the same molecular formula but different spatial arrangements of their atoms in three-dimensional space.
2. Cis-trans isomerases: These enzymes interconvert cis and trans isomers, which differ in the arrangement of groups on opposite sides of a double bond.
3. Intramolecular oxidoreductases: These enzymes catalyze the transfer of electrons within a single molecule, resulting in the formation of different isomers.
4. Mutases: These enzymes catalyze the transfer of functional groups within a molecule, resulting in the formation of different isomers.
5. Tautomeres: These enzymes catalyze the interconversion of tautomers, which are isomeric forms of a molecule that differ in the location of a movable hydrogen atom and a double bond.

Isomerases play important roles in various biological processes, including metabolism, signaling, and regulation.

Carbon-carbon double bond isomerases are a class of enzymes that catalyze the conversion of one geometric or positional isomer of a molecule containing a carbon-carbon double bond into another. These enzymes play an important role in the metabolism and biosynthesis of various biological compounds, including fatty acids, steroids, and carotenoids.

There are several types of carbon-carbon double bond isomerases, each with their own specific mechanisms and substrate preferences. Some examples include:

1. Ene/Yne Isomerases: These enzymes catalyze the conversion of a carbon-carbon double bond that is conjugated to an alkene or alkyne group into a new double bond location through a series of [1,5]-sigmatropic shifts.

2. Cis-Trans Isomerases: These enzymes catalyze the interconversion of cis and trans geometric isomers of carbon-carbon double bonds. They are often involved in the biosynthesis of complex lipids and other biological molecules where specific stereochemistry is required for proper function.

3. Peroxisomal Isomerases: These enzymes are involved in the metabolism of fatty acids with very long chains (VLCFA) in peroxisomes. They catalyze the conversion of cis-delta(3)-double bonds to trans-delta(2)-double bonds, which is a necessary step for further processing and degradation of VLCFAs.

4. Retinal Isomerases: These enzymes are involved in the visual cycle and catalyze the conversion of 11-cis-retinal into all-trans-retinal during the process of vision.

5. Carotenoid Isomerases: These enzymes are involved in the biosynthesis of carotenoids, which are pigments found in plants and microorganisms. They catalyze the conversion of cis-configured carotenoids into trans-configured forms, which have higher stability and bioactivity.

In general, carbon-carbon double bond isomerases function by lowering the energy barrier for a specific isomerization reaction, allowing it to occur under physiological conditions. They often require cofactors or other proteins to facilitate their activity, and their regulation is critical for maintaining proper metabolism and homeostasis in cells.

Peptidylprolyl Isomerase (PPIase) is an enzyme that catalyzes the cis-trans isomerization of peptidyl-prolyl bonds in proteins. This isomerization process, which involves the rotation around a proline bond, is a rate-limiting step in protein folding and can be a significant factor in the development of various diseases, including neurodegenerative disorders and cancer.

PPIases are classified into three families: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. These enzymes play important roles in protein folding, trafficking, and degradation, as well as in signal transduction pathways and the regulation of gene expression.

Inhibitors of PPIases have been developed as potential therapeutic agents for various diseases, including transplant rejection, autoimmune disorders, and cancer. For example, cyclosporine A and FK506 are immunosuppressive drugs that inhibit cyclophilins and FKBPs, respectively, and are used to prevent transplant rejection.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

Carbohydrate epimerases are a group of enzymes that catalyze the interconversion of specific stereoisomers (epimers) of carbohydrates by the reversible oxidation and reduction of carbon atoms, usually at the fourth or fifth position. These enzymes play important roles in the biosynthesis and modification of various carbohydrate-containing molecules, such as glycoproteins, proteoglycans, and glycolipids, which are involved in numerous biological processes including cell recognition, signaling, and adhesion.

The reaction catalyzed by carbohydrate epimerases involves the transfer of a hydrogen atom and a proton between two adjacent carbon atoms, leading to the formation of new stereochemical configurations at these positions. This process can result in the conversion of one epimer into another, thereby expanding the structural diversity of carbohydrates and their derivatives.

Carbohydrate epimerases are classified based on the type of substrate they act upon and the specific stereochemical changes they induce. Some examples include UDP-glucose 4-epimerase, which interconverts UDP-glucose and UDP-galactose; UDP-N-acetylglucosamine 2-epimerase, which converts UDP-N-acetylglucosamine to UDP-N-acetylmannosamine; and GDP-fucose synthase, which catalyzes the conversion of GDP-mannose to GDP-fucose.

Understanding the function and regulation of carbohydrate epimerases is crucial for elucidating their roles in various biological processes and developing strategies for targeting them in therapeutic interventions.

Imidazolidines are a class of heterocyclic organic compounds that contain a four-membered ring with two nitrogen atoms and two carbon atoms. The nitrogen atoms are adjacent to each other in the ring structure. These compounds have various applications, including as building blocks for pharmaceuticals and other organic materials. However, I couldn't find a specific medical definition related to disease or pathology for "imidazolidines." If you have any further questions or need information about a specific imidazolidine derivative with medicinal properties, please let me know!

Protein Disulfide-Isomerases (PDIs) are a family of enzymes found in the endoplasmic reticulum (ER) of eukaryotic cells. They play a crucial role in the folding and maturation of proteins by catalyzing the formation, breakage, and rearrangement of disulfide bonds between cysteine residues in proteins. This process helps to stabilize the three-dimensional structure of proteins and is essential for their proper function. PDIs also have chaperone activity, helping to prevent protein aggregation and assisting in the correct folding of nascent polypeptides. Dysregulation of PDI function has been implicated in various diseases, including cancer, neurodegenerative disorders, and diabetes.

Steroid isomerases are a class of enzymes that catalyze the interconversion of steroids by rearranging various chemical bonds within their structures, leading to the formation of isomers. These enzymes play crucial roles in steroid biosynthesis and metabolism, enabling the production of a diverse array of steroid hormones with distinct biological activities.

There are several types of steroid isomerases, including:

1. 3-beta-hydroxysteroid dehydrogenase/delta(5)-delta(4) isomerase (3-beta-HSD): This enzyme catalyzes the conversion of delta(5) steroids to delta(4) steroids, accompanied by the oxidation of a 3-beta-hydroxyl group to a keto group. It is essential for the biosynthesis of progesterone, cortisol, and aldosterone.
2. Aromatase: This enzyme converts androgens (such as testosterone) into estrogens (such as estradiol) by introducing a phenolic ring, which results in the formation of an aromatic A-ring. It is critical for the development and maintenance of female secondary sexual characteristics.
3. 17-beta-hydroxysteroid dehydrogenase (17-beta-HSD): This enzyme catalyzes the interconversion between 17-keto and 17-beta-hydroxy steroids, playing a key role in the biosynthesis of estrogens, androgens, and glucocorticoids.
4. 5-alpha-reductase: This enzyme catalyzes the conversion of testosterone to dihydrotestosterone (DHT) by reducing the double bond between carbons 4 and 5 in the A-ring. DHT is a more potent androgen than testosterone, playing essential roles in male sexual development and prostate growth.
5. 20-alpha-hydroxysteroid dehydrogenase (20-alpha-HSD): This enzyme catalyzes the conversion of corticosterone to aldosterone, a critical mineralocorticoid involved in regulating electrolyte and fluid balance.
6. 3-beta-hydroxysteroid dehydrogenase (3-beta-HSD): This enzyme catalyzes the conversion of pregnenolone to progesterone and 17-alpha-hydroxypregnenolone to 17-alpha-hydroxyprogesterone, which are essential intermediates in steroid hormone biosynthesis.

These enzymes play crucial roles in the biosynthesis, metabolism, and elimination of various steroid hormones, ensuring proper endocrine function and homeostasis. Dysregulation or mutations in these enzymes can lead to various endocrine disorders, including congenital adrenal hyperplasia (CAH), polycystic ovary syndrome (PCOS), androgen insensitivity syndrome (AIS), and others.

Cyclophilins are a family of proteins that have peptidyl-prolyl isomerase activity, which means they help with the folding and functioning of other proteins in cells. They were first identified as binding proteins for the immunosuppressive drug cyclosporine A, hence their name.

Cyclophilins are found in various organisms, including humans, and play important roles in many cellular processes such as signal transduction, protein trafficking, and gene expression. In addition to their role in normal cell function, cyclophilins have also been implicated in several diseases, including viral infections, cancer, and neurodegenerative disorders.

In medicine, the most well-known use of cyclophilins is as a target for immunosuppressive drugs used in organ transplantation. Cyclosporine A and its derivatives work by binding to cyclophilins, which inhibits their activity and subsequently suppresses the immune response.

Sorbitol is a type of sugar alcohol used as a sweetener in food and drinks, with about half the calories of table sugar. In a medical context, sorbitol is often used as a laxative to treat constipation, or as a sugar substitute for people with diabetes. It's also used as a bulk sweetener and humectant (a substance that helps retain moisture) in various pharmaceutical and cosmetic products.

When consumed in large amounts, sorbitol can have a laxative effect because it's not fully absorbed by the body and draws water into the intestines, which can lead to diarrhea. It's important for people with certain digestive disorders, such as irritable bowel syndrome or fructose intolerance, to avoid sorbitol and other sugar alcohols, as they can cause gastrointestinal symptoms like bloating, gas, and diarrhea.

The systematic name of this enzyme class is hydroxypyruvate aldose-ketose-isomerase. This enzyme participates in glyoxylate and ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... de Windt FE, van der Drift C (1980). "Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus". ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
The systematic name of this enzyme class is 11-deoxycorticosterone aldose-ketose-isomerase. Martin KO, Oh SW, Lee HJ, Monder C ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a corticosteroid side-chain-isomerase (EC 5.3.1.21) is an enzyme that catalyzes the chemical reaction 11- ... Monder C, Martin KO, Bogumil J (1980). "Presence of epimerase activity in hamster liver corticosteroid side chain isomerase". J ...
The systematic name of this enzyme class is D-arabinose aldose-ketose-isomerase. Other names in common use include D-arabinose( ... L-fucose) isomerase, D-arabinose isomerase, L-fucose isomerase, and D-arabinose ketol-isomerase. As of late 2007, only one ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, an arabinose isomerase (EC 5.3.1.3) is an enzyme that catalyzes the chemical reaction D-arabinose ⇌ {\ ...
The systematic name of this enzyme class is L-fucose aldose-ketose-isomerase. This enzyme participates in fructose and mannose ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a L-fucose isomerase (EC 5.3.1.25) is an enzyme that catalyzes the chemical reaction L-fucose ⇌ {\displaystyle \ ... The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and has no sequence or structural similarity ...
The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... L-arabinose isomerase". J. Biol. Chem. 231 (2): 1031-7. PMID 13539034. Nakamatu T, Yamanaka K (1969). "Crystallization and ... In enzymology, a L-arabinose isomerase (EC 5.3.1.4) is an enzyme that catalyzes the chemical reaction L-arabinose ⇌ {\ ...
The systematic name of this enzyme class is D-lyxose aldose-ketose-isomerase. Other names in common use include D-lyxose ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a D-lyxose ketol-isomerase (EC 5.3.1.15) is an enzyme that catalyzes the chemical reaction D-lyxose ⇌ {\ ... ANDERSON RL, ALLISON DP (1965). "Purification and Characterization of D-Lyxose Isomerase". J. Biol. Chem. 240: 2367-72. PMID ...
The systematic name of this enzyme class is L-rhamnose aldose-ketose-isomerase. Other names in common use include rhamnose ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... I. L-Rhamnose Isomerase from Lactobacillus Plantarum". Biochem. Z. 339: 145-53. PMID 14095156. Portal: Biology v t e (EC 5.3.1 ... In enzymology, a L-rhamnose isomerase (EC 5.3.1.14) is an enzyme that catalyzes the chemical reaction L-rhamnose ⇌ {\ ...
The systematic name of this enzyme class is D-glucuronate aldose-ketose-isomerase. Other names in common use include uronic ... isomerase, uronate isomerase, D-glucuronate isomerase, uronic acid isomerase, and D-glucuronate ketol-isomerase. This enzyme ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a glucuronate isomerase (EC 5.3.1.12) is an enzyme that catalyzes the chemical reaction D-glucuronate ⇌ {\ ...
The systematic name of this enzyme class is D-xylose aldose-ketose-isomerase. Other names in common use include D-xylose ... specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The isomerase has now been observed in ... Xylose-isomerases are also commonly called fructose-isomerases due to their ability to interconvert glucose and fructose. ... isomerase, D-xylose ketoisomerase, and D-xylose ketol-isomerase. The activity of D-xylose isomerase was first observed by ...
The systematic name of this enzyme class is D-ribose aldose-ketose-isomerase. Other names in common use include D-ribose ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a ribose isomerase (EC 5.3.1.20) is an enzyme that catalyzes the chemical reaction D-ribose ⇌ {\displaystyle \ ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
The systematic name of this enzyme class is D-mannose aldose-ketose-isomerase. Other names in common use include D-mannose ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a mannose isomerase (EC 5.3.1.7) is an enzyme that catalyzes the chemical reaction D-mannose ⇌ {\displaystyle \ ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
The systematic name of this enzyme class is D-galactose-6-phosphate aldose-ketose-isomerase. This enzyme participates in ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a galactose-6-phosphate isomerase (EC 5.3.1.26) is an enzyme that catalyzes the chemical reaction D-galactose 6- ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
The systematic name of this enzyme class is D-arabinose-5-phosphate aldose-ketose-isomerase. Other names in common use include ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, an arabinose-5-phosphate isomerase (EC 5.3.1.13) is an enzyme that catalyzes the chemical reaction D-arabinose 5 ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
The systematic name of this enzyme class is D-ribose-5-phosphate aldose-ketose-isomerase. RpiA in human beings is encoded on ... Ribose-5-phosphate isomerase deficiency is mutated in a rare disorder, Ribose-5-phosphate isomerase deficiency. The disease has ... Ribose-5-phosphate isomerase (Rpi) encoded by the RPIA gene is an enzyme (EC 5.3.1.6) that catalyzes the conversion between ... The first is an insertion of a premature stop codon into the gene encoding the isomerase, and the second is a missense mutation ...
... anthranilate aldose-ketose-isomerase. Other names in common use include: PRA isomerase, PRAI, IGPS:PRAI (indole-3-glycerol- ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... As the name phosphoribosylanthranilate isomerase suggests, it functions as an isomerase, rearranging the parts of the molecule ... Phosphoribosylanthranilate isomerase is also found in various forms of fungi such as Kluyveromyces lactis (yeast), ...
The systematic name of this enzyme class is 4-deoxy-L-threo-5-hexosulose-uronate aldose-ketose-isomerase. This enzyme is also ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... In enzymology, a 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (EC 5.3.1.17) is an enzyme that catalyzes the chemical ... Preiss J (1966). "4-Deoxy-L-threo-5-hexosulose uronic acid isomerase". Carbohydrate Metabolism. Methods in Enzymology. Vol. 9. ...
... aldose-ketose-isomerase, 1-phospho-5'-S-methylthioribose isomerase, and S-methyl-5-thio-D-ribose-1-phosphate aldose-ketose- ... The systematic name of this enzyme class is S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase. Other names in ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... 1-PMTR isomerase, 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, S-methyl-5-thio-5-deoxy-D-ribose-1-phosphate ketol ...
... aldose-ketose isomerases MeSH D08.811.399.475.200.174 - autocrine motility factor MeSH D08.811.399.475.200.350 - glucose-6- ... triose-phosphate isomerase MeSH D08.811.399.475.400 - carbon-carbon double bond isomerases MeSH D08.811.399.475.400.700 - ... steroid isomerases MeSH D08.811.399.475.800 - sulfur-sulfur bond isomerases MeSH D08.811.399.475.800.550 - protein disulfide- ... phosphate isomerase MeSH D08.811.399.475.200.550 - mannose-6-phosphate isomerase MeSH D08.811.399.475.200.662 - neuroleukin ...
... imidazole-4-carboxamide aldose-ketose-isomerase. This enzyme catalyses the following chemical reaction 1-(5-phosphoribosyl)-5 ... 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase (EC 5.3.1.16, N-(5-phospho-D- ... 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide+isomerase at the U.S. National Library ... isomerase) of histidine biosynthesis from Salmonella typhimurium". The Journal of Biological Chemistry. 241 (14): 3262-9. PMID ...
... is an enzyme with systematic name D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase. This enzyme catalyses the ... D-sedoheptulose 7-phosphate isomerase (EC 5.3.1.28, sedoheptulose-7-phosphate isomerase, phosphoheptose isomerase, gmhA (gene ... D-sedoheptulose+7-phosphate+isomerase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Kim MS, Shin DH (November 2009). "A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia ...
Like most sugar isomerases, glucose isomerase catalyzes the interconversion of aldoses and ketoses. The conversion of glucose ... Phosphohexose Isomerase Deficiency (PHI) is also known as phosphoglucose isomerase deficiency or Glucose-6-phosphate isomerase ... Generally, "the names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate ... A ketose is then formed and the ring is closed again. Glucose-6-phosphate first binds to the active site of the isomerase. The ...
MPI must convert an aldose (mannose) to a ketose (fructose), in addition to opening and closing the rings for these sugars. In ... Mannose-6 phosphate isomerase (MPI), alternately phosphomannose isomerase (PMI) (EC 5.3.1.8) is an enzyme which facilitates the ... anomeric form used by phosphomannose isomerase and its 1-epimerization by phosphoglucose isomerase". The Journal of Biological ... "Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle ...
The mechanism that GPI uses to interconvert glucose 6-phosphate and fructose 6-phosphate (aldose to ketose) consists of three ... Glucose-6-phosphate isomerase in PROSITE Phosphoglucose Isomerase Glucose phosphate isomerase deficiency This article ... Glucose-6-phosphate isomerase (GPI), alternatively known as phosphoglucose isomerase/phosphoglucoisomerase (PGI) or ... Swan MK, Hansen T, Schönheit P, Davies C (September 2004). "A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase ...
Meyerhoff and Junowicz found that the equilibrium constant for the isomerase and aldoses reaction were not affected by ... a ketose), and glyceraldehyde 3-phosphate (an aldose). There are two classes of aldolases: class I aldolases, present in ... Cofactors: Mg2+ G6P is then rearranged into fructose 6-phosphate (F6P) by glucose phosphate isomerase. Fructose can also enter ... The reaction requires an enzyme, phosphoglucose isomerase, to proceed. This reaction is freely reversible under normal cell ...
This isomerization of a ketose to an aldose proceeds through an cis-enediol(ate) intermediate. This isomerization proceeds ... Triose Phosphate Isomerase is a member of the alpha and beta (α/β) class of proteins; it is a homodimer, and each subunit ... "Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human ... Triosephosphate isomerase is an enzyme that in humans is encoded by the TPI1 gene. This gene encodes an enzyme, consisting of ...
... a ketose), found in avocadoes L-glycero-D-manno-heptose (an aldose), a late intermediate in lipid A biosynthesis. Horecker, B. ... "Structure and Function of Sedoheptulose-7-phosphate Isomerase, a Critical Enzyme for Lipopolysaccharide Biosynthesis and a ... a ketose), an intermediate in the Calvin cycle and in lipid A biosynthesis mannoheptulose ( ...
The systematic name of this enzyme class is hydroxypyruvate aldose-ketose-isomerase. This enzyme participates in glyoxylate and ... This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ... de Windt FE, van der Drift C (1980). "Purification and some properties of hydroxypyruvate isomerase of Bacillus fastidiosus". ... Portal: Biology v t e (EC 5.3.1, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
Aldose-Ketose Isomerases. , Amino Acid Transport Systems. , Anti-Inflammatory Agents. , Cells, Cultured. , Cytokines. , Gene ...
D-xylose isomerase; D-xylose ketoisomerase; D-xylose ketol-isomerase; D-xylose aldose-ketose-isomerase. ... β-L-arabinopyranose aldose-ketose-isomerase. Comments:. Requires a divalent metal ion (the enzyme from the bacterium ... α-D-xylopyranose aldose-ketose-isomerase. Comments:. Contains two divalent metal ions, preferably magnesium, located at ... Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase. Proc. Natl. ...
Aldose-Ketose Isomerases, Base Sequence, Carbohydrate Epimerases, Ethanol, Fermentation, Genes, Bacterial, Molecular Sequence ... Aldose-Ketose Isomerases; Base Sequence; Carbohydrate Epimerases; Ethanol; Fermentation; Genes, Bacterial; Molecular Sequence ... The recombinant xylose isomerase showed the highest activity at 85 degrees C with a specific activity of 1.0 U mg-1. A new ... The recombinant xylose isomerase showed the highest activity at 85 degrees C with a specific activity of 1.0 U mg-1. A new ...
MeSH headings : Aldose-Ketose Isomerases / chemistry; Aldose-Ketose Isomerases / classification; Aldose-Ketose Isomerases / ... Glucose-to-fructose conversion at high temperatures with xylose (glucose) isomerases from Streptomyces murinus and two ...
Systematic name: D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase Comments: In Gram-negative bacteria the enzyme ... Other name(s): sedoheptulose-7-phosphate isomerase; phosphoheptose isomerase; gmhA (gene name); lpcA (gene name). ... Accepted name: D-sedoheptulose-7-phosphate isomerase. Reaction: D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7- ... 4. Kim, M.S. and Shin, D.H. A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei. ...
Isomerases may catalyze the conversion of an aldose to a ketose, and mutases catalyze reactions in which a functional group is ... isomerases. reactions in which a compound is converted to its isomer. ...
Ketose Aldose Isomerases use Aldose-Ketose Isomerases Ketose-Aldose Isomerases use Aldose-Ketose Isomerases ... Ketol-Isomerase, 2-Amino-2-Deoxy-D-Glucose-6-Phosphate use Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) ...
Ketose-Aldose Isomerases use Aldose-Ketose Isomerases Ketoses Ketosis Ketosis, Diabetic use Diabetic Ketoacidosis ...
Ketose Aldose Isomerases use Aldose-Ketose Isomerases Ketose-Aldose Isomerases use Aldose-Ketose Isomerases ... Ketol-Isomerase, 2-Amino-2-Deoxy-D-Glucose-6-Phosphate use Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) ...
Aldose-Ketose Isomerases Bacillus subtilis regulation métabolisme carboné structure protéique Domains Molecular biology ...
As shown in Table 1, isomerases that are specific for 2R-aldoses were found to activate the 1-R proton of the ketose produced. ... The enzyme catalyzing this reaction is phosphohexose isomerase (also known as phosphoglucose isomerase). 0 0 ... The enzyme catalyzing this reaction is phosphohexose isomerase (also known as phosphoglucose isomerase). 0 0 ... The anomeric specificities of 5 isomerases were determined in the course of our studies on the isomerases that continued until ...
intramolecular oxidoreductase activity, interconverting aldoses and ketoses. IEP. Enrichment. MF. GO:0016874. ligase activity. ... glucose-6-phosphate isomerase activity. IEP. Enrichment. MF. GO:0004375. glycine dehydrogenase (decarboxylating) activity. IEP ... peptidyl-prolyl cis-trans isomerase activity. IEP. Enrichment. MF. GO:0004329. formate-tetrahydrofolate ligase activity. IEP. ...
intramolecular oxidoreductase activity, interconverting aldoses and ketoses. None. Extended. BP. GO:0019752. carboxylic acid ... N-(5-phosphoribosyl)anthranilate isomerase [Ensembl]..... 0.16. OrthoFinder. AGT24681. N559_3018. bifunctional indole-3- ... phosphoribosylanthranilate isomerase activity. IEA. Interproscan. BP. GO:0006082. organic acid metabolic process. None. ... Description : indole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase [Ensembl]. Indole-3-glycerol ...
intramolecular oxidoreductase activity, interconverting aldoses and ketoses. IEP. HCCA. InterPro domains. Description. Start. ... triose-phosphate isomerase activity. IEP. HCCA. MF. GO:0016860. intramolecular oxidoreductase activity. IEP. HCCA. ...
The Fehling test is a classic method for the detection of aldoses.[150] Due to mutarotation, glucose is always present to a ... Glucose can also be converted from bacterial xylose isomerase to fructose. In addition, glucose metabolites produce all ... Therefore, glucose is also classified as an aldose, or an aldohexose. The aldehyde group makes glucose a reducing sugar giving ...
intramolecular oxidoreductase activity, interconverting aldoses and ketoses. IEP. Neighborhood. MF. GO:0016880. acid-ammonia ( ... ribose-5-phosphate isomerase activity. IEP. Neighborhood. MF. GO:0004807. triose-phosphate isomerase activity. IEP. ...
... ketose,/p,, ,p,enantiomers,/p, and others. Study with Knowt flashcards for free. ...
We showed that the homogeneous aldol-ketose isomerization mechanism is similar to that over Sn-BEA. Hydrolysis of the salt ... 2-intramolecular carbon shift reactions of aldoses, for example, various molybdenum oxide and molybdate species and alkali- ... that the Sn4+ centers catalyze the intramolecular H-shift to fructose similarly to the reaction catalyzed by D-xylose isomerase ...
The presence of an aldehyde group in aldoses and the primary hydroxyl groups of aldoses and ketoses enables their further ... Phosphohexose isomerase. liver?, brain?. Liver enlargement, CNS damage, ``dancing eye symptoms (nystagmus), tremors, muscle ... Aldoses and ketoses can also be enzymatically reduced to polyhydroxyalcohols, the so-called alcoholic sugars - alditols , by ... on the C1 carbon of aldoses and the C2 carbon of ketoses), forming so-called glycosides, and their bond is called a glycosidic ...
Fructose is a 6-carbon hexose with a ketone group (ketose), while ribulose and xylulose have 5 carbons (incorrect answers d, e ... Triose phosphate isomerase interconverts dihydroxyacetone phosphate and glyceraldehyde 3-phosphate without phosphorylation ( ... and aldoses with a C1 aldehyde group (glucose, galactose, and mannose). All are reducing sugars that will give a positive ... Fructose is among several carbohydrate groups known as ketoses because it possesses a ketone group. The ketone group is at ...
glucose, an aldose, and fructose, a ketose differ only in the position of the carbonyl group ...
ALDOSE-KETOSE ISOMERASE. .shs-wrapper-processed { display:flex; flex-direction: row; flex-wrap: wrap; } .shs-wrapper-processed ...
MeSH Terms: Aldose-Ketose Isomerases/genetics*; Arabidopsis/classification; Arabidopsis/genetics*; Cloning, Molecular; Cytosine ...
Aldose-Ketose Isomerases / genetics Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Enzymes that catalyze the interconversion of aldose and ketose compounds.. Terms. Aldose-Ketose Isomerases Preferred Term Term ... Enzymes that catalyze the interconversion of aldose and ketose compounds.. Entry Term(s). Ketose-Aldose Isomerases Registry ... Isomerases [D08.811.399] * Intramolecular Oxidoreductases [D08.811.399.475] * Aldose-Ketose Isomerases [D08.811.399.475.200] * ... Ketose-Aldose Isomerases Term UI T058732. Date04/11/1997. LexicalTag NON. ThesaurusID NLM (1998). ...
Enzymes that catalyze the interconversion of aldose and ketose compounds.. Terms. Aldose-Ketose Isomerases Preferred Term Term ... Enzymes that catalyze the interconversion of aldose and ketose compounds.. Entry Term(s). Ketose-Aldose Isomerases Registry ... Isomerases [D08.811.399] * Intramolecular Oxidoreductases [D08.811.399.475] * Aldose-Ketose Isomerases [D08.811.399.475.200] * ... Ketose-Aldose Isomerases Term UI T058732. Date04/11/1997. LexicalTag NON. ThesaurusID NLM (1998). ...
... phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose isomerization. Here we describe the human recombinant ... The second enzyme in the glycolytic pathway, phosphoglucose isomerase (PGI), catalyses an intracellular aldose-ketose ... Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps A T Cordeiro 1 , P H C Godoi, C ... Glucose-6-phosphate isomerase. Achari A, Marshall SE, Muirhead H, Palmieri RH, Noltmann EA. Achari A, et al. Philos Trans R Soc ...
scientific article published on July 1, 1980
Aldose-Ketose Isomerases. [NCBI]. Gene. Gene. Link. Information. Gain. 01. XYLB [NCBI] 7.3128e-05 GNPDA1 [NCBI] 1.93278e-05 ... ribose 5-phosphate isomerase deficiency [NCBI] 0.000274729 GNPI [NCBI] 0.00023396 RPIA [NCBI] 4.95167e-05 H6PD [NCBI] 2.747e-05 ...
Aldose Ketose Isomerases Isomerases, Aldose-Ketose Isomerases, Ketose-Aldose Ketose Aldose Isomerases Ketose-Aldose Isomerases ... Aldose Ketose Isomerases. Isomerases, Aldose-Ketose. Isomerases, Ketose-Aldose. Ketose Aldose Isomerases. Ketose-Aldose ... Aldose-Ketose Isomerases - Preferred Concept UI. M0029314. Scope note. Enzymes that catalyze the interconversion of aldose and ... Enzymes that catalyze the interconversion of aldose and ketose compounds.. Allowable Qualifiers:. AD administration & dosage. ...
Aldehyde-Lyases N0000008128 Aldehydes N0000006812 aldesleukin N0000166716 Aldicarb N0000168087 Aldose-Ketose Isomerases ... N0000168085 Protein Disulfide-Isomerases N0000170091 Protein Hydrolysates N0000170469 Protein Inhibitors of Activated STAT ... N0000008168 Amines N0000170225 Amino Acid Chloromethyl Ketones N0000168100 Amino Acid Isomerases N0000167825 Amino Acid ... Monoxide N0000166118 Carbon Radioisotopes N0000166327 Carbon Tetrachloride N0000168091 Carbon-Carbon Double Bond Isomerases ...
Ketose-Aldose Isomerases use Aldose-Ketose Isomerases. Ketoses. Ketosis. Ketosis, Diabetic use Diabetic Ketoacidosis ...
D8.811.520.224.62 Aldose-Ketose Isomerases D8.586.399.475.200 D8.811.399.475.200 Aldosterone D6.472.40.668.478.561.187 D6.472. ... D8.811.464.263.200.450 Isomerases D8.586.399 D8.811.399 Isometric Contraction G11.427.661.472 G11.427.792.540.472 Isopoda ... D3.494.154 Carbon-Carbon Double Bond Isomerases D8.586.399.475.400 D8.811.399.475.400 Carbon-Carbon Ligases D8.586.464.257 ... B1.500.272.727.300 cis-trans-Isomerases D8.586.399.325 D8.811.399.325 Citrate (si)-Synthase D8.586.520.224.600.400 D8.811. ...
Aldose-Ketose Isomerases Aldosterone Aldrin Alendronate Alert Fatigue, Health Personnel Aleurites Aleutian Mink Disease ... Amino Acid Isomerases Amino Acid Metabolism, Inborn Errors Amino Acid Motifs Amino Acid Oxidoreductases Amino Acid Sequence ... cis-trans-Isomerases Cisapride Cisplatin Cissampelos Cissus Cistaceae Cistanche Cisterna Magna Cistus Citalopram Cities ... Dodecenoyl-CoA Isomerase Dog Diseases Dogfish Dogs Dolichol Dolichol Monophosphate Mannose Dolichol Phosphates Dolichos ...
We showed that the homogeneous aldol-ketose isomerization mechanism is similar to that over Sn-BEA. Hydrolysis of the salt ... 2-intramolecular carbon shift reactions of aldoses, for example, various molybdenum oxide and molybdate species and alkali- ... that the Sn4+ centers catalyze the intramolecular H-shift to fructose similarly to the reaction catalyzed by D-xylose isomerase ...
Because °H is irreversibly lost at the isomerase step to *H,O, the principal *H-labeled metabolite of [2-°H]glucose, such ... These can spontaneously undergo Amadori re- arrangements to 1-amino-1-deoxy-2-ketoses, reactions which would cause loss of 9H ... Amino acids are known to react with glucose and other aldoses to form N-substituted glyco- sylamines. ... cose-6-P derived from the rapid reversibility of the isomerase step would then return ["C]glucose without the °H label back to ...
  • The recombinant xylose isomerase showed the highest activity at 85 degrees C with a specific activity of 1.0 U mg-1. (lu.se)
  • The systematic name of this enzyme class is hydroxypyruvate aldose-ketose-isomerase. (wikipedia.org)
  • The Thermus thermophilus xylA gene encoding xylose (glucose) isomerase was cloned and expressed in Saccharomyces cerevisiae under the control of the yeast PGK1 promoter. (lu.se)
  • Dephosphorylation of the detritiated but still 'C-labeled glu- cose-6-P derived from the rapid reversibility of the isomerase step would then return ["C]glucose without the °H label back to the glucose pool. (nih.gov)
  • Because °H is irreversibly lost at the isomerase step to *H,O, the principal *H-labeled metabolite of [2-°H]glucose, such dephosphorylation would affect neither the production of *H-labeled metabolites nor the specific activity of the (*H]glucose pool. (nih.gov)