| 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 |
|
| D010088 |
Oxidoreductases |
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,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase |
|
| D010396 |
Penicillamine |
3-Mercapto-D-valine. The most characteristic degradation product of the penicillin antibiotics. It is used as an antirheumatic and as a chelating agent in Wilson's disease. |
Dimethylcysteine,Mercaptovaline,beta,beta-Dimethylcysteine,Copper Penicillaminate,Cuprenil,Cuprimine,D-3-Mercaptovaline,D-Penicillamine,Metalcaptase,D 3 Mercaptovaline,D Penicillamine,Penicillaminate, Copper,beta,beta Dimethylcysteine |
|
| D010957 |
Plasmids |
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS. |
Episomes,Episome,Plasmid |
|
| D011490 |
Protein Disulfide Reductase (Glutathione) |
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2. |
Glutathione Insulin Transhydrogenase,Glutathione Protein Disulfide Oxidoreductase,Thiol-Disulfide Oxidoreductase,Thiol-Protein Disulfide Oxidoreductase,Disulfide Oxidoreductase, Thiol-Protein,Insulin Transhydrogenase, Glutathione,Oxidoreductase, Thiol-Disulfide,Oxidoreductase, Thiol-Protein Disulfide,Thiol Disulfide Oxidoreductase,Thiol Protein Disulfide Oxidoreductase,Transhydrogenase, Glutathione Insulin |
|
| D002712 |
Chlorides |
Inorganic compounds derived from hydrochloric acid that contain the Cl- ion. |
Chloride,Chloride Ion Level,Ion Level, Chloride,Level, Chloride Ion |
|
| D005696 |
Galactosidases |
A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-. |
Galactosidase |
|
| 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 |
|
| D001483 |
Base Sequence |
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. |
DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA |
|
| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
|