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Article

Identification of essential tryptophan in amylomaltase from Corynebacterium glutamicum.

International journal of biological macromolecules - 1 May 2015

Rachadech Wanitcha, Nimpiboon Pitchanan, Naumthong Wachiraporn, Nakapong Santhana, Krusong Kuakarun, Pongsawasdi Piamsook

Abstract excerpt

This work aims to identify essential tryptophan residue(s) of amylomaltase from Corynebacterium glutamicum (CgAM) through chemical modification and site-directed mutagenesis techniques. The recombinant enzyme expressed by Escherichia coli was purified and treated with N-bromosuccinimide (NBS), a modifying agent for tryptophan. A significant decrease in enzyme activity was observed indicating that tryptophan is...

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PMID: 25748841
DOI: 10.1016/j.ijbiomac.2015.02.035

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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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