Nucleotide sequence and deduced amino acid sequence of a gene encoding the 23 kDa polypeptide of the oxygen-evolving complex from mustard (Sinapis alba L.)

1990 ◽  
Vol 14 (5) ◽  
pp. 889-890 ◽  
Author(s):  
Thomas Merkle ◽  
Martina Krenz ◽  
Andreas Wenng ◽  
Eberhard Sch�fer
1998 ◽  
Vol 42 (5) ◽  
pp. 1245-1248 ◽  
Author(s):  
François Sanschagrin ◽  
Julien Dufresne ◽  
Roger C. Levesque

ABSTRACT We have determined the nucleotide sequence of the blaSgene encoding the carbapenem-hydrolyzing L-1 β-lactamase fromStenotrophomonas maltophilia GN12873. Analysis of the DNA and deduced amino acid sequences identified a product of 290 amino acids. Comparisons of the L-1 amino acid sequence with those of other zinc β-lactamases showed 88.6% identity with the L-1 enzyme fromS. maltophilia IID1275 and less than 20% identity with other class B metalloenzymes.


Author(s):  
Hoang Thi Thu Yen ◽  
Mai Thi Huyen Trang ◽  
Pham Thi Hang ◽  
Huynh Thi Thu Hue

In this study, we conducted the cloning and sequencing gene encoding FLS from the two green and purple Trung Du tea cultivars. The length of FLS gene is 996 bp, encodes 331 amino acid. Results of FLS gene analysis showed that green and purple Trung Du cultivars has 13 nucleotide variants total as compare with FLS sequence published on Genbank. Nucleotide sequence differences lead to change amino acid sequence of key functional motives in FLS like motif characterizes the 2OG-Fe (II) oxygenase superfamily, the PxxxIRxxx-EQP motif at the N-terminal (18→29) determines the FLS activity, the CPQ/RPxLAL motif) is the binding site of 2-oxoglutarate. How amino acid position changes affect FLS activity need further research. FLS gene isolates are sources for further research to aim elucidating the function of this enzyme.


1989 ◽  
Vol 3 (3) ◽  
pp. 169-174 ◽  
Author(s):  
R. J. Crawford ◽  
V. E. Hammond ◽  
P. J. Roche ◽  
P. D. Johnston ◽  
G. W. Tregear

ABSTRACT The gene encoding rhesus monkey relaxin has been investigated. A cDNA library was prepared using corpus luteal RNA from a pregnant rhesus monkey, cDNA clones encoding relaxin were isolated and the nucleotide sequence was determined. The amino acid sequence of rhesus monkey preprorelaxin, predicted from the cDNA, demonstrates that the sequence has not been strongly conserved when compared with that of man, although features characteristic of the relaxin molecule have been maintained. This structural information will allow production of rhesus monkey relaxin, leading to studies investigating the bioactivity of relaxin in a homologous primate system. Southern blot analysis indicated that there is only one relaxin gene in the rhesus monkey and baboon genomes. In this respect these primate genomes are different from the human genome which contains two relaxin genes.


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