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Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover.
Ortiz-Maldonado M, Cole LJ, Dumas SM, Entsch B, Ballou DP. Ortiz-Maldonado M, et al. Among authors: entsch b. Biochemistry. 2004 Feb 17;43(6):1569-79. doi: 10.1021/bi030193d. Biochemistry. 2004. PMID: 14769033
We conclude that the new open structure found in crystals of the Arg220Gln mutant enzyme [Wang, J., Ortiz-Maldonado, M., Entsch, B., Massey, V., Ballou, D., and Gatti, D. L. (2002) Proc. ...
We conclude that the new open structure found in crystals of the Arg220Gln mutant enzyme [Wang, J., Ortiz-Maldonado, M., Entsch, B …
Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase.
Cole LJ, Gatti DL, Entsch B, Ballou DP. Cole LJ, et al. Among authors: entsch b. Biochemistry. 2005 Jun 7;44(22):8047-58. doi: 10.1021/bi050108x. Biochemistry. 2005. PMID: 15924424
Controlled catalysis is achieved by movement of the flavin and protein between three conformations, in, out, and open [Entsch, B., et al. (2005) Arch. Biochem. Biophys. 433, 297-311]. The open conformation is important for substrate binding and product release, the …
Controlled catalysis is achieved by movement of the flavin and protein between three conformations, in, out, and open [Entsch, B …
The mobile flavin of 4-OH benzoate hydroxylase.
Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML. Gatti DL, et al. Among authors: entsch b. Science. 1994 Oct 7;266(5182):110-4. doi: 10.1126/science.7939628. Science. 1994. PMID: 7939628
51 results