scholarly journals The nucleotide sequence and deduced amino acid sequence of the cytochrome cL gene of Methylobacterium extorquens AM1, a novel class of c-type cytochrome

1988 ◽  
Vol 256 (2) ◽  
pp. 673-676 ◽  
Author(s):  
D N Nunn ◽  
C Anthony
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Methylobacterium Extorquens ◽  
Methylobacterium Extorquens Am1 ◽  
Cytochrome Cl

The nucleotide sequence and deduced amino acid sequence of the cytochrome cL of Methylobacterium extorquens (Pseudomonas AM1; Methylobacterium AM1) shows that this cytochrome c is completely different, except for its haem-binding site, from all other cytochromes.

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.

scholarly journals The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1

1989 ◽  
Vol 260 (3) ◽  
pp. 857-862 ◽  
Author(s):  
D N Nunn ◽  
D Day ◽  
C Anthony
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Methanol Dehydrogenase ◽  
Beta Subunit ◽  
Methylobacterium Extorquens ◽  
Methylobacterium Extorquens Am1 ◽  
Beta 2

The nucleotide and deduced amino acid sequence of a novel small (beta) subunit of methanol dehydrogenase of Methylobacterium extorquens AM1 (previously Pseudomonas AM1) has been determined. Work with the whole protein has shown that is has an alpha 2 beta 2 configuration.

scholarly journals Nucleotide sequence of the melB gene and characteristics of deduced amino acid sequence of the melibiose carrier in Escherichia coli.

1984 ◽  
Vol 259 (7) ◽  
pp. 4320-4326 ◽  
Author(s):  
H Yazyu ◽  
S Shiota-Niiya ◽  
T Shimamoto ◽  
H Kanazawa ◽  
M Futai ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence

scholarly journals The Amino Acid Sequence of Wheat Germ Cytochrome c

1967 ◽  
Vol 242 (11) ◽  
pp. 2764-2779
Author(s):  
Frits C. Stevens ◽  
A.N. Glazer ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Wheat Germ

scholarly journals Terminal deoxynucleotidyltransferase. Alignment of α- and β-subunits of the core enzyme along the primary translation product

1985 ◽  
Vol 227 (3) ◽  
pp. 1003-1007 ◽  
Author(s):  
C M Beach ◽  
S K Chan ◽  
T C Vanaman ◽  
M S Coleman
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Beta Subunits ◽  
Isolation And Purification ◽  
C Terminus ◽  
Human Lymphoblast ◽  
Catalytically Active ◽  
Single Polypeptide ◽  
Dna Nucleotide Sequence

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.

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

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