Kathleen M. Holtz, Ph.D. - Publications
Affiliations: | 2000 | Boston College, Newton, MA, United States |
Area:
BiochemistryYear | Citation | Score | |||
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2005 | Stec B, Holtz KM, Wojciechowski CL, Kantrowitz ER. Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme. Acta Crystallographica. Section D, Biological Crystallography. 61: 1072-9. PMID 16041072 DOI: 10.1107/S0907444905014356 | 0.466 | |||
2000 | Holtz KM, Catrina IE, Hengge AC, Kantrowitz ER. Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases. Biochemistry. 39: 9451-8. PMID 10924140 DOI: 10.1021/Bi000899X | 0.604 | |||
2000 | Stec B, Holtz KM, Kantrowitz ER. A revised mechanism for the alkaline phosphatase reaction involving three metal ions. Journal of Molecular Biology. 299: 1303-11. PMID 10873454 DOI: 10.1006/Jmbi.2000.3799 | 0.648 | |||
2000 | Holtz KM, Stec B, Myers JK, Antonelli SM, Widlanski TS, Kantrowitz ER. Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes. Protein Science : a Publication of the Protein Society. 9: 907-15. PMID 10850800 DOI: 10.1110/Ps.9.5.907 | 0.587 | |||
1999 | Holtz KM, Kantrowitz ER. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. Febs Letters. 462: 7-11. PMID 10580082 DOI: 10.1016/S0014-5793(99)01448-9 | 0.668 | |||
1999 | Holtz KM, Stec B, Kantrowitz ER. A model of the transition state in the alkaline phosphatase reaction. The Journal of Biological Chemistry. 274: 8351-4. PMID 10085061 DOI: 10.1074/Jbc.274.13.8351 | 0.64 | |||
1997 | Widlanski TS, Myers JK, Stec B, Holtz KM, Kantrowitz ER. The road less travelled: taming phosphatases. Chemistry & Biology. 4: 489-92. PMID 9263635 DOI: 10.1016/S1074-5521(97)90319-7 | 0.474 | |||
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