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Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine.
Baburina I, Gao Y, Hu Z, Jordan F, Hohmann S, Furey W. Baburina I, et al. Among authors: jordan f. Biochemistry. 1994 May 10;33(18):5630-5. doi: 10.1021/bi00184a035. Biochemistry. 1994. PMID: 8180188
Earlier studies conducted on a variant of the enzyme with a single Cys at position 221 (derived from a gene that was the product of spontaneous fusion) showed that this enzyme is still subject to substrate activation [Zeng, X., Farrenkopf, B., Hohmann, S., Jordan, F …
Earlier studies conducted on a variant of the enzyme with a single Cys at position 221 (derived from a gene that was the product of spontane …
Role of cysteines in the activation and inactivation of brewers' yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein.
Zeng X, Farrenkopf B, Hohmann S, Dyda F, Furey W, Jordan F. Zeng X, et al. Among authors: jordan f. Biochemistry. 1993 Mar 16;32(10):2704-9. doi: 10.1021/bi00061a031. Biochemistry. 1993. PMID: 8448127
These substrates are now known to cause inactivation of pdc1 with concomitant modification of one Cys of the four [Zeng, X.; Chung, A.; Haran, M.; Jordan, F. (1991) J. Am. Chem. Soc. 113, 5842-49].(ABSTRACT TRUNCATED AT 250 WORDS)...
These substrates are now known to cause inactivation of pdc1 with concomitant modification of one Cys of the four [Zeng, X.; Chung, A.; Hara …
564 results