| D008836 |
Micrococcal Nuclease |
An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1. |
Staphylococcal Nuclease,TNase,Thermonuclease,Thermostable Nuclease,Nuclease, Micrococcal,Nuclease, Staphylococcal,Nuclease, Thermostable |
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| D011506 |
Proteins |
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. |
Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene |
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| D004768 |
Enterotoxins |
Substances that are toxic to the intestinal tract causing vomiting, diarrhea, etc.; most common enterotoxins are produced by bacteria. |
Staphylococcal Enterotoxin,Enterotoxin,Staphylococcal Enterotoxins,Enterotoxin, Staphylococcal,Enterotoxins, Staphylococcal |
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| D001226 |
Aspartate-tRNA Ligase |
An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12. |
Aspartyl T RNA Synthetase,Asp-tRNA Ligase,Aspartyl-tRNA Synthetase,Asp tRNA Ligase,Aspartate tRNA Ligase,Aspartyl tRNA Synthetase,Ligase, Asp-tRNA,Ligase, Aspartate-tRNA,Synthetase, Aspartyl-tRNA |
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| D001427 |
Bacterial Toxins |
Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases. |
Bacterial Toxin,Toxins, Bacterial,Toxin, Bacterial |
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| D013211 |
Staphylococcus aureus |
Potentially pathogenic bacteria found in nasal membranes, skin, hair follicles, and perineum of warm-blooded animals. They may cause a wide range of infections and intoxications. |
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| D017433 |
Protein Structure, Secondary |
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. |
Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein |
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| D017510 |
Protein Folding |
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. |
Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular |
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| D046911 |
Macromolecular Substances |
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. |
Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular |
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| D022622 |
Shiga Toxin 1 |
A toxin produced by certain pathogenic strains of ESCHERICHIA COLI such as ESCHERICHIA COLI O157. It is closely related to SHIGA TOXIN produced by SHIGELLA DYSENTERIAE. |
SLT-I,SLTI,Shiga-Like Toxin I,Stx1 Protein,VT1 Cytotoxin,Vero Cytotoxin VT1,Verocytotoxin 1,Verotoxin I,Protein, Stx1,SLT I,Shiga Like Toxin I |
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