| D007521 |
Isocitrate Dehydrogenase |
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. |
NAD Isocitrate Dehydrogenase,Isocitrate Dehydrogenase (NAD+),Isocitrate Dehydrogenase-I,Dehydrogenase, Isocitrate,Dehydrogenase, NAD Isocitrate,Isocitrate Dehydrogenase I,Isocitrate Dehydrogenase, NAD |
|
| D007527 |
Isoenzymes |
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. |
Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes |
|
| D007931 |
Leucyl Aminopeptidase |
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide. |
Cytosol Aminopeptidase,Leucine Aminopeptidase,L-Leucylnaphthylamidase,Methoxyleucine Aminopeptidase,Peptidase S,Zinc-Manganese-Leucine Aminopeptidase,Aminopeptidase, Cytosol,Aminopeptidase, Leucine,Aminopeptidase, Leucyl,Aminopeptidase, Methoxyleucine,Aminopeptidase, Zinc-Manganese-Leucine,Zinc Manganese Leucine Aminopeptidase |
|
| D008875 |
Middle Aged |
An adult aged 45 - 64 years. |
Middle Age |
|
| D008970 |
Molecular Weight |
The sum of the weight of all the atoms in a molecule. |
Molecular Weights,Weight, Molecular,Weights, Molecular |
|
| D004591 |
Electrophoresis, Polyacrylamide Gel |
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. |
Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs |
|
| D005260 |
Female |
|
Females |
|
| D005956 |
Glucose-6-Phosphate Isomerase |
An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA. |
Glucosephosphate Isomerase,Phosphoglucose Isomerase,Phosphohexose Isomerase,Autocrine Motility Factor,Isomerase, Glucose 6 Phosphate,Neuroleukin,Tumor Autocrine Motility Factor,Tumor-Cell Autocrine Motility Factor,Factor, Autocrine Motility,Glucose 6 Phosphate Isomerase,Isomerase, Glucose-6-Phosphate,Isomerase, Glucosephosphate,Isomerase, Phosphoglucose,Isomerase, Phosphohexose,Motility Factor, Autocrine,Tumor Cell Autocrine Motility Factor |
|
| D005969 |
Glutamate Dehydrogenase |
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2. |
Dehydrogenase, Glutamate |
|
| D006224 |
Cricetinae |
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. |
Cricetus,Hamsters,Hamster |
|