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Article

Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis.

Biochimica et biophysica acta - 17 Oct 1996

Pasquo A, Britton K L, Stillman T J, Rice D W, Cölfen H, Harding S E, Scandurra R, Engel P C

Abstract excerpt

By using site-directed mutagenesis, Phe-187, one of the amino-acid residues involved in hydrophobic interaction between the three identical dimers comprising the hexamer of Clostridium symbiosum glutamate dehydrogenase (GDH), has been replaced by an aspartic acid residue. Over-expression in Escherichia coli led to production of large amounts of a soluble protein which, though devoid of GDH activity, showed the...

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Source

Identifiers

PMID: 8917616
DOI: 10.1016/s0167-4838(96)00017-9

Genes

DTNB
SDS

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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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