Escherichia coli specificity

R. T. The DegP and DegQ periplasmic endoproteases of Escherichia coli Specificity for cleavage sites and substrate conformation./. Bacterid. 1996, 178, 5925-5929. 

Berkower, I., Leis, J., and Hurwitz, J. (1973) Isolation and characterization of an endonuclease from Escherichia coli specific for ribonucleic acid in ribonucleic acid deoxyribonucleic acid hybrid structures J Biol C/iem. 248,5914-5921... 

Patching SG, Baldwin SA, Baldwin AD, Young JD, Gallagher MP, Henderson PJ, Herbert RB. The nucleoside transport proteins, NupC and NupG, from Escherichia coli specific structural motifs necessary for the binding of ligands. Org. Biomol Chem. 2005 3 462 70. 

Specific bacteriostatic activity against Escherichia coli (681, 896, 899), Staphylococcus aureus (681, 896), Cocci (900), Shigella dysenteriae (681), Salmonella ryphi (681), Proteus vulgaris (681), Pseudomonas aeruginosa (681), Streptococcus (889, 901, 902) and Pneumococcus (901-904). 

Enzyme preparations from liver or microbial sources were reported to show rather high substrate specificity [76] for the natural phosphorylated acceptor d-(18) but, at much reduced reaction rates, offer a rather broad substrate tolerance for polar, short-chain aldehydes [77-79]. Simple aliphatic or aromatic aldehydes are not converted. Therefore, the aldolase from Escherichia coli has been mutated for improved acceptance of nonphosphorylated and enantiomeric substrates toward facilitated enzymatic syntheses ofboth d- and t-sugars [80,81]. High stereoselectivity of the wild-type enzyme has been utilized in the preparation of compounds (23) / (24) and in a two-step enzymatic synthesis of (22), the N-terminal amino acid portion of nikkomycin antibiotics (Figure 10.12) [82]. 

Azam, T., Ishihama, A. Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. The Journal of Biological Chemistry, Vol.274, No.46, (November 1999), pp. 33105-33113, ISSN 0021-9258... 

A number of allergens from both honey bee and vespid venoms have been cloned and expressed by either Escherichia coli or baculovirus-infected insect cells (table 1) phospholipase Aj [20], hyaluronidase [21], acid phosphatase [13] and Api m6 [14] from honey bee venom, as well as antigen 5 [22], phospholipase A and hyaluronidase [23] from vespid venom, and dipeptidylpeptidases from both bee and Vespula venoms [15, 16]. Their reactivity with human-specific IgE antibodies to the respective allergens has been documented [11-16, 22, 23] and their specificity is superior... 

Restriction enzymes are named after the bacterium from which they are isolated. For example, EcoRI is from Escherichia coli, and BamEII is from Bacillus amyloliquefaciens (Table 40-2). The first three letters in the restriction enzyme name consist of the first letter of the genus (E) and the first two letters of the species (co). These may be followed by a strain designation (R) and a roman numeral (I) to indicate the order of discov-ery (eg, EcoRI, EcoRIE). Each enzyme recognizes and cleaves a specific double-stranded DNA sequence that is 4—7 bp long. These DNA cuts result in blunt ends (eg,... 

Resistance to phagocytosis is sometimes associated with specific components of the cell wall and/or with the presence of capsules surrounding the cell wall. Classic examples of these are the M-proteins of the streptococci and the polysaccharide capsules of pneumococci. The acidic polysaccharide K-antigens of Escherichia coli and Sal typhi behave similarly, in that (i) they can mediate attachment to the intestinal epithelial cells, and (ii) they render phagocytosis more difficult. Generally, possession of an extracellular capsule will reduce the likelihood of phagocytosis. 

In addition to phosphotriesterase from P. diminuta (PTE) discussed above, two other types of enzymes were found to exhibit phosphotriesterase activity. Interestingly, both are peptidases - the enzymes which in nature hydrolyse a peptide bond. The first one - organophosphorus acid anhydrolase (OPAA) from Alteromonas sp. JD6.5 - is a proline dipeptidase its original activity is to cleave a dipepfide bond with a prolyl residue at the carboxy terminus. The second one - aminopeptidase P (AMPP) from Escherichia coli - is a proline-specific peptidase that catalyses hydrolysis of N-terminal peptide bonds containing a proline residue. ° ... 

Wan J, TK Tokunaga, E Brodie, Z Wang, Z Zheng, D Herman, TC Hazen, MK Firestone, SR Sutton (2005) Reoxidation of bioreduced uranium under reducing conditions. Environ Sci Technol 39 6162-6169. Weiner JH, DP Macisaac, RE Bishop, PT Bilous (1988) Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity J Bacterial 170 1505-1510. 

Stalker DM, KE McBride (1987) Cloning and expresssion in Escherichia coli of a Klebsiella ozaenae plasmid-borne gene encoding a nitrilase specific for the herbicide Bromoxynil. J Bacterial 169 ... 

All earlier studies [155-158] reported the complexation of berberine with calf thymus DNA and suggested by a mechanism of intercalation. Maiti and coworkers [159-162] demonstrated first the base- and sequence-specificity of berberine from studies with several naturally occurring DNAs (Clostridium perfringenes, cholera bacteriophage 02, calf thymus, Escherichia coli, Micrococcus lysodeikticus) and synthetic DNAs ((poly(dG-dC) poly(dG-dC), poly(dG)-poly(dC), poly(dA-dT) poly(dA-dT), poly(dA)-poly(dT)) using various physicochemical techniques. Several aspects of the interaction were reported ... 

High-specific activity D-P- H] panthothenic acid (Figure 10.8) was prepared from commercially available p-[3-3H]alanine using Escherichia coli strain DVl, which converted 85 to 90% of the input p-[3-3H]alanine to extracellular D-[3- H]panthoth-enate under appropriate growth conditions. The radiolabeled vitamin was purified... 

Allwood, P. B., Malik, Y. S., Maherchandani, S., Vought, K., Johnson, L. A., Braymen, C., Hedberg, C. W., and Goyal, S. M. (2004). Occurrence of Escherichia coli, noroviruses, and F-specific coliphages in fresh market-ready produce. /. Food Prot. 67, 2387-2390. 

Z. Banfalvi and A. Kondorosi, Production of root hair deformation factors by Rhizohium meliloti nodulation genes in Escherichia coli H.mD (NocM) is involved in the plant host-specific modification of the NodABS-factor. Plant Mol. Biol. 13 1 (1989). 

Regnault, B. Martin-Delautre, S. Lejay-Collin, M. Lefevre, M. Grimont, P. A. D. Oligonucleotide probe for the visualization of Escherichia coli Escherichia fergu-sonii cells by in situ hybridization Specificity and potential applications. Res. Microbiol. 2000,151,521-533. 

Kusunoki, H. Latiful Bari, M. Kita,T. Sugii, S. Uemura,T. Flow cytometry for the detection of enterohaemorrhagic Escherichia coli 0157 H7 with latex beads sensitized with specific antibody. J. Vet. Med. 2000,47,551-559. 

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