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1  MSH was not found in representatives of the Arthrobacter, Agromyces, or Actinomyces genera.
2 he broad-specificity triazine hydrolase from Arthrobacter and Nocardioides spp., is reportedly in the
3 enzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains
4 n isotope effects in atrazine degradation by Arthrobacter aurescens TC1 (i) delivered highly characte
5 teny to the Arthrobacter sp. strain FB24 and Arthrobacter aurescens TC1 genomes, but it is approximat
6  (Proteus vulgaris) and chondroitinase ACII (Arthrobacter aurescens), having action patterns previous
7                                           An Arthrobacter beta-galactosidase has homology with the ly
8                Four isolates from the genera Arthrobacter, Brevibacterium, and Microbacterium, which
9             All the above data suggests that Arthrobacter can be considered as an excellent PGP rhizo
10 NA amplicon sequencing showed that the genus Arthrobacter comprised more than 21% of the total commun
11 it is approximately 1.9 Mb smaller than both Arthrobacter genomes and has a lower G+C content, sugges
12 is reaction in phenylethylamine oxidase from Arthrobacter globiformis (AGAO) has been determined.
13 he activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values betwee
14 ses from Brevibacterium fuscum (Fe-HPCD) and Arthrobacter globiformis (Mn-MndD) that share high seque
15 O), human kidney diamine oxidase (KDAO), and Arthrobacter globiformis amine oxidase (AGAO) to examine
16 ver reoxidation by O(2) of substrate-reduced Arthrobacter globiformis amine oxidase (AGAO) under a wi
17 binant human kidney diamine oxidase (rhDAO), Arthrobacter globiformis amine oxidase (AGAO), and Pichi
18 e (EPAO), pea seedling amine oxidase (PSAO), Arthrobacter globiformis amine oxidase (AGAO), Escherich
19 otocatechuate 2,3-dioxygenases isolated from Arthrobacter globiformis and Brevibacterium fuscum have
20 ined their toxicity toward the soil bacteria Arthrobacter globiformis and the Collembola Folsomia can
21 rated a lysine residue in the active site of Arthrobacter globiformis CAO (AGAO) by site-directed mut
22 oxyphenylacetate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2 is dependent on manganese
23 ication for apophenylethylamine oxidase from Arthrobacter globiformis has been developed, which avoid
24 mber of mutant forms of choline oxidase from Arthrobacter globiformis have recently been carried out,
25 4-dihydroxyphenylactate 2,3-dioxygenase from Arthrobacter globiformis strain CM-2 (MndD) cloned in Es
26 xidase (DMGO) is a covalent flavoenzyme from Arthrobacter globiformis that catalyzes the oxidative de
27 hylglycine oxidase (DMGO) from the bacterium Arthrobacter globiformis, a bifunctional enzyme that cat
28 is the flavin-dependent choline oxidase from Arthrobacter globiformis, for which structural, mechanis
29 d for wild-type HPAO, the amine oxidase from Arthrobacter globiformis, pea seedling amine oxidase at
30  TPQ in phenylethylamine oxidase (PEAO) from Arthrobacter globiformis, we have identified the C=O str
31 er) with a chloroplast-targeted codA gene of Arthrobacter globiformis, which encodes choline oxidase
32 functional dimethylglycine oxidase (DMGO) of Arthrobacter globiformis.
33 ne oxidase (PEAO) and histamine oxidase from Arthrobacter globiformis.
34 benzoates) were converted by phthalate-grown Arthrobacter keyseri (formerly Micrococcus sp.) 12B to t
35 erse bacterial hosts, including Escherichia, Arthrobacter, Mycobacterium, Rhodobacter, Staphylococcus
36 with sialidase from Clostridium perfringens, Arthrobacter neurofaciens, or Streptococcus, but not Vib
37 y-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus Ru61a and 1-H-3-hydroxy-4
38  the endo-beta-N-acetylglucosaminidases from Arthrobacter protophormiae (Endo-A) and Mucor hiemalis (
39   The endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) is of particular int
40                              The enzyme from Arthrobacter protophormiae (Endo-A) was found to be rema
41 f the endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) with synthetic sugar
42 22G/H130Y/D36A/E263Q) of wild-type NylC from Arthrobacter sp. (plasmid pOAD2-encoding enzyme), with a
43         Studies with sarcosine oxidases from Arthrobacter sp. and Pseudomonas sp. show that these het
44 arbamoylsarcosine amidohydrolase (CSHase) of Arthrobacter sp. and YcaC of Escherichia coli, a protein
45 to convert the D-selective hydantoinase from Arthrobacter sp. DSM 9771 into an L-selective enzyme and
46 illus spharericus JS905, Pseudomonas sp. 1A, Arthrobacter sp. JS443, Pseudomonas putida B2) in the pH
47 zoyl-coenzyme A (4-HB-CoA) thioesterase from Arthrobacter sp. strain AU catalyzes the hydrolysis of 4
48 enome has extended regions of synteny to the Arthrobacter sp. strain FB24 and Arthrobacter aurescens
49 es of a p-nitrophenol catabolic pathway from Arthrobacter sp. strain JS443, was cloned and sequenced.
50 oyl-coenzyme A (4-HBA-CoA) thioesterase from Arthrobacter sp. strain SU in the millisecond time domai
51 f the 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU.
52 hat it was phylogenetically related to other Arthrobacter species.
53 taphylococcus warneri, Flectobacillus major, Arthrobacter stackebrantii, and Flavobacterium sp. and t
54           Our results indicate that isolated Arthrobacter strains present a very high genetic diversi
55                                           55 Arthrobacter strains were isolated and characterized usi
56 brosis patients, with P. aeruginosa and with Arthrobacter, suggesting that formation of hydroxylated
57 piratory activity of carbonate-precipitating Arthrobacter sulfonivorans , isolated from the recently
58                                       In the Arthrobacter thioesterase, each of the four active sites
59 rs that Glu73 is the active site base in the Arthrobacter thioesterase.
60  was reversed by treatment of the cells with Arthrobacter ureafaciens sialidase, indicating that sial
61 stion studies, treatment with sialidase from Arthrobacter ureafaciens--which hydrolyzed mucin-associa

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