Amino acid decarboxylases bacterial

A group of enzymes which may be employed in the measurement of L amino acids are the L-amino acid decarboxylases (EC 4.1.1) of bacterial origin, many of which are substrate specific. They catalyse reactions of the type ... 

Gale, E. (1946). The bacterial amino acid decarboxylases, Adv. Enzymol. Relat. Subjects... 

Amino Acids, Determination by Use of Bacterial Amino Acid Decarboxylases... 

Bacterial Amino Acid Decarboxylases in Determination of Amino Adds (Gale). 4... 

Studies on Bacterial Amino-acid Decarboxylases. 5. The Use of Specific... 

Bacterial histidine decarboxylase (EC 4.1.1.22) is unique among bacterial amino acid decarboxylases in not requiring PEP. Mammalian histidine decarboxylase does have a PEP requirement. Battersby et al. (298, 299)... 

Fish muscle can support formation of a wide variety of amine compounds resulting from the direct enzymatic decarboxylation of amino acids. The substrate for the decarboxylase enzymes are free amino acids, therefore amine build-up normally occurs during a decomposition or spoilage process involving formation of free amino acids through proteolysis together with bacterial production and action of an amino acid decarboxylase (Eitenmiller... 

Gale, E. F. and Epps, H. M. R., Studies on bacterial amino-acid decarboxylases ... 

Bacterial Amino Acid Decarboxylases. Tyrosine decarboxylase was used extensively in studies on the nature of the amino acid decarboxylases. This activity is found in several microorganisms and the enzyme was purified over 100-fold from S. faecalis. It is easily resolved, and the apoenzyme has been used to assay pyridoxal phosphate (PALPO). Final concentrations of PALPO between 10 M and 10 M are conveniently measured by the rate of CO2 liberation from tyrosine. Phenylalanine is decarboxylated by this or a similar enzyme. Tyrosine decarboxylase and all of the other amino acid decarboxylases described in this section act only on the L-isomers of their respective substrates. 

L-Lysine is produced in some organisms by decarboxylation of meso-diaminopimelic acid. This enzyme has a pH optimum over 7, in contrast with the acidic pH optima of the other bacterial amino acid decarboxylases. It is extremely specific it does not attack higher or lower homologs, or compounds in which the methylene carbons bear a methyl or hydroxyl group. This has also been shown to be a PALPO-requiring enzyme. 

Formation of Sebiff s bases is also postulated in the ease of decaibo lation at keto acids by amino compounds (Langenbeek s artificial carboxylases). Recently bacterial amino acid decarboxylases have also been shown to contain an active carbonyl in their prosthetic component—phosphorylated pyridoxal (84).i... 

Gale, Ernest F., The Bacterial Amino Acid Decarboxylases. VI 1... 

The principal pathways for the biogenesis and metabolism of histamine are well known. Histamine is formed by decarboxylation of the amino acid, L-histidine, a reaction catalyzed by the enzyme, histidine decarboxylase. This decarboxylase is found in both mammalian and non-mammalian species. The mammalian enzyme requires pyridoxal phosphate as a cofactor. The bacterial enzyme has a different pH optimum and utilizes pyruvate as a cofactor (26.27). 

Amine build-up in fish muscle usually results from decarboxylation of amino acids in the muscle by enzymes of bacterial origin. This review will present information on the activity of bacterial decarboxylases and the formation of amines in fish. Mechanisms of decarboxylase action and production of bacterial decarboxylases in fish muscle are discussed. Emphasis is placed upon studies dealing with formation of histidine decarboxylase and histamine. Histamine, because of its involvement in Scombroid food poisoning, has been extensively studied with regard to its formation in fish and fishery products. 

Table I. Historical Perspective on Bacterial Decarboxylases Amino Acid...

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