Lakenya Williams, Ph.D. - Publications

Affiliations: 
Texas A & M University, College Station, TX, United States 
Area:
Enzymology

7 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2009 Nguyen TT, Fedorov AA, Williams L, Fedorov EV, Li Y, Xu C, Almo SC, Raushel FM. The mechanism of the reaction catalyzed by uronate isomerase illustrates how an isomerase may have evolved from a hydrolase within the amidohydrolase superfamily. Biochemistry. 48: 8879-90. PMID 19678710 DOI: 10.1021/Bi901046X  0.734
2008 Williams L, Fan F, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the Mycobacterium smegmatis cysteine ligase (MshC). Biochemistry. 47: 4843-50. PMID 18373355 DOI: 10.1021/Bi800327U  0.601
2007 Fresquet V, Williams L, Raushel FM. Partial randomization of the four sequential amidation reactions catalyzed by cobyric acid synthetase with a single point mutation. Biochemistry. 46: 13983-93. PMID 18001139 DOI: 10.1021/Bi7016238  0.68
2007 Williams L, Fresquet V, Santander PJ, Raushel FM. The multiple amidation reactions catalyzed by Cobyric acid synthetase from Salmonella typhimurium are sequential and dissociative. Journal of the American Chemical Society. 129: 294-5. PMID 17212407 DOI: 10.1021/Ja067962B  0.657
2006 Williams L, Nguyen T, Li Y, Porter TN, Raushel FM. Uronate isomerase: a nonhydrolytic member of the amidohydrolase superfamily with an ambivalent requirement for a divalent metal ion. Biochemistry. 45: 7453-62. PMID 16768441 DOI: 10.1021/Bi060531L  0.473
2004 Fresquet V, Williams L, Raushel FM. Mechanism of cobyrinic acid a,c-diamide synthetase from Salmonella typhimurium LT2. Biochemistry. 43: 10619-27. PMID 15311923 DOI: 10.1021/Bi048972X  0.641
2003 Williams L, Zheng R, Blanchard JS, Raushel FM. Positional isotope exchange analysis of the pantothenate synthetase reaction. Biochemistry. 42: 5108-13. PMID 12718554 DOI: 10.1021/Bi0340853  0.648
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