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Article

Glu 103 Gln site-directed mutation causes an alteration in physical properties of spinach betaine aldehyde dehydrogenase.

Journal of biochemistry, molecular biology, and biophysics : JBMBB : the official journal of the Federation of Asian and Oceanian Biochemists and Molecular Biologists (FAOBMB) - 1 Aug 2002

Incharoensakdi Aran, Hibino Takashi, Takabe Teruhiro

Abstract excerpt

Site-directed mutant of spinach betaine aldehyde dehydrogenase (BADH) was obtained by replacing Glu 103 with Gln 103 and the resulting E 103 Q mutant was expressed in Escherichia coli. The mutant BADH as compared to the wild-type BADH was slightly more sensitive to inhibition by NaCl but less sensitive to inhibition by (NH(4))(2)SO(4). Glycinebetaine (GB) activated the wild-type enzyme but not the mutant enzyme....

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PMID: 12186739
DOI: 10.1080/10258140290018658

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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