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1 Serratia marcescens, Proteus mirabilis, and Proteus vulgaris).
2 by expressing an L-amino acid deaminase from Proteus vulgaris.
3 nzymes, cABCI and cABCII, were identified in Proteus vulgaris.
4 udomonas aeruginosa, Enterococcus aerogenes, Proteus vulgaris and Enterobacter sakazakii) bacteria, w
5 Two commercial enzymes, chondroitinase ABC (Proteus vulgaris) and chondroitinase ACII (Arthrobacter
6 eas MICs for E. coli, Klebsiella pneumoniae, Proteus vulgaris, and Pseudomonas aeruginosa were > 100
8 Serratia marcescens, Erwinia carotovora, and Proteus vulgaris but not in several nonenteric bacteria.
10 of these enzymes, chondroitinase ABC I from Proteus vulgaris, has the broadest substrate specificity
12 species-specific class A beta-lactamase from Proteus vulgaris K1 was crystallized at pH 6.25 and its
13 oaceticus BD413, Vibrio cholerae El Tor, and Proteus vulgaris K80, were members of a previously descr
15 of the PvuII plasmid pPvu1, originally from Proteus vulgaris, making this the first completely seque
16 erived from either Salmonella typhimurium or Proteus vulgaris, microorganisms that have diverged from
17 ound in the O-polysaccharide of the LPS from Proteus vulgaris OX19 used in the Weil-Felix test, sugge
18 ression of the tryptophanase (tna) operon of Proteus vulgaris, short deletions were introduced in the
19 st Listeria monocytogenes, Escherichia coli, Proteus vulgaris, Staphylococcus aureus, and Candida alb
20 Serratia marcescens, Erwinia carotovora, and Proteus vulgaris, strongly suggesting that the physiolog
22 e solved two x-ray crystal structures of the Proteus vulgaris tetrameric HigB-(HigA)2-HigB TA complex
23 ng of substrates and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and to wild typ
25 scherichia coli, Salmonella typhimurium, and Proteus vulgaris) We also isolated transposition events
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