Complete amino acid sequence of yeast thioltransferase (glutaredoxin).
The amino acid sequence of a thioltransferase isolated from Saccharomyces cerevisiae was determined. The protein was cleaved by trypsin, Staphylococcus aureus V8 protease, and cyanogen bromide. The peptides generated were purified by reverse phase HPLC. Sequencing of intact protein and its fragments were achieved by automated Edman degradation. The protein contains 106 amino acid residues with two cysteines. Yeast thioltransferase showed 51% structural similarity to pig liver thioltransferase and 34% to E. coli glutaredoxin.
Department of Biological Chemistry, Merck Sharp & Dohme Research Laboratories, West Point, Pennsylvania 19486.
Z R
ZR
Gan
M A
MA
Polokoff
J W
JW
Jacobs
M K
MK
Sardana
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D054477:Glutaredoxins; D008969:Molecular Sequence Data; D010088:Oxidoreductases; D010446:Peptide Fragments; D010449:Peptide Mapping; D011506:Proteins / Q000235:genetics* / Q000302:isolation & purification; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D054477:Glutaredoxins; D010446:Peptide Fragments; D011506:Proteins; D010088:Oxidoreductases; D003488:Cyanogen Bromide