関: glucan 1,4-alpha-glucosidase

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/20 22:22:11」(JST)

wiki en

Glucan 1,4-alpha-glucosidase (EC 3.2.1.3, glucoamylase, amyloglucosidase, gamma-amylase, lysosomal alpha-glucosidase, acid maltase, exo-1,4-alpha-glucosidase, glucose amylase, gamma-1,4-glucan glucohydrolase, acid maltase, 1,4-alpha-D-glucan glucohydrolase) is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose

Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4.

References

^ French, D. and Knapp, D.W. (1950). "The maltase of Clostridium acetobutylicum". J. Biol. Chem. 187: 463–471. PMID 14803428.
^ Illingworth Brown, B. and Brown, D.H. (1965). "The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues". Biochim. Biophys. Acta 110: 124–133. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.
^ Jeffrey, P.L., Brown, D.H. and Brown, B.I. (1970). "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry 9: 1403–1415. doi:10.1021/bi00808a015. PMID 4313883.
^ Kelly, J.J. and Alpers, D.H. (1973). "Properties of human intestinal glucoamylase". Biochim. Biophys. Acta 315: 113–122. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.
^ Miller, K.D. and Copeland, W.H. (1956). "A blood trans-α-glucosylase". Biochim. Biophys. Acta 22: 193–194. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.
^ Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. (1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature 181: 770–771. doi:10.1038/181770a0. PMID 13517301.

External links

Glucan 1,4-alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)

English Journal

Synergistic amylomaltase and branching enzyme catalysis to suppress cassava starch digestibility.

Sorndech W1, Meier S2, Jansson AM2, Sagnelli D3, Hindsgaul O2, Tongta S4, Blennow A5.
Carbohydrate polymers.Carbohydr Polym.2015 Nov 5;132:409-18. doi: 10.1016/j.carbpol.2015.05.084. Epub 2015 Jun 18.
Starch provides our main dietary caloric intake and over-consumption of starch-containing foods results in escalating life-style disease including diabetes. By increasing the content of α-1,6 branch points in starch, digestibility by human amylolytic enzymes is expected to be retarded. Aiming at ge
PMID 26256365

Characterisation of branched gluco-oligosaccharides to study the mode-of-action of a glucoamylase from Hypocrea jecorina.

Jonathan MC1, van Brussel M2, Scheffers MS3, Kabel MA4.
Carbohydrate polymers.Carbohydr Polym.2015 Nov 5;132:59-66. doi: 10.1016/j.carbpol.2015.06.023. Epub 2015 Jun 15.
In the conversion of starch to fermentable glucose for bioethanol production, hydrolysis of amylopectin by α-amylases and glucoamylases is the slowest step. In this process, α-1,6-branched gluco-oligosaccharides accumulate and are slowly degraded. Glucoamylases that are able to degrade such branch
PMID 26256324

Production of raw starch-degrading enzyme by Aspergillus sp. and its use in conversion of inedible wild cassava flour to bioethanol.

Moshi AP1, Hosea KM2, Elisante E2, Mamo G3, Önnby L3, Nges IA4.
Journal of bioscience and bioengineering.J Biosci Bioeng.2015 Oct 15. pii: S1389-1723(15)00332-1. doi: 10.1016/j.jbiosc.2015.09.001. [Epub ahead of print]
The major bottlenecks in achieving competitive bioethanol fuel are the high cost of feedstock, energy and enzymes employed in pretreatment prior to fermentation. Lignocellulosic biomass has been proposed as an alternative feedstock, but because of its complexity, economic viability is yet to be real
PMID 26481161

Japanese Journal

Aspergillus属菌とRhizopus属菌の混合液体培養におけるグルコアミラーゼおよびα-アミラーゼ生産の増強

日本食品工学会誌 = Japan journal of food engineering 16(2), 111-121,123, 2015-06
NAID 40020514440

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

Tetrahedron 71(9), 1419-1424, 2015-03-04
NAID 120005595709

Screening of accurate clones for gene synthesis in yeast(GENETICS, MOLECULAR BIOLOGY, AND GENE ENGINEERING)

Journal of bioscience and bioengineering 119(3), 251-259, 2015-03
NAID 110009923563

Related Pictures

★リンクテーブル★

リンク元	「グルコアミラーゼ」「glucan 1,4-alpha-glucosidase」

「グルコアミラーゼ」

Search
PMC	articles
PubMed	articles
NCBI	proteins

Glucan 1,4-alpha-glucosidase
Identifiers
EC number	3.2.1.3
CAS number	9032-08-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: glucoamylase
関: グルカン-1,4-αグルコシダーゼ

「glucan 1,4-alpha-glucosidase」

　　[★]

グルカン-1

関: glucoamylase

[1] French, D. and Knapp, D.W. (1950). "The maltase of Clostridium acetobutylicum". J. Biol. Chem. 187: 463–471. PMID 14803428.

[2] Illingworth Brown, B. and Brown, D.H. (1965). "The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues". Biochim. Biophys. Acta 110: 124–133. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.

[3] Jeffrey, P.L., Brown, D.H. and Brown, B.I. (1970). "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry 9: 1403–1415. doi:10.1021/bi00808a015. PMID 4313883.

[4] Kelly, J.J. and Alpers, D.H. (1973). "Properties of human intestinal glucoamylase". Biochim. Biophys. Acta 315: 113–122. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.

[5] Miller, K.D. and Copeland, W.H. (1956). "A blood trans-α-glucosylase". Biochim. Biophys. Acta 22: 193–194. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.

[6] Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. (1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature 181: 770–771. doi:10.1038/181770a0. PMID 13517301.

匿名

検索

案内

案内

glucoamylase