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Showing results 1 to 4 of 4

1
Contribution of the hydrogen-bond network involving a tyrosine triad in the active site to the structure and function of a highly proficient ketosteroid isomerase from Pseudomonas putida biotype B

Kim, DH; Jang, DS; Nam, GH; Choi, G; Kim, JS; Ha, NC; Kim, MS; et al, BIOCHEMISTRY, v.39, no.16, pp.4581 - 4589, 2000-04

2
Maintenance of alpha-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B

Nam, GH; Jang, DS; Cha, SS; Lee, TH; Kim, DH; Hong, BH; Yun, YS; et al, BIOCHEMISTRY, v.40, no.45, pp.13529 - 13537, 2001-11

3
Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B

Kim, DH; Nam, GH; Jang, DS; Choi, G; Joo, S; Kim, JS; Oh, Byung-Ha; et al, BIOCHEMISTRY, v.38, no.42, pp.13810 - 13819, 1999-10

4
Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B

Yun, YS; Nam, GH; Kim, YG; Oh, Byung-Ha; Choi, KY, FEBS JOURNAL, v.272, pp.1999 - 2011, 2005-04

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