Bacteria Brevibacterium

Dufosse, L. and de Echanove, C., The last step in the biosynthesis of aryl carotenoids in the cheese ripening bacteria Brevibacterium linens ATCC 9175 (Brevibacterium aurantiacum sp. nov.) involves a cytochrome P450-dependent monooxygenase. Food Res. Int, 38, 967, 2005. 

Efforts to develop organisms that overproduce L-phenylalanine have been vigorously pursued by the Nutrasweet Company, Ajinomoto, Kyowa Hakko Kogyo, and others. The focus has centered on bacterial strains that have previously demonstrated the ability to overproduce other amino acids. Such organisms include principally the coryneform bacteria, Brevibacterium flavum [1,2] and Corynebac-terium glutamicum [3,4] used in L-glutamic acid production. In addition, Escherichia coli has been extensively studied for L-phenylalanine manufacture due to... 

S., and Sano, K. (1985) Construction of novel shuttle vectors and a cosmid vector for the glutamic acid-producing bacteria Brevibacterium lactofermen-tum and Corynebacterium glutamicum. Gene, 39 (2-3), 281-286. 

K Hatakeyama, M Kobayashi, H Yukawa. Analysis of biotin biosynthesis pathway in coryneform bacteria Brevibacterium flavum. Methods Enzymol 279 339-348, 1997. 

Phenylethanol production is very strain-specific [65] and has been rarely observed in bacteria (Brevibacterium linens. Microbacterium sp.), while it is much more common in fungi. The best producers are doubtlessly the yeasts Kluyveromyces marxianus [66, 67] and Saccharomyces cerevisiae [68], but lower yields have been obtained with many strains, such as K. lactis [69], Pichia fermentans [70, 71], and P. (formerly//a/ise/i /a) anomala [72]. 

A different system for the enzymatic production of L-aspartate was proposed and used by Mitsubishi Petrochemical Co. in Japan in 1985. In this system, resting intact coryneform bacteria, Brevibacterium flavum, were used without immobilization in a reactor with an ultrafiltration membrane (Terasawa et al. 1985). The starting material, maleate, was converted to fumarate... 

The oxidation of cholesterol to cholest-4-ene-3-one is carried ont by an oxidase in several bacteria. This activity has been fonnd in Brevibacterium sterolicum and Streptomyces sp. strain SA-COO (Ohta et al. 1991), and the extracellnlar enzyme that has been purified from Pseudomonas sp. strain ST-200 (Donkyn and Aono 1998) has a preference for 3p-hydroxy componnds. 

The removal of Pb by Brevibacterium sp strain PBZ was markedly enhanced by the presence of glucose (Simine et al. 1998). Desorption of the metal by EDTA restored the binding capacity of the cells. U(VI) could be desorped from the cell surface of B. cereus by citric acid or sodium bicarbonate with the formation of water-soluble complexes although U(VI) was strongly bound on the cell surface of the bacteria. However, uranyl in... 

In surface smear-ripened cheeses, e.g. Munster, Limburger, Tilsit, Trapist, the surface of the cheese is colonized first by yeasts which catabolize lactic acid, causing the pH to increase, and then by Brevibacterium linens, the characteristic micro-organism of the surface smear but which does not grow below pH 5.8, and various other micro-organisms, including Micrococcus, Arthrobacter and coryneform bacteria. 

Bacteria reported to metabolize PAHs include species of Acido-vorax, Acinetobacter, Actinomyces, Aeromonas, Agrobacterium, Alcaligenes, Arthrobacter, Aureobacterium, Bacillus, Brevibacterium, Burkholderia, Chryseobacterium, Comamonas, Corynebacterium, Cycloclasticus,... 

L-aspartic acid ammonia lyase, or aspartase (E.C. 4.3.1.1) is used on a commercial scale by Kyowa Hakko, Mitsubishi, Tanabe and DSM to produce L-aspartic acid, which is used as a building block for the sweetener Aspartame, as a general acidulant and as a chiral building block for synthesis of active ingrediants[1]. The reaction is performed with enzyme preparations from E. coli, Brevibacterium jlavum or other coryneform bacteria either as permeabilized whole cells or as isolated, immobilized enzymes. The process is carried out under an excess of ammonia to drive the reaction equilibrium from fumaric acid (1) in the direction of L-aspartic acid (l-2) (see Scheme 12.6-1) and results in a product of excellent quality (over 99.9% e.e.) at a yield of practically 100%. The process is carried out on a multi-thousand ton scale by the diverse producers of L-aspartic acid. Site directed mutagenesis of aspartase from E. coli by introduction of a Cys430Trp mutation has resulted in significant activation and stabilization of the enzyme P1. 

L-Lysine is produced by some mutants induced from wild strain of glutamate-producing bacteria including Corynebacterium glutamicum, Brevibacterium lactofermentum, and B. flavum in the presence of high concentrations of sugar and ammonium ions at neutral pH and under aerobic condition [2]. 

L-Threonine is produced by some auxotrophic mutants and/or threonine-analog resistant mutants and those bred by gene engineering techniques. The bacteria are Escherichia coli, Corynebacterium glutamicum, Brevibacterium lactofermentum, B.flavum, Serratia marcescens, and Proteus retgerii. 

The third class of reductases apparently requires manganese for activity, although few other characterizations have been performed. This enzymic activity is found solely in bacteria, specifically in Brevibacterium ammoniagenes, Ar-throbacter, Micrococcus luteus, and Nocardia opaca (37, 38). 

MGL catalyzes the o ,7-elimination reaction of methionine to a-ketobutyrate, methanethiol, and ammonia. MGL has been isolated from a number of bacteria, including Pseudomonas putida, Aeromonas sp., Clostridium sporogenes, P. taetrolens, and Brevibacterium linens, from the primitive protozoa Entamoeba histolytica and Trichomonas vaginalis, but is not believed to be present in yeast, plants, or mammals. " " Two MGL isoforms have been isolated from T. vaginali and Entamoeba histolytica, which differ in substrate specificity, overall charge, and catalytic properties. They show a high degree of sequence identity to MGL from Pseudomonas putida. MGL has demonstrated antitumor efficacy in a number of methionine-dependent cancer cell lines. ... 

The need for divalent manganese in cell proliferation of certain gram-positive bacteria has long been known but its involvement in ribonucleotide reduction was recognized only recently. Strains like Brevibacterium ammoniagenes or Micrococcus luteus cease to synthesize DNA (but not RNA or protein) in manganese-free fermentation... 

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