| 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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| D005798 |
Genes, Bacterial |
The functional hereditary units of BACTERIA. |
Bacterial Gene,Bacterial Genes,Gene, Bacterial |
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| 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 |
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| D005970 |
Glutamate Synthase |
An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13. |
Glutamine Ketoglutarate Amidotransferase,Ketoglutarate Glutamine Amidotransferase,Amidotransferase, Glutamine Ketoglutarate,Amidotransferase, Ketoglutarate Glutamine,Glutamine Amidotransferase, Ketoglutarate,Ketoglutarate Amidotransferase, Glutamine,Synthase, Glutamate |
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| D006715 |
Homoserine Dehydrogenase |
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, Homoserine |
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| D000596 |
Amino Acids |
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. |
Amino Acid,Acid, Amino,Acids, Amino |
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| D001222 |
Aspartate Kinase |
An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4. |
Aspartokinase,Aspartate Kinase I,Aspartate Kinase II,Aspartate Kinase III,Aspartyl Kinase,Kinase I, Aspartate,Kinase II, Aspartate,Kinase III, Aspartate,Kinase, Aspartate,Kinase, Aspartyl |
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| D013912 |
Threonine |
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins. |
L-Threonine,L Threonine |
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| D014161 |
Transduction, Genetic |
The transfer of bacterial DNA by phages from an infected bacterium to another bacterium. This also refers to the transfer of genes into eukaryotic cells by viruses. This naturally occurring process is routinely employed as a GENE TRANSFER TECHNIQUE. |
Genetic Transduction,Genetic Transductions,Transductions, Genetic |
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