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Article

Structural insights reveal the second base catalyst of isomaltose glucohydrolase.

The FEBS journal - 1 Feb 2022

Tagami Takayoshi, Chen Minghao, Furunaga Yuta, Kikuchi Asako, Sadahiro Juri, Lang Weeranuch, Okuyama Masayuki, Tanaka Yoshikazu, Iwasaki Tomohito, Yao Min, Kimura Atsuo

Abstract excerpt

Glycoside hydrolase family 15 (GH15) inverting enzymes contain two glutamate residues functioning as a general acid catalyst and a general base catalyst, for isomaltose glucohydrolase (IGHase), Glu178 and Glu335, respectively. Generally, a two-catalytic residue-mediated reaction exhibits a typical bell-shaped pH-activity curve. However, IGHase is found to display atypical non-bell-shaped pH-kcat and pH-kcat /Km...

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PMID: 34665923
DOI: 10.1111/febs.16237

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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