Nucleotide sequence and characteristics of the gene for l-lactate dehydrogenase of Thermus caldophilus GK24 and the deduced amino-acid sequence of the enzyme

1986 ◽  
Vol 160 (2) ◽  
pp. 433-440 ◽  
Author(s):  
Kenji KUNAI ◽  
Masayuki MACHIDA ◽  
Hiroshi MATSUZAWA ◽  
Takahisa OHTA
Keyword(s):  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Thermus Caldophilus

scholarly journals Amino acid sequence of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene

1987 ◽  
Vol 165 (3) ◽  
pp. 581-586 ◽  
Author(s):  
David A. BARSTOW ◽  
Jonathan P. MURPHY ◽  
Andy F. SHARMAN ◽  
Anthony R. CLARKE ◽  
J. John HOLBROOK ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Cloned Gene

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 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.

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