Dehydrogenase, Sorbitol
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  Dehydrogenase, Sorbitol



Dehydrogenase, Sorbitol

   An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14

RELATED TERMS
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Alcohol
An organic chemical in which one or more hydroxyl (OH) groups are attached to carbon (C) atoms in place of hydrogen (H) atoms. Common alcohols include ethyl alcohol or ethanol (found in alcoholic beverages), methyl alcohol or methanol (can cause blindness) and propyl alcohol or propanol (used as a solvent and antiseptic). Rubbing alcohol is a mixture of acetone, methyl isobutyl ketone, and ethyl alcohol. In everyday talk, alcohol usually refers to ethanol as, for example, in wine, beer, and liquor. It can cause changes in behavior and be addictive.

Oxidation
A process in which free radicals released during metabolism damage cells and the DNA that control cell growth. Oxidation can accelerate the process of atherosclerosis by damaging particles of low-density lipoprotein cholesterol, making them more potent as a plaque builder.

Sugar
A class of carbohydrates that taste sweet. Sugar is a quick and easy fuel for the body to use. Types of sugar are lactose, glucose, fructose, and sucrose.



SIMILAR TERMS
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Dehydrase, Carbamoylaspartic
An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.

Dehydrase, Diol
An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

Dehydrase, Threonine
A pyridoxal-phosphate protein that catalyzes the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. EC 4.2.1.16.

Dehydrases, beta-Hydroxyacyl-CoA
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.

Dehydratase, Aminolevulinic Acid
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.

Dehydratase, Carbonate
A family of zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide. They play an important role in the transport of CARBON DIOXIDE from the tissues to the LUNG. EC 4.2.1.1.

Dehydratase, Chorismate Mutase-Prephenate
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.

Dehydratase, delta-Aminolevulinate
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.

Dehydratase, delta-Aminolevulinic Acid
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.

Dehydratase, Diol
An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

Dehydratase, Homoserine
A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.

Dehydratase, L-Serine
An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.

Dehydratase, Prephenate
An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51.

Dehydratase, Propanediol
An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.

Dehydratase, Serine
An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.

Dehydratase, Serine-Threonine
An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.

Dehydratase, Threonine
A pyridoxal-phosphate protein that catalyzes the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. EC 4.2.1.16.

Dehydratases
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.

Dehydratases, 3-Hydroxyacyl
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.

Dehydratases, beta-Hydroxyacyl
An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonyl-CoA. EC 4.2.1.17.

Dehydration
Loss of fluids from the body, often caused by diarrhea. May result in loss of important salts and minerals.

Dehydrations
The condition that results from excessive loss of body water.

Dehydroascorbatase
Catalyzes the hydrolysis of the gamma lactone, dehydroascorbate, to diketogulonate.

Dehydroascorbic Acid
The reversibly oxidized form of ascorbic acid. It is the lactone of 2,3-DIKETOGULONIC ACID and has antiscorbutic activity in man on oral ingestion.

Dehydrobenzperidol
A butyrophenone with general properties similar to those of HALOPERIDOL. It is used in conjunction with an opioid analgesic such as FENTANYL to maintain the patient in a calm state of neuroleptanalgesia with indifference to surroundings but still able to cooperate with the surgeon. It is also used as a premedicant, as an antiemetic, and for the control of agitation in acute psychoses. (From Martindale, The Extra Pharmacopoeia, 29th ed, p593)

Dehydrobilirubin
1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of amphibia and of birds, but not in normal human bile or serum.

Dehydrocholate
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholate, Sodium
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholesterols
Cholesterol derivatives having an additional double bond in any position. 24-Dehydrocholesterol is DESMOSTEROL. The other most prevalent dehydrocholesterol is the 7-isomer. This compound is a precursor of cholesterol and of vitamin D3.

Dehydrocholic Acid
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholic Acid, Lithium Salt
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholic Acid, Magnesium Salt
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholic Acid, Potassium Salt
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocholic Acid, Sodium Salt
A semisynthetic bile acid made from cholic acid. It is used as a cholagogue, hydrocholeretic, diuretic, and as a diagnostic aid.

Dehydrocortisone
A synthetic anti-inflammatory glucocorticoid derived from CORTISONE. It is biologically inert and converted to PREDNISOLONE in the liver.

Dehydroepiandrosterone
DHEA. A steroid hormone made by the adrenal glands that acts on the body much like testosterone and is converted into testosterone and estrogen. DHEA and its sulfate (DHEAS) are abundant in the body, but their normal roles are not fully understood. The blood levels of DHEA and DHEAS decline with age.

Dehydroepiandrosterone Sulfate
A precursor of androgens and estrogen and the most abundant steroid in the circulation. (J Gerontol 1993;48(5):B196-200)

Dehydrogenase
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

Dehydrogenase Complex, Pyruvate
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE C (LIPOAMIDE), dihydrolipoamide acetyltransferase and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phoshorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)

Dehydrogenase Deficiencies, Glucosephosphate
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of enzyme activity in erythrocytes, leading to hemolytic anemia.

Dehydrogenase Deficiency, Glucosephosphate
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of enzyme activity in erythrocytes, leading to hemolytic anemia.

Dehydrogenase E1, Aldehyde
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. EC 1.2.1.3. Before 1978, it was classified as EC 1.1.1.70.

Dehydrogenase E2, Aldehyde
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. EC 1.2.1.3. Before 1978, it was classified as EC 1.1.1.70.

Dehydrogenase, 17 beta-Estradiol
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62

Dehydrogenase, 20-beta-Hydroxysteroid
An enzyme that catalyzes the interconversion of a ketone and hydroxy group at C-20 of cortisone and other 17,20,21-trihydroxy steroids. EC 1.1.1.53.

Dehydrogenase, 3 beta-Hydroxy-delta-5-Steroid
An enzyme that catalyzes the reduction of a 3 beta-hydroxy-delta(5)-steroid to 3-oxo-delta(4)-steroid in the presence of NAD. It converts pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. EC 1.1.1.145.

Dehydrogenase, 3-beta-Hydroxysteroid
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

Dehydrogenase, 5,10-Methylenetetrahydrofolate
Catalyzes the oxidation of methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. Includes EC 1.5.1.15 which uses NAD+. EC 1.5.1.5.

Dehydrogenase, 5-Ene-3 beta-hydroxysteroid
An enzyme that catalyzes the reduction of a 3 beta-hydroxy-delta(5)-steroid to 3-oxo-delta(4)-steroid in the presence of NAD. It converts pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. EC 1.1.1.145.

Dehydrogenase, 6-Phosphogluconate
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.

Dehydrogenase, Acetoin
An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD. EC 1.1.1.5.

Dehydrogenase, Alcohol
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.

Dehydrogenase, Aldehyde
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. EC 1.2.1.3. Before 1978, it was classified as EC 1.1.1.70.

Dehydrogenase, Ascorbino
An enzyme that converts ascorbic acid to dehydroascorbic acid. EC 1.10.3.3.

Dehydrogenase, Aspartate-Semialdehyde
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.

Dehydrogenase, Aspartokinase Homoserine
An enzyme complex consisting of aspartokinase, EC 2.7.2.4, and homoserine dehydrogenase, EC 1.1.1.3. The complex has been isolated from E. coli and consists of four identical subunits with a molecular weight of 85,000. The enzyme complex is involved in the biosynthesis of amino acids of the aspartate family.

Dehydrogenase, beta-Hydroxyacyl CoA
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis. EC 1.1.1.35.

Dehydrogenase, Chorismate Mutase-Prephenate
An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.

Dehydrogenase, D-Glucuronolactone
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. EC 1.2.1.3. Before 1978, it was classified as EC 1.1.1.70.

Dehydrogenase, D-Mannonate-NAD
An enzyme that catalyzes the reversible oxidation of mannonate to fructuronate in the presence of NAD. Also reduces D-tagaturonate to D-altronate. EC 1.1.1.57.

Dehydrogenase, Decanoyl CoA
Enzymes that catalyze the conversion of saturated fatty acid CoA complexes to unsaturated fatty acid CoA complexes in the presence of any acceptor. They include EC 1.3.1.8, EC 1.3.99.3 and EC 1.14.99.5.

Dehydrogenase, Dihydrofolate
An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

Dehydrogenase, Dihydrolipoamide
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Dihydrolipoyl
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Estradiol
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62

Dehydrogenase, Glutamate
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

Dehydrogenase, Glyceraldehydephosphate
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Dehydrogenase, Homoserine
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.

Dehydrogenase, Hydroxyprostaglandin
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

Dehydrogenase, Hypoxanthine
An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria. EC 1.1.3.22.

Dehydrogenase, Iditol
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14

Dehydrogenase, Isocitrate
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

Dehydrogenase, Lactate
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.

Dehydrogenase, Lipoamide
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Lipoic Acid
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Lipoyl
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Malate
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

Dehydrogenase, Malic
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

Dehydrogenase, Methylenetetrahydrofolate
Catalyzes the oxidation of methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate. Includes EC 1.5.1.15 which uses NAD+. EC 1.5.1.5.

Dehydrogenase, NAD Isocitrate
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.

Dehydrogenase, NAD-Dependent Glyceraldehyde-3-phosphate
An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.

Dehydrogenase, NAD-Formate
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

Dehydrogenase, NAD-Malate
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.

Dehydrogenase, NADH
A flavoprotein containing iron. Cytochrome c may act as receptor. The enzyme catalyzes the oxidation of NADH to NAD and reduced acceptor. EC 1.6.99.3

Dehydrogenase, NADP
A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1.

Dehydrogenase, NADP+-Dependent Glutamate
An enzyme that catalyzes the conversion of L-glutamate, H2O, and NADP+ to 2-oxoglutarate, NH3, and NADPH. (From Enzyme Nomenclature, 1992) EC 1.4.1.4.

Dehydrogenase, NADP-Dependent Glutamate
An enzyme that catalyzes the conversion of L-glutamate, H2O, and NADP+ to 2-oxoglutarate, NH3, and NADPH. (From Enzyme Nomenclature, 1992) EC 1.4.1.4.

Dehydrogenase, NADP-Specific Glutamate
An enzyme that catalyzes the conversion of L-glutamate, H2O, and NADP+ to 2-oxoglutarate, NH3, and NADPH. (From Enzyme Nomenclature, 1992) EC 1.4.1.4.

Dehydrogenase, NADPH
A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1.

Dehydrogenase, NADPH-Dependent Glutamate
An enzyme that catalyzes the conversion of L-glutamate, H2O, and NADP+ to 2-oxoglutarate, NH3, and NADPH. (From Enzyme Nomenclature, 1992) EC 1.4.1.4.

Dehydrogenase, Phosphogluconate
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.

Dehydrogenase, Phosphoglyceraldehyde
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Dehydrogenase, Phosphorylating Glyceraldehyde-3-Phosphate
An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.

Dehydrogenase, Polyol
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14

Dehydrogenase, Prephenate
An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.

Dehydrogenase, Proline
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.

Dehydrogenase, Prostacyclin
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

Dehydrogenase, Semiaspartate Aldehyde
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.

Dehydrogenase, Tetrahydrofolate
An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

Dehydrogenase, Triosephosphate
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Dehydrogenase, UDP Glucose
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

Dehydrogenase, UDPG
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

Dehydrogenase, Valine Lipoamide
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, Xanthine
An enzyme that catalyzes the oxidation of xanthine in the presence of NAD+ to form urate and NADH. It acts also on a variety of other purines and aldehydes. EC 1.1.1.204.

Dehydrogenase, Yeast Alcohol
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.

Dehydrogenases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)

Dehydrogenases, 17 beta-Hydroxysteroid
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

Dehydrogenases, 17-Hydroxysteroid
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

Dehydrogenases, 20 Hydroxysteroid
Catalyze the oxidation of 20-hydroxysteroids to 20-ketosteroids. Includes EC 1.1.1.149 and EC 1.1.1.53.

Dehydrogenases, 20-Hydroxysteroid
Catalyze the oxidation of 20-hydroxysteroids to 20-ketosteroids. Includes EC 1.1.1.149 and EC 1.1.1.53.

Dehydrogenases, 3 Hydroxysteroid
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

Dehydrogenases, 3-Hydroxyacyl CoA
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis. EC 1.1.1.35.

Dehydrogenases, 3-Hydroxysteroid
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.

Dehydrogenases, Acyl CoA
Enzymes that catalyze the conversion of saturated fatty acid CoA complexes to unsaturated fatty acid CoA complexes in the presence of any acceptor. They include EC 1.3.1.8, EC 1.3.99.3 and EC 1.14.99.5.

Dehydrogenases, beta-Hydroxyacyl
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis. EC 1.1.1.35.

Dehydrogenases, Carbohydrate
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.

Dehydrogenases, Estradiol
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62

Dehydrogenases, Formate
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.

Dehydrogenases, Galactose
D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.

Dehydrogenases, Glucose
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.

Dehydrogenases, Glyceraldehyde-3-Phosphate
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Dehydrogenases, Hydroxyprostaglandin
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

Dehydrogenases, Hydroxysteroid
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.

Dehydrogenases, Saccharopine
A collection of enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS. EC 1.5.1.

Dehydrogenases, Sugar Alcohol
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.

Dehydrogenases, Sulfite
A molybdohemoprotein which catalyzes the terminal reaction in the oxidative degradation of sulfur-containing amino acids with the formation of a sulfate. Cytochrome c, ferricyanide and molecular oxygen can act as acceptors. A deficiency is manifested by brain damage and mental deterioration. EC 1.8.2.1 utilizes ferricytochrome C as acceptor. EC 1.8.3.1 uses molecular oxygen.

Dehydrogenases, Testosterone
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.

Dehydrogesterone
A synthetic progestational hormone with no androgenic or estrogenic properties. Unlike many other progestational compounds, dydrogesterone produces no increase in temperature and does not inhibit ovulation.

Dehydroisoandrosterone
A naturally occurring androgen isolated from urine.

Dehydroisoandrosterone Sulfate
A precursor of androgens and estrogen and the most abundant steroid in the circulation. (J Gerontol 1993;48(5):B196-200)

Dehydromethyltestosterone
A synthetic steroid with anabolic properties that are more pronounced than its androgenic effects. It has little progestational activity. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1188)



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Dehydrogenase, Valine Lipoamide
A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.

Dehydrogenase, UDPG
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

Dehydrogenase, UDP Glucose
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.

Dehydrogenase, Tetrahydrofolate
An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.

Dehydrogenase, Triosephosphate
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

Dehydrogenase, Sorbitol

Dehydrogenase, Semiaspartate Aldehyde
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.

Dehydrogenases, Saccharopine
A collection of enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS. EC 1.5.1.

Dehydrogenases, Hydroxysteroid
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.

Dehydrogenases, Hydroxyprostaglandin
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.

Dehydrogenases, Glyceraldehyde-3-Phosphate
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.

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