scholarly journals New TEM Variant (TEM-92) Produced by Proteus mirabilis and Providencia stuartiiIsolates

2001 ◽  
Vol 45 (4) ◽  
pp. 1278-1280 ◽  
Author(s):  
Christophe de Champs ◽  
Claire Monne ◽  
Richard Bonnet ◽  
Wladimir Sougakoff ◽  
Danielle Sirot ◽  
...  

ABSTRACT The sequences of the bla TEM genes encoding TEM-92 in Proteus mirabilis and Providencia stuartii isolates were determined and were found to be identical. Except for positions 218 (Lys-6) and 512 (Lys-104), the nucleotide sequence of bla TEM-92 was identical to that ofbla TEM-20, including the sequence of the promoter region harboring a 135-bp deletion combined with a G-162→T substitution. The deduced amino acid sequence of TEM-92 differed from that of TEM-52 by the presence of a substitution (Gln-6→Lys) in the peptide signal.

1999 ◽  
Vol 43 (12) ◽  
pp. 2960-2963 ◽  
Author(s):  
Patricia A. Bradford

ABSTRACT Genes encoding SHV-1 and SHV-2 were sequenced by different methods. Nucleotide sequencing of the coding strand by standard dideoxy-chain termination methods resulted in errors in the interpretation of the nucleotide sequence and the derived amino acid sequence in two main regions which corresponded to nucleotide and amino acid changes that had been reported previously. The automated thermal cycling method was clearly superior and consistently resulted in the correct sequences for these genes.


2000 ◽  
Vol 44 (4) ◽  
pp. 1070-1074 ◽  
Author(s):  
Daniele Choury ◽  
Marie-France Szajnert ◽  
Marie-Laure Joly-Guillou ◽  
Kemal Azibi ◽  
Marc Delpech ◽  
...  

ABSTRACT We determined the nucleotide sequence of the bla gene for the Acinetobacter calcoaceticus β-lactamase previously described as CARB-5. Alignment of the deduced amino acid sequence with those of known β-lactamases revealed that CARB-5 possesses an RTG triad in box VII, as described for the Proteus mirabilis GN79 enzyme, instead of the RSG consensus characteristic of the other carbenicillinases. Phylogenetic studies showed that these RTG enzymes constitute a new, separate group, possibly ancestors of the carbenicillinase family.


1984 ◽  
Vol 259 (7) ◽  
pp. 4320-4326 ◽  
Author(s):  
H Yazyu ◽  
S Shiota-Niiya ◽  
T Shimamoto ◽  
H Kanazawa ◽  
M Futai ◽  
...  

1985 ◽  
Vol 227 (3) ◽  
pp. 1003-1007 ◽  
Author(s):  
C M Beach ◽  
S K Chan ◽  
T C Vanaman ◽  
M S Coleman

Terminal deoxynucleotidyltransferase exists in multiple Mr forms, all apparently generated from a single polypeptide of 62kDa. On isolation and purification, the smallest catalytically active protein of this enzyme consists of two subunits, alpha (12kDa) and beta (30kDa). Recently a complementary-DNA nucleotide sequence has been reported for a portion of the enzyme from human lymphoblast. We have pinpointed the locations of the alpha- and beta-subunits within the elucidated nucleotide sequence. From these data, the portions of the nucleotide sequence coding for the catalytically important area of the transferase can be estimated. Here the amino acid sequence of a number of tryptic peptides from calf alpha- and beta-subunits is presented. Because of the striking homology between the amino acid sequence of the calf enzyme and that predicted for human lymphoblast enzyme, it is possible for us to conclude that the alpha-subunit was generated from the C-terminus of the precursor protein and the beta-subunit was non-overlapping and proximal.


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