Glucan 1,4-alpha-maltohydrolase

Glucan 1,4-alpha-maltohydrolase
Identifiers
EC no.3.2.1.133
CAS no.160611-47-2
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Glucan 1,4-alpha-maltohydrolase (EC 3.2.1.133, maltogenic alpha-amylase, 1,4-alpha-D-glucan alpha-maltohydrolase) is an enzyme with systematic name 4-alpha-D-glucan alpha-maltohydrolase.[1][2] This enzyme catalyses the following chemical reaction

hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains

This enzyme acts on starch and related polysaccharides and oligosaccharides. Maltogenic amylases from Bacillus stearothermophilus,[3] Thermus sp.[4] and Geobacillus thermoleovorans[5] are able to degrade acarbose to glucose and acarviosine-glucose.

Acarbose is degraded by different enzymes in the gut microbiome. secretion of gut bacterial enzymes inhibit acarbose.
Acarbose is degraded by different enzymes in the gut microbiome. secretion of gut bacterial enzymes inhibit acarbose.

References

  1. ^ Diderichsen B, Christiansen L (1988). "Cloning of a maltogenic α-amylase from Bacillus stearothermophilus". FEMS Microbiol. Lett. 56: 53–59. doi:10.1111/j.1574-6968.1988.tb03149.x.
  2. ^ Outtrup H, Norman BE (1984). "Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques". Stärke. 36 (12): 405–411. doi:10.1002/star.19840361202.
  3. ^ Cha HJ, Yoon HG, Kim YW, Lee HS, Kim JW, Kweon KS, et al. (April 1998). "Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose". European Journal of Biochemistry. 253 (1): 251–262. doi:10.1046/j.1432-1327.1998.2530251.x. PMID 9578484.
  4. ^ Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH (April 1999). "Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain". Applied and Environmental Microbiology. 65 (4): 1644–1651. Bibcode:1999ApEnM..65.1644K. doi:10.1128/AEM.65.4.1644-1651.1999. PMC 91232. PMID 10103262.
  5. ^ Mehta D, Satyanarayana T (2013-09-19). "Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans". PLOS ONE. 8 (9): e73612. Bibcode:2013PLoSO...873612M. doi:10.1371/journal.pone.0073612. PMC 3777949. PMID 24069213.

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