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Article

Significance of H461 at subsite +1 in substrate binding and transglucosylation activity of amylomaltase from Corynebacterium glutamicum.

Archives of biochemistry and biophysics - 15 Aug 2018

Tumhom Suthipapun, Krusong Kuakarun, Kidokoro Shun-Ichi, Katoh Etsuko, Pongsawasdi Piamsook

Abstract excerpt

Amylomaltase (AM) catalyzes inter- and intra-molecular transglycosylation reactions of glucan to yield linear and cyclic oligosaccharide products. The functional roles of the conserved histidine at position 461 in the active site of AM from Corynebacterium glutamicum (CgAM) was investigated. H461 A/S/D/R/W were constructed, their catalytic properties were compared to the wild-type (WT). A significant decrease in...

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PMID: 29885290
DOI: 10.1016/j.abb.2018.06.002

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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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