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Article

Homotropic allosteric control in clostridial glutamate dehydrogenase: different mechanisms for glutamate and NAD+?

FEBS letters - 11 Jun 2008

Hamza Muaawia A, Engel Paul C

Abstract excerpt

Clostridial glutamate dehydrogenase mutants with the 5 Trp residues in turn replaced by Phe showed the importance of Trp 64 and 449 in cooperativity with glutamate at pH 9. These mutants are examined here for their behaviour with NAD+ at pH 7.0 and 9.0. The wild-type enzyme displays negative NAD+...

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PMID: 18472008
DOI: 10.1016/j.febslet.2008.04.049

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-18472008-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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