Biomaterial Database

[Aromatic amino acid metabolism in Enterobacteriaceae microorganisms]. 1978

Iu V Galaev, and E I Pimenova

The authors revealed phenylalanine deaminase (PAD) in the majority of the Citrobacter strains investigated; the activity of PAD varied within a rather considerable range (0.3--4.58 micrometer of phenylpiruvate in 1 hr per 1 mg of bacterial protein). The presence of this enzyme thus served as an auxiliary biochemical test characterising this group of conditionally pathogenic microbes of the Enterobacteriacea family. Tyrosine decarboxylase was absent in 26 of 50 strains of Citrobacter examined. In the rest of the strains the activity of this enzyme was low. Consequently, tyrosine decarboxylase could not be used for identification of microorganisms of the Citrobacter genus.

UI	MeSH Term	Description	Entries
D010649	Phenylalanine	An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.	Endorphenyl,L-Phenylalanine,Phenylalanine, L-Isomer,L-Isomer Phenylalanine,Phenylalanine, L Isomer
D002954	Citrobacter	A genus of gram-negative, rod-shaped enterobacteria that can use citrate as the sole source of carbon.
D004755	Enterobacteriaceae	A family of gram-negative, facultatively anaerobic, rod-shaped bacteria that do not form endospores. Its organisms are distributed worldwide with some being saprophytes and others being plant and animal parasites. Many species are of considerable economic importance due to their pathogenic effects on agriculture and livestock.	Coliform Bacilli,Enterobacteria,Ewingella,Leclercia,Paracolobactrum,Sodalis
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
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
D000594	Amino Acid Oxidoreductases	A class of enzymes that catalyze oxidation-reduction reactions of amino acids.	Acid Oxidoreductases, Amino,Oxidoreductases, Amino Acid
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
D012475	Salmonella	A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that utilizes citrate as a sole carbon source. It is pathogenic for humans, causing enteric fevers, gastroenteritis, and bacteremia. Food poisoning is the most common clinical manifestation. Organisms within this genus are separated on the basis of antigenic characteristics, sugar fermentation patterns, and bacteriophage susceptibility.
D014445	Tyrosine Decarboxylase	A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC 4.1.1.25.	Decarboxylase, Tyrosine