| 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 |
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| D008025 |
Ligases |
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6. |
Ligase,Synthetases,Synthetase |
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| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
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| D010749 |
Phosphoprotein Phosphatases |
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) |
Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase |
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| D011485 |
Protein Binding |
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. |
Plasma Protein Binding Capacity,Binding, Protein |
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| D011994 |
Recombinant Proteins |
Proteins prepared by recombinant DNA technology. |
Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA |
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| D004926 |
Escherichia coli |
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. |
Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli |
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| D000071636 |
Protein Phosphatase 2C |
One of four major classes of mammalian serine/threonine specific protein phosphatases. Protein phosphatase 2C is a monomeric enzyme about 42 kDa in size. It shows broad substrate specificity dependent on divalent cations (mainly manganese and magnesium). Three isozymes are known in mammals: PP2C -alpha, -beta and -gamma. In yeast, there are four PP2C homologues: phosphatase PTC1 that have weak tyrosine phosphatase activity, phosphatase PTC2, phosphatase PTC3, and PTC4. Isozymes of PP2C also occur in Arabidopsis thaliana where the kinase-associated protein phosphatase (KAPP) containing a C-terminal PP2C domain, dephosphorylates Ser/Thr receptor-like kinase RLK5. |
Magnesium-Dependent Protein Phosphatase 2C beta,PP2C beta,PP2Cepsilon,PP2Cgamma,PPM1 Magnesium-Dependent Protein Phosphatases,PPM1 Protein Phosphatases,PPM1D Phosphatase,PPM1E Phosphatase,PPM1G Phosphatase,Ppm1b Phosphatase,Protein Phosphatase 1D Magnesium-Dependent, delta isoform,Protein Phosphatase 2C beta,Protein Phosphatase 2C delta,Protein Phosphatase 2C epsilon,Protein Phosphatase 2C gamma,Ptc2 Phosphatase,2C, Protein Phosphatase,Magnesium Dependent Protein Phosphatase 2C beta,PPM1 Magnesium Dependent Protein Phosphatases,Phosphatase 2C, Protein,Phosphatase, PPM1D,Phosphatase, PPM1E,Phosphatase, PPM1G,Phosphatase, Ppm1b,Phosphatase, Ptc2,Phosphatases, PPM1 Protein,Protein Phosphatase 1D Magnesium Dependent, delta isoform,Protein Phosphatases, PPM1,beta, PP2C |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
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