COOH-terminal Amino Acid Sequence of Histidinol Dehydrogenase from a Salmonella typhimurium Mutant
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چکیده
منابع مشابه
COOH-terminal amino acid sequence of histidinol dehydrogenase from a Salmonella typhimurium mutant.
histidinol dehydrogenase. The wild type sequence, Arg ( > Lys Glu-Gln-Ala, has been replaced by the sequence -Lys-AlaSer-Leu-Thr in the hisD2352 dehydrogenase. The permuted amino acid sequence may be explained if hisD2352 is a two-base deletion near the end of the hisD gene. A unique nucleotide sequence may be written for this region which indicates that the normal termination signal of the his...
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The biosynthesis of histidine, studied in most complete detail in Salmonella typhimurium with both genetic and biochemical techniques, has been reviewed recently (I, 2). The final step in this pathway, oxidation of the amino alcohol, histidinol, to histidine, was first described enzymatically in an Arthrobacter species and Escherichia coli (3)) and in yeast (4). Two oxidation steps are involved...
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The amino acid sequence of ATP phosphoribosyltransferase [1-(5'-phosphoribosyl)-ATP:pyrophosphate phosphoribosyltransferase, EC 2.4.2.17] of Salmonella typhimurium has been determined. The amino acid sequence analysis was carried out with a combination of manual and automated methods. It was complemented by DNA sequence analysis (done in another laboratory) of the hisG gene, which codes for it....
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The amino acid sequence of the unique COOH-terminal region of the beta subunit of human choriogonadotropin has been reinvestigated. The desialylated subunit was digested with thermolysin and a 27-residue peptide from positions 115 through 141 isolated in a high yield. Quantitative Edman sequence degradation of this peptide, of another peptide produced by thermolysin digestion containing residue...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44744-3