scholarly journals Nucleotide sequence analysis of the gene encoding the Deinococcus radiodurans surface protein, derived amino acid sequence, and complementary protein chemical studies.

1987 ◽  
Vol 169 (11) ◽  
pp. 5216-5223 ◽  
Author(s):  
J Peters ◽  
M Peters ◽  
F Lottspeich ◽  
W Schäfer ◽  
W Baumeister
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Deinococcus Radiodurans ◽  
Surface Protein ◽  
Nucleotide Sequence Analysis ◽  
Gene Encoding ◽  
Chemical Studies

scholarly journals Cloning and Sequence Analysis of Gene Encoding Flavonol Synthase from Trung Du Teas Growing in Thai Nguyen

2017 ◽  
Vol 33 (4) ◽  
Author(s):  
Hoang Thi Thu Yen ◽  
Mai Thi Huyen Trang ◽  
Pham Thi Hang ◽  
Huynh Thi Thu Hue
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Amino Acid Position ◽  
Gene Analysis ◽  
Cloning And Sequencing ◽  
Gene Encoding ◽  
Flavonol Synthase

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.

Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

2020 ◽  
Vol 85 (3) ◽  
pp. 626-629
Author(s):  
Hisashi Muramatsu ◽  
Hiroki Maguchi ◽  
Taisuke Harada ◽  
Takehiro Kashiwagi ◽  
Chul-Sa Kim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Propionic Acid ◽  
Unknown Function ◽  
Protein Family ◽  
Amino Acid Sequence Analysis ◽  
Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

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