関: alpha-glucosidase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/09/12 21:57:47」(JST)

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Maltose

Maltase (EC 3.2.1.20, alpha-glucosidase, glucoinvertase, glucosidosucrase, maltase-glucoamylase, alpha-glucopyranosidase, glucosidoinvertase, alpha-D-glucosidase, alpha-glucoside hydrolase, alpha-1,4-glucosidase, alpha-D-glucoside glucohydrolase) is an enzyme located in on the brush border of the small intestine that breaks down the disaccharide maltose.^[1]^[2]^[3]^[4]^[5]^[6] Maltase catalyzes the hydrolysis of maltose to the simple sugar glucose. This enzyme is found in plants, bacteria, and yeast. Acid maltase deficiency is categorized into three separate types based on the age of onset of symptoms in the affected individual.

In most cases, it is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide^{[citation needed]}.

In humans, maltase will break down the alpha form of the maltose.

Vampire bats are the only vertebrates that do not exhibit intestinal maltase activity. ^[7]

References

^ "Maltase - Definition from the Merriam-Webster Online Dictionary". Retrieved 2009-04-06.
^ Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. (1970). "Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver". Biochim. Biophys. Acta 212 (3): 470–477. doi:10.1016/0005-2744(70)90253-6. PMID 5466143.
^ Flanagan, P.R. and Forstner, G.G. (1978). "Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH". Biochem. J. 173 (2): 553–563. PMID 29602.
^ Larner, J. (1960). "Other glucosidases". In Boyer, P.D., Lardy, H. and Myrbäck, K. The Enzymes 4 (2nd ed.). New York: Academic Press. pp. 369–378.
^ Sivikami, S. and Radhakrishnan, A.N. (1973). "Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200". Indian J. Biochem. Biophys. 10 (4): 283–284. PMID 4792946.
^ Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. (1982). "Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity". Eur. J. Biochem. 126: 559–568. doi:10.1111/j.1432-1033.1982.tb06817.x. PMID 6814909.
^ Jorge E. Schondube, L. Gerardo Herrera-M., Carlos Martínez del Rio (2001). "Diet and the evolution of digestion and renal function in phyllostomid bats" (PDF). Zoology 104: 59–73.

External links

Maltases at the US National Library of Medicine Medical Subject Headings (MeSH)
Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase

UpToDate Contents

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1. リソソーム酸α-グルコシダーゼ欠損症（ポンペ病、糖原病II型、酸マルターゼ欠損症） lysosomal acid alpha glucosidase deficiency pompe disease glycogen storage disease ii acid maltase deficiency
2. グルコースおよびグリコーゲン代謝の遺伝性疾患の概要 overview of inherited disorders of glucose and glycogen metabolism
3. 筋緊張低下および脱力を呈する幼児に対するアプローチ approach to the infant with hypotonia and weakness
4. 代謝性ミオパチーへのアプローチ approach to the metabolic myopathies
5. 先天性代謝異常：個々の障害の発見 inborn errors of metabolism identifying the specific disorder

English Journal

Functional expression and molecular characterization of Culex quinquefasciatus salivary α-glucosidase (MalI).

Suthangkornkul R1, Sirichaiyakul P1, Sungvornyothin S2, Thepouyporn A1, Svasti J3, Arthan D4.
Protein expression and purification.Protein Expr Purif.2015 Jun;110:145-50. doi: 10.1016/j.pep.2015.02.018. Epub 2015 Mar 5.
Salivary α-glucosidases (MalI) have been much less characterized when compared with midgut α-glucosidases, which have been studied in depth. Few studies have been reported on the partial characterization of MalI, but no clear function has been ascribed. The aim of this study is to purify and chara
PMID 25746591

Dietary Phenolic Compounds Selectively Inhibit the Individual Subunits of Maltase-Glucoamylase and Sucrase-Isomaltase with the Potential of Modulating Glucose Release.

Simsek M1, Quezada-Calvillo R2,3, Ferruzzi MG1, Nichols BL3, Hamaker BR1.
Journal of agricultural and food chemistry.J Agric Food Chem.2015 Apr 13. [Epub ahead of print]
In this study, it was hypothesized that dietary phenolic compounds selectively inhibit the individual C- and N-terminal (Ct, Nt) subunits of the two small intestinal α-glucosidases, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), for a modulated glycemic carbohydrate digestion. The inhibit
PMID 25816913

Design and Synthesis of Labystegines, Hybrid Iminosugars from LAB and Calystegine, as Inhibitors of Intestinal α-Glucosidases: Binding Conformation and Interaction for ntSI.

Kato A1, Zhang ZL2, Wang HY2, Jia YM2, Yu CY2, Kinami K1, Hirokami Y1, Tsuji Y1, Adachi I1, Nash RJ3, Fleet GW4,5, Koseki J6, Nakagome I6, Hirono S6.
The Journal of organic chemistry.J Org Chem.2015 Apr 13. [Epub ahead of print]
This paper identifies the required configuration and orientation of α-glucosidase inhibitors, miglitol, α-1-C-butyl-DNJ, and α-1-C-butyl-LAB for binding to ntSI (isomaltase). Molecular dynamics (MD) calculations suggested that the flexibility around the keyhole of ntSI is lower than that of ctSI
PMID 25843107

Japanese Journal

Selective purification of intestinal maltase complex by affinity chromatography employing an uncompetitive inhibitor as the ligand

Kato Eisuke,Tsuji Hiroki,Kawabata Jun
Tetrahedron 71(9), 1419-1424, 2015-03-04
… Use of the potent α-glucosidase uncompetitive inhibitor 2-aminoresorcinol as the ligand of the affinity gel offered selective purification of maltase-glucoamylase complex from the crude mixture of intestinal α-glucosidases. …
NAID 120005595709

Influence of Chronic Social Defeat Stress on Digestive System Functioning in Rats

TOYODA Atsushi,IIO Wataru,MATSUKAWA Noriko [他],TSUKAHARA Takamitsu
Journal of Nutritional Science and Vitaminology 61(3), 280-284, 2015
… mRNA expression associated with a nutrient absorption, glucose absorption activity, and activities of the digestive enzymes such as maltase, sucrase and lactase was measured. …
NAID 130005089923

Inhibitory Effect of Oligomeric Polyphenols from Peanut-skin on Sugar Digestion Enzymes and Glucose Transport

Tamura Tomoko,Ozawa Megumi,Kobayashi Shoko,Watanabe Hirohito,Arai Soichi,Mura Kiyoshi
Food Science and Technology Research 21(1), 111-115, 2015
… Inhibitory effects of oligomeric polyphenols extracted from peanut skin on α-amylase, maltase, sucrase and glucose transport were investigated. …
NAID 130005061941

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拡張検索	「isomaltase」「acid maltase欠損症」

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Alpha-glucosidase
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EC number	3.2.1.20
CAS number	9001-42-7
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ExPASy	NiceZyme view
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MetaCyc	metabolic pathway
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