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. 2020 Jul 11;19:140. doi: 10.1186/s12934-020-01397-y

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — Preliminary structural analysis of recombinant α-glucosidases. Superposition of the overall structures of Mg/Mr-αGlu based on the S. cerevisiae oligo-1,6-glucosidase (PDB: 3A47_A) template. The tree typical domains of the glycoside hydrolase family GH13 were depicted using the colour code given in the scheme (a). Sequence logo of the four conserved regions from the family GH13 identified in Mg/Mr-αGlu proteins. Amino acids of the catalytic triad were indicated with red arrows. The rest of highly conserved residues important for the catalytic mechanism were marked with asterisks. The logo was performed using 11 characterised microbial glycoside hydrolases of the family GH13 (PDB: 3A47_A; 1UOK_A; 5DO8_A; 4MB1_A; 5BRQ_A; 5ZCB_A; 2ZE0_A; 4AIE_A; 1M53_A; 1ZJA_A and UniProtKB: Q9P6J3) (b). Schematic view of the conserved residues (shown in yellow) of Mg/Mr-αGlu potentially implicated in subsite -1: Y64, V101, H104, R204, D206, E264, H338 and D339 (c). Surface representation of the active site entrance. Catalytic domain was coloured in dark cyan and domain B in red orange. The subsite -1 surface was highlighted in yellow and residues implicated were labelled (d)