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Arthrobacter globiformis

An extracellular inulin fructotransferase that results in the formation of a-D-Fru/-1,2 2,1 -(3-D-Fru/ [difructose anhydride I (5)] has been purified from Arthrobacter globiformis S14-3,65,66 from Arthrobacter sp. MCI-249367 and from Streptomyces sp. MCI-2524.68... [Pg.215]

Boldt YR, Ml Sadowsky, LBM Ellis, L Que, LP Wackett (1995) A manganese-dependent dioxygenase from Arthrobacter globiformis CM-2 belongs to the major extradiol dioxygenase family. J Bacterial 177 1225-1232. [Pg.136]

Recently novel methods were reported to make (lR)-trans-chrysanthemic acid including optical resolutions with the (+)-3-caranediol or l,l -binaphthol monoethylether, enzymatic resolution with Arthrobacter globiformis and the asymmetric synthesis with a new Cu catalyst. These methods are reviewed in this section. [Pg.34]

In contrast to the substantial work with MAO, relatively little research has been reported on the mechanism of inhibition of copper-containing amine oxidases and SSAO by cyclopropylamines. Bovine plasma amine oxidase, equine plasma amine oxidase, Escherichia coii amine oxidase, and Arthrobacter globiformis amine oxidase were inhibited by frans-2-phenylcyclopropylamine (8a) and the mode of inhibition was shown by spectral and crystal structure analyses to be competitive and reversible [36,37,129],... [Pg.683]

Hasegawa, S. Bennett, R. D. Maier, V. P. King, A. D., Jr. Limonoate dehydrogenase from Arthrobacter globiformis. [Pg.165]

Hasegawa, S. Brewster, L. C. Maier, V. P. Use of limonoate dehydrogenase of Arthrobacter globiformis for the prevention or removal of limonin bitterness in citrus products. J. Food Sci., 1973, 38, 1153-1155. [Pg.165]

Nishizawa M, Shimizu M et al (1995) Stereoselective production of (+)-tram-chrysanthemic acid by a microbial esterase cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli. Appl Environ Microbiol 61 3208-3215... [Pg.38]

Nishizawa M, Gomi H et al (1993) Purification and some properties of carboxylesterase from Arthrobacter globiformis, stereoselective hydrolysis of ethyl chrysanthemate. Biosci Biotech Biochem 57 594-598... [Pg.38]

Shepard E. M. Dooley D. M. Intramolecular electron transfer rate between active-site copper and TPQ in Arthrobacter globiformis amine oxidase. J. Biol. Inorg. Chem. 2006, 11, 1039-1048. [Pg.456]

Mukai, K., Watanabe, H., Kubota, M., Chaen, H., Fukuda, S., and Kurimoto, M. 2006. Purification, characterization and gene cloning of a novel maltosyltransferase from an Arthrobacter globiformis strain that produces an alternating a-1,4- and -1,6-cyclic tetrasaccharide from starch. Appl. Environ. Microbiol., 72,1065-1071. [Pg.317]

Tanizawa, K., Matsuzaki, R., Shimizu, E., Yorifuji, T., and Fukui, T., 1994, Cloning and sequencing of phenylethylamine oxidase from Arthrobacter globiformis and implication of Tyr 382 as the precursor to its covalently bound quinone cofactor, Biochem. Biophys. Res. Commun. 199 1096nll02. [Pg.230]

Wilce, M. C. J-, Dooley, D. M., Freeman, H. C., Guss, J. M., Matsunami, H., Mclntire, W. S., Ruggiero, C. E., Tanizawa, K., and Yamaguchi, H., 1997, Crystal shnctiwes of die copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms. Biochemistry, 36 16116fil6133. [Pg.231]

Dihydroxyphenylacetate-2/3-dioxygenase from Arthrobacter globiformis (Boldt et al. 1995) and from Bacillus brevis (Que et al. 1981) is an Mn(II) enzyme, and is neither activated by Fe(II) nor rapidly inhibited by FI2O2. [Pg.305]

Biological Removal Six species of bacteria, each capable of metabolizing limonoids, have been isolated from soil by enrichment using limonoids as carbon sources. They are Arthrobacter globiformis (34), Pseudomonas 321-18 (35), Arthrobacter globiformis II (36), Bacterium 342-152-1, Corynebacterium fasclans (37) and Aclnetobacter sp. (38). Based on the metabolites and enzymes produced by these species of bacteria, five metabolic pathways of limonoids have been established in bacteria (3)(Fig. 4). [Pg.91]


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