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Article

Interactions across the interface contribute the stability of homodimeric 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase.

Archives of biochemistry and biophysics - 1 Oct 2009

Hwang Chi-Ching, Hsu Chao-Nan, Huang Tzu-Jung, Chiou Shean-Jaw, Hong Yi-Ren

Abstract excerpt

The dimerization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase was studied by interrupting the salt bridge interactions between D249 and R167 in the dimeric interface. Substitution of alanine, lysine and serine for D249 decreased catalytic efficiency 30, 1400 and 1.4-fold, and lowered the melting temperature 6.9, 5.4 and 7.6 degrees C, respectively. The mutated enzymes have the dimeric species but the...

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Source

Identifiers

PMID: 19683506
DOI: 10.1016/j.abb.2009.08.006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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