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Radiation chemical evidence for differences in the amino acid composition of yeast and horse liver alcohol dehydrogenases



Radiation chemical evidence for differences in the amino acid composition of yeast and horse liver alcohol dehydrogenases



International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine 33(1): 95-101



The 2 enzymes show significant differences in amino acid sequence. In YADH [yeast alcohol dehydrogenase] there are 5 cyclic amino acids near the -SH groups and only 1 in LADH [horse liver alcohol dehydrogenase]. This could also explain the greater sensitivity of YADH to radiation-induced inactivation by the radical probes, i.e., Br2- and (SCN)2-. Of particular interest is the replacement of the arginine residue which occurs adjacent to the reactive cysteine in LADH by histidine in YADH. The radiation chemical studies reflect the similarities and the differences in amino-acid composition of YADH and LADH. The bulk of the inactivation is caused in both enzymes by damage to cysteine residues. The results reveal the different extent of participation of tyrosine, histidine and tryptophan in the active site.

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Accession: 006248758

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PMID: 342432


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Radiation Chemical Evidence for Differences in the Amino-acid Composition of Yeast and Horse-liver Alcohol Dehydrogenases. International Journal of Radiation Biology 33(1): 95-101, 1978

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