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Page 1
Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants.
Szabo E, Wilk P, Nagy B, Zambo Z, Bui D, Weichsel A, Arjunan P, Torocsik B, Hubert A, Furey W, Montfort WR, Jordan F, Weiss MS, Adam-Vizi V, Ambrus A. Szabo E, et al. Among authors: jordan f. Hum Mol Genet. 2019 Oct 15;28(20):3339-3354. doi: 10.1093/hmg/ddz177. Hum Mol Genet. 2019. PMID: 31334547 Free PMC article.
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 …
Role of glutamate 91 in information transfer during substrate activation of yeast pyruvate decarboxylase.
Li H, Furey W, Jordan F. Li H, et al. Among authors: jordan f. Biochemistry. 1999 Aug 3;38(31):9992-10003. doi: 10.1021/bi9902438. Biochemistry. 1999. PMID: 10433706
While C221 on the beta domain is the residue at which substrate activation is triggered [Baburina, I., et al. (1994) Biochemistry 33, 5630-5635; Baburina, I., et al. (1996) Biochemistry 35, 10249-10255], that information, via the substrate bound at C221, is transmitted to H92 on …
While C221 on the beta domain is the residue at which substrate activation is triggered [Baburina, I., et al. (1994) Biochemistry 33, 5630-5 …
575 results