ArticleThe Journal of biological chemistry2015
Structural Basis for the Interconversion of Maltodextrins by MalQ, the Amylomaltase of Escherichia coli.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 59 citations in OpenAlex.
- Acarbose differentially affects gut microbial metabolism of maltose and sucrose, distinctly modulating host metabolism.iScience · 2026Article
- Article
- Role of MalQ Enzyme in a Reconstructed Maltose/Maltodextrin Pathway inMicroorganisms · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Exploring the biosynthetic gene clusters in Brevibacterium: a comparative genomic analysis of diversity and distribution.BMC genomics · 2023Article
- Enhanced production of maltobionic acid by a metabolically engineered Escherichia coli incapable of maltose utilization.Bioprocess and biosystems engineering · 2023Article
- The 4-α-Glucanotransferase AcbQ Is Involved in Acarbose Modification inMicroorganisms · 2023Article
- Identification of crucial amino acid residues involved in large ring cyclodextrin synthesis by amylomaltase from Corynebacterium glutamicum.Computational and structural biotechnology journal · 2023Article
- A Novel Subfamily GH13_46 of the α-Amylase Family GH13 Represented by the Cyclomaltodextrinase fromMolecules (Basel, Switzerland) · 2022Article
- Microbial Fermentation of Polyethylene Terephthalate (PET) Plastic Waste for the Production of Chemicals or Electricity.Angewandte Chemie (International ed. in English) · 2022Article
- Rapid Mining of NovelMarine drugs · 2022Article
- Production of Large-Ring Cyclodextrins by Amylomaltases.Molecules (Basel, Switzerland) · 2022Review
- Identification of an Amylomaltase from the Halophilic ArchaeonLife (Basel, Switzerland) · 2022Article
- Heterologous expression of 4α-glucanotransferase: overproduction and properties for industrial applications.World journal of microbiology & biotechnology · 2022Review
- Amylomaltases in Extremophilic Microorganisms.Biomolecules · 2021Review
- A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77.3 Biotech · 2021Article
- Streptococcus agalactiae amylomaltase offers insight into the transglycosylation mechanism and the molecular basis of thermostability among amylomaltases.Scientific reports · 2021Article
- An 1,4-α-Glucosyltransferase Defines a New Maltodextrin Catabolism Scheme in Lactobacillus acidophilus.Applied and environmental microbiology · 2020Article
- Enzymes Required for Maltodextrin Catabolism in Enterococcus faecalis Exhibit Novel Activities.Applied and environmental microbiology · 2017Article
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amylomaltase MalQ is essential for the metabolism of maltose and maltodextrins in Escherichia coli. It catalyzes transglycosylation/disproportionation reactions in which glycosyl or dextrinyl units are transferred among linear maltodextrins of various lengths. To elucidate the molecular basis of transglycosylation by MalQ, we have determined three crystal structures of this enzyme, i.e. the apo-form, its complex with maltose, and an inhibitor complex with the transition state analog acarviosine-glucose-acarbose, at resolutions down to 2.1 Å. MalQ represents the first example of a mesophilic bacterial amylomaltase with known structure and exhibits an N-terminal extension of about 140 residues, in contrast with previously described thermophilic enzymes. This moiety seems unique to amylomaltases from Enterobacteriaceae and folds into two distinct subdomains that associate with different parts of the catalytic core. Intriguingly, the three MalQ crystal structures appear to correspond to distinct states of this enzyme, revealing considerable conformational changes during the catalytic cycle. In particular, the inhibitor complex highlights the requirement of both a 3-OH group and a 4-OH group (or α1-4-glycosidic bond) at the acceptor subsite +1 for the catalytically competent orientation of the acid/base catalyst Glu-496. Using an HPLC-based MalQ enzyme assay, we could demonstrate that the equilibrium concentration of maltodextrin products depends on the length of the initial substrate; with increasing numbers of glycosidic bonds, less glucose is formed. Thus, both structural and enzymatic data are consistent with the extremely low hydrolysis rates observed for amylomaltases and underline the importance of MalQ for the metabolism of maltodextrins in E. coli.
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