Maltase

Maltase (EC 3.2.1.20 (https://enzyme.expasy.org/EC/3.2.1.20),

alpha-glucosidase, glucoinvertase, glucosidosucrase, maltase-
Alpha-glucosidase
glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha- Identifiers
D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, EC no. 3.2.1.20 (https://www.qm
alpha-D-glucoside glucohydrolase) is one type of alpha-glucosidase ul.ac.uk/sbcs/iubmb/enzy
enzymes located in the brush border of the small intestine.[1][2] This
me/EC3/2/1/20.html)
enzyme catalyzes the hydrolysis of disaccharide maltose into two
simple sugars of glucose. Maltase is found in plants, bacteria, yeast, CAS no. 9001-42-7 (http://www.co
humans, and other vertebrates. It is thought to be synthesized by mmonchemistry.org/Che
cells of the mucous membrane lining the intestinal wall.[3] micalDetail.aspx?ref=900
1-42-7&title=)
Digestion of starch requires six intestinal enzymes. Two of these
Databases
enzymes are luminal endo-glucosidases named alpha-amylases. The
other four enzymes have been identified as different maltases, exo- IntEnz IntEnz view (https://www.
glucosidases bound to the luminal surface of enterocytes. Two of ebi.ac.uk/intenz/query?c
these maltase activities were associated with sucrase-isomaltase md=SearchEC&ec=3.2.1.
(maltase Ib, maltase Ia). The other two maltases with no 20)
distinguishing characteristics were named maltase-glucoamylase
(maltases II and III). The activities of these four maltases are also BRENDA BRENDA entry (http://ww
described as alpha-glucosidase because they all digest linear starch w.brenda-enzymes.org/e
oligosaccharides to glucose.[4][2] nzyme.php?ecno=3.2.1.
20)
In most cases, it is equivalent to alpha-glucosidase, but the term
ExPASy NiceZyme view (https://e
"maltase" emphasizes the disaccharide nature of the substrate from
nzyme.expasy.org/EC/3.
which glucose is cleaved, and "alpha-glucosidase" emphasizes the
bond, whether the substrate is a disaccharide or polysaccharide. 2.1.20)
KEGG KEGG entry (https://ww
Vampire bats are the only vertebrates known to not exhibit intestinal w.genome.jp/dbget-bin/w
maltase activity.[5] ww_bget?enzyme+3.2.1.
20)
MetaCyc metabolic pathway (http
Contents s://biocyc.org/META/subs
Structure tring-search?type=NIL&o
bject=3.2.1.20)
Mechanism
PRIAM profile (http://priam.prabi.
Industrial applications
fr/cgi-bin/PRIAM_profiles
History _CurrentRelease.pl?EC=
Maltase deficiency 3.2.1.20)
See also PDB RCSB PDB (https://www.r
References structures csb.org/search?q=rcsb_
polymer_entity.rcsb_ec_li
External links
neage.id:3.2.1.20) PDBe
(https://www.ebi.ac.uk/pd

Structure be/entry/search/index?ec
Maltase is part of a group of intestinal enzymes called FamilyGH13 _number:3.2.1.20)
(Glycoside hydrolase family 13) that are responsible for breaking PDBsum (https://www.eb
apart the α-glucosidase linkages of complex carbohydrates into i.ac.uk/thornton-srv/data
simple to use glucose molecules.[6] The glucose molecules would bases/cgi-bin/enzymes/G
then be used as a sort of "food" for cells to produce energy etPage.pl?ec_number=3.
(Adenosine triphosphate) during Cellular respiration. The following
2.1.20)
are genes that can code for maltase:
Search
Acid alpha-glucosidase which is coded on the GAA gene PMC articles (https://www.ncbi.nlm.ni
is essential to breakdown complex sugars called h.gov/entrez/query.fcgi?db=pub
Glycogen into glucose. med&term=3.2.1.20%5BEC/R
Maltase-glucoamylase which is coded on the MGAM N%20Number%5D%20AND%
gene plays a roll in the digestion of starches. It is due to 20pubmed%20pmc%20local%
this enzyme in humans that starches of plant origin are 5Bsb%5D)
able to digested.[7] PubMed articles (https://www.ncbi.nlm.ni
Sucrase-isomaltase which is coded on the SI gene is h.gov/entrez/query.fcgi?db=pub
essential for the digestion of carbohydrates including med&term=3.2.1.20%5BEC/R
starch, sucrose and isomaltose. N%20Number%5D)
Alpha-amylase 1 which is coded on the AMY1A gene is NCBI proteins (https://www.ncbi.nlm.n
responsible of cleaving α-glucosidase linkages in ih.gov/protein?term=3.2.1.20%
oligosaccharides and polysaccharides in order to 5BEC/RN%20Number%5D)
produce starches and glycogen for the previous enzymes
to catalyze. Higher quantities of this gene in the brain
have been shown to lower the risk of Alzheimer's
disease.[8]

Mechanism
Maltose
The mechanism of all FamilyGH13 enzymes is to break a α-
glucosidase linkage by hydrolyzing it. Maltase focuses on breaking
apart maltose, a disaccharide that is a link between 2 units of glucose,
at the α-(1->4) bond. The rate of hydrolysis is controlled by the size of
the substrate (carbohydrate size).[9]

Industrial applications
Ligand (NAG) interactions in
Alpha-amylase has an important function in degradation of starches, Maltase-Glucoamylase
so it extremely common used in the baking industry. It is mostly used
a means of flavor enhancing to improve bread quality.[7] Without
alpha-amylase, yeast would not be able to ferment.[1]

Maltose-glucoamylase is commonly used as a fermentation source as

it is able to cut starch into maltose, which is then used for brewing
beers and sake.[7]

Other than brewing, maltose glucoamylase has been studied by Interactions of oligosaccharides in
introducing specific inhibitors to stop the hydrolysis of the α- Alpha-amylase
glucosidase linkages. By inhibiting the cleave of the linkages,
scientists are hoping to devise a drug that is more efficient and less
toxic to treating diabetes.[10]
History
The history of maltase discovery began when Napoleon Bonaparte
declared a continental blockade in his “Berlin decree” in 1806. This Hydrolysis reaction of Maltose being
initiated the search for alternative sources of sugar. In 1833 French broken at the 1-4 alpha-glucosidase
chemists Anselm Payen and Jean-Francois Persoz discovered a malt linkage.
extract that converted starch into glucose which they called diastase at
the time.[11] In 1880, H.T. Brown discovered mucosal maltase
activity and differentiated it from diastase, now called amylase.[2] In the 1960s advances in protein chemistry
allowed Arne Dahlqvist and Giorgio Semenza to fractionate and characterize small intestinal maltase activities.
Both groups showed there were four major fractions of maltase activity that were intrinsic to two different
peptide structures, sucrase-isomaltase and maltase-glucoamylase.[4][2][11][9] Fifty years later entering the
genomic age, cloning and sequencing of the mucosal starch hydrolase confirmed Dahlqvist and Semenza’s
findings.[11]

Maltase deficiency
Acid maltase deficiency (AMD) also known as Pompe disease was first described by Dutch pathologist JC
Pompe in 1932.[12][13] AMD is a non sex linked autosomal recessive condition in which excessive
accumulation of glycogen build up within lysosome vacuoles in nearly all types of cells all over the
body.[12][13][14] It is one of the more serious glycogen storage diseases affecting muscle tissue.[15]

AMD is categorized into three separate types based on the age of onset of symptoms in the affected individual.
Infantile (Type a), childhood (Type b), and adulthood (Type c). The type of AMD is determined by the type of
gene mutation localized on 17q23. Mutation type will determine production level of acid maltase. AMD is
extremely fatal. Type a generally die of heart failure prior to age one. Type b die of respiratory failure between
ages three to twenty-four. Type c die of respiratory failure 10-20 years of the onset of symptoms.[15]

See also
Maltase-glucoamylase
Sucrase-isomaltase

References
1. "Maltase: Baking Ingredients" (https://bakerpedia.com/ingredients/maltase/). BAKERpedia. 14
January 2021.
2. Quezada-Calvillo R, Robayo-Torres CC, Opekun AR, Sen P, Ao Z, Hamaker BR, et al. (July
2007). "Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal
starch alpha-glucogenesis" (https://doi.org/10.1093%2Fjn%2F137.7.1725). The Journal of
Nutrition. 137 (7): 1725–33. doi:10.1093/jn/137.7.1725 (https://doi.org/10.1093%2Fjn%2F137.7.
1725). PMID 17585022 (https://pubmed.ncbi.nlm.nih.gov/17585022).
3. The Editors (8 June 2020). "Maltase" (https://www.britannica.com/science/maltase).
Encyclopedia Britannica.
4. Nichols BL, Baker SS, Quezada-Calvillo R (June 2018). "Metabolic Impacts of Maltase
Deficiencies". Journal of Pediatric Gastroenterology and Nutrition. 66 Suppl 3 (3): S24–S29.
doi:10.1097/MPG.0000000000001955 (https://doi.org/10.1097%2FMPG.0000000000001955).
PMID 29762372 (https://pubmed.ncbi.nlm.nih.gov/29762372). S2CID 46891498 (https://api.se
manticscholar.org/CorpusID:46891498).
 5. Schondube JE, Herrera-M LG, Martínez del Rio C (2001). "Diet and the evolution of digestion
and renal function in phyllostomid bats" (http://www.uwyo.edu/cmdelrio/site/publications_files/b
ats,%20isotopes,%20and%20kidneys.pdf) (PDF). Zoology. 104 (1): 59–73. doi:10.1078/0944-
2006-00007 (https://doi.org/10.1078%2F0944-2006-00007). PMID 16351819 (https://pubmed.n
cbi.nlm.nih.gov/16351819).
6. "Glycoside Hydrolase Family 13 - CAZypedia" (https://www.cazypedia.org/index.php/Glycoside
_Hydrolase_Family_13). www.cazypedia.org. Retrieved 2021-03-06.
7. Nichols BL, Avery S, Sen P, Swallow DM, Hahn D, Sterchi E (February 2003). "The maltase-
glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch
digestion activities" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC298790). Proceedings of
the National Academy of Sciences of the United States of America. 100 (3): 1432–7.
Bibcode:2003PNAS..100.1432N (https://ui.adsabs.harvard.edu/abs/2003PNAS..100.1432N).
doi:10.1073/pnas.0237170100 (https://doi.org/10.1073%2Fpnas.0237170100). PMC 298790 (h
ttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC298790). PMID 12547908 (https://pubmed.ncbi.nl
m.nih.gov/12547908).
8. Byman E, Nägga K, Gustavsson AM, Andersson-Assarsson J, Hansson O, Sonestedt E,
Wennström M (November 2020). "Alpha-amylase 1A copy number variants and the association
with memory performance and Alzheimer's dementia" (https://www.ncbi.nlm.nih.gov/pmc/article
s/PMC7680592). Alzheimer's Research & Therapy. 12 (1): 158. doi:10.1186/s13195-020-
00726-y (https://doi.org/10.1186%2Fs13195-020-00726-y). PMC 7680592 (https://www.ncbi.nl
m.nih.gov/pmc/articles/PMC7680592). PMID 33220711 (https://pubmed.ncbi.nlm.nih.gov/3322
0711).
9. "Maltase" (http://worthington-biochem.com/MALT/default.html). Worthington Enzyme Manual.
Worthington Biochemical Corporation.
10. Shang Q, Xiang J, Zhang H, Li Q, Tang Y (2013). "The effect of polyhydroxylated alkaloids on
maltase-glucoamylase" (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742645). PLOS ONE.
8 (8): e70841. Bibcode:2013PLoSO...870841S (https://ui.adsabs.harvard.edu/abs/2013PLoS
O...870841S). doi:10.1371/journal.pone.0070841 (https://doi.org/10.1371%2Fjournal.pone.007
0841). PMC 3742645 (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3742645).
PMID 23967118 (https://pubmed.ncbi.nlm.nih.gov/23967118).
11. Lentze MJ (June 2018). "The History of Maltose-active Disaccharidases" (https://doi.org/10.109
7%2FMPG.0000000000001960). Journal of Pediatric Gastroenterology and Nutrition. 66 Suppl
3 (3): S4–S6. doi:10.1097/MPG.0000000000001960 (https://doi.org/10.1097%2FMPG.0000000
000001960). PMID 29762367 (https://pubmed.ncbi.nlm.nih.gov/29762367).
12. "Maltase" (http://worldofenzymes.info/enzymes-introduction/maltase/2/). World of Enzymes and
Probiotics. 2012.
13. Kishner S, Sterne FE (5 December 2020). "Acid Maltase Deficiency Myopathy" (https://emedici
ne.medscape.com/article/313724-overview). Practice Essentials, Pathophysiology,
Epidemiology. Medscape.
14. Merritt II LJ (20 December 2020). "Lysosomal Acid Alpha-Glucosidase Deficiency (Pompe
Disease, Glycogen Storage Disease II, Acid Maltase Deficiency)" (https://www.uptodate.com/co
ntents/lysosomal-acid-alpha-glucosidase-deficiency-pompe-disease-glycogen-storage-disease
-ii-acid-maltase-deficiency). UpToDate.
15. "Acid maltase deficiency" (https://www.encyclopedia.com/science/encyclopedias-almanacs-tra
nscripts-and-maps/acid-maltase-deficiency). Gale Encyclopedia of Genetic Disorders.
Encyclopedia.com. 5 March 2021.

External links
Maltases (https://meshb.nlm.nih.gov/record/ui?name=Maltases) at the US National Library of
Medicine Medical Subject Headings (MeSH)
 Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase (http
s://web.archive.org/web/20110709191916/http://bioinform.genetika.ru/members/Naumoff/MB20
07E.pdf)

Retrieved from "https://en.wikipedia.org/w/index.php?title=Maltase&oldid=1018317760"

This page was last edited on 17 April 2021, at 12:06 (UTC).

Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this
site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia
Foundation, Inc., a non-profit organization.