:Glucan 1,4-alpha-maltohydrolase

{{Infobox enzyme

| Name = Glucan 1,4-alpha-maltohydrolase

| EC_number = 3.2.1.133

| CAS_number = 160611-47-2

| GO_code =

| image =

| width =

| caption =

}}

Glucan 1,4-alpha-maltohydrolase ({{EC number|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.{{cite journal | title = Cloning of a maltogenic α-amylase from Bacillus stearothermophilus | vauthors = Diderichsen B, Christiansen L |journal = FEMS Microbiol. Lett. |year = 1988 |volume = 56 |pages = 53–59 |doi=10.1111/j.1574-6968.1988.tb03149.x|doi-access = free }}{{cite journal | title = Properties and application of a thermostable maltogenic amylase produced by a strain of Bacillus modified by recombinant-DNA techniques | vauthors = Outtrup H, Norman BE |journal = Stärke |year = 1984 |volume = 36 | issue = 12 |pages = 405–411 |doi=10.1002/star.19840361202}} 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,{{cite journal | vauthors = Cha HJ, Yoon HG, Kim YW, Lee HS, Kim JW, Kweon KS, Oh BH, Park KH | display-authors = 6 | title = Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose | journal = European Journal of Biochemistry | volume = 253 | issue = 1 | pages = 251–262 | date = April 1998 | pmid = 9578484 | doi = 10.1046/j.1432-1327.1998.2530251.x | doi-access = free }} Thermus sp.{{cite journal | vauthors = Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW, Park KH | title = Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain | language = EN | journal = Applied and Environmental Microbiology | volume = 65 | issue = 4 | pages = 1644–1651 | date = April 1999 | pmid = 10103262 | doi = 10.1128/AEM.65.4.1644-1651.1999 | pmc = 91232 | bibcode = 1999ApEnM..65.1644K }} and Geobacillus thermoleovorans{{cite journal | vauthors = Mehta D, Satyanarayana T | title = Dimerization mediates thermo-adaptation, substrate affinity and transglycosylation in a highly thermostable maltogenic amylase of Geobacillus thermoleovorans | journal = PLOS ONE | volume = 8 | issue = 9 | pages = e73612 | date = 2013-09-19 | pmid = 24069213 | pmc = 3777949 | doi = 10.1371/journal.pone.0073612 | bibcode = 2013PLoSO...873612M | doi-access = free }} are able to degrade acarbose to glucose and acarviosine-glucose.

File:Acarbose degradation by gut bacterial maltogenic amylase.png