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Keywords: ketosteroid isomerase
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Articles

Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B

Do Soo JANG, Hyung Jin CHA, Sun-Shin CHA, Bee Hak HONG, Nam-Chul HA, Ja Young LEE, Byung-Ha OH, Heung-Soo LEE, Kwan Yong CHOI
Journal: Biochemical Journal
Biochem J (2004) 382 (3): 967–973.
https://doi.org/10.1042/BJ20031871
Published: 07 September 2004
...Do Soo JANG; Hyung Jin CHA; Sun-Shin CHA; Bee Hak HONG; Nam-Chul HA; Ja Young LEE; Byung-Ha OH; Heung-Soo LEE; Kwan Yong CHOI KSI (ketosteroid isomerase) catalyses an allylic isomerization reaction at a diffusion-controlled rate. A hydrogen bond network, Asp 99 ···Water 504 ···Tyr 14 ···Tyr 55...
View articletitled, Structural double-mutant cycle analysis of a hydrogen bond network in ketosteroid isomerase from Pseudomonas putida biotype B
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Articles

The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni

Gyu Hyun NAM, Sun-Shin CHA, Young Sung YUN, Yun Hee OH, Bee Hak HONG, Heung-Soo LEE, Kwan Yong CHOI
Journal: Biochemical Journal
Biochem J (2003) 375 (2): 297–305.
https://doi.org/10.1042/bj20030263
Published: 15 October 2003
...Gyu Hyun NAM; Sun-Shin CHA; Young Sung YUN; Yun Hee OH; Bee Hak HONG; Heung-Soo LEE; Kwan Yong CHOI KSI (ketosteroid isomerase) from Comamonas testosteroni is a homodimeric enzyme that catalyses the allylic isomerization of Δ 5 -3-ketosteroids to their conjugated Δ 4 -isomers at a reaction rate...
View articletitled, The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni
Open the PDF for The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni in another window