Zobrazeno 1 - 10
of 21
pro vyhledávání: '"E. Ann MacGregor"'
Publikováno v:
Janeček, Š, Majzlová, K, Svensson, B & MacGregor, E A 2017, ' The starch-binding domain family CBM41-an in silico analysis of evolutionary relationships : Carbohydrate-binding module family 41 ', Proteins: Structure, Function, and Bioinformatics, vol. 85, no. 8, pp. 1480-1492 . https://doi.org/10.1002/prot.25309
Within the CAZy database, there are 81 carbohydrate-binding module (CBM) families. A CBM represents a non-catalytic domain in a modular arrangement of glycoside hydrolases (GHs). The present in silico study has been focused on starch-binding domains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa3de5db6ba8ce1dd9614b542e5633f4
https://doi.org/10.1002/prot.25309
https://doi.org/10.1002/prot.25309
Publikováno v:
Biotechnology advances. 37(8)
The term "starch-binding domain" (SBD) has been applied to a domain within an amylolytic enzyme that gave the enzyme the ability to bind onto raw, i.e. thermally untreated, granular starch. An SBD is a special case of a carbohydrate-binding domain, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a27c33f4f124c0be5d4b0bcebd5363a
https://pubmed.ncbi.nlm.nih.gov/31536775
https://pubmed.ncbi.nlm.nih.gov/31536775
Publikováno v:
Proteins. 85(8)
Within the CAZy database, there are 81 carbohydrate-binding module (CBM) families. A CBM represents a non-catalytic domain in a modular arrangement of glycoside hydrolases (GHs). The present in silico study has been focused on starch-binding domains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a1e476e47d5b9830a067fa761d81be06
https://pubmed.ncbi.nlm.nih.gov/28425599
https://pubmed.ncbi.nlm.nih.gov/28425599
Publikováno v:
FEBS Journal. 272:5497-5513
Approximately 10% of amylolytic enzymes are able to bind and degrade raw starch. Usually a distinct domain, the starch-binding domain (SBD), is responsible for this property. These domains have been classified into families of carbohydrate-binding mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e189e4a4ea33a05ede1784a31d59e14
https://doi.org/10.1111/j.1742-4658.2005.04942.x
https://doi.org/10.1111/j.1742-4658.2005.04942.x
Publikováno v:
European Journal of Biochemistry. 270:635-645
The alpha-amylase family (glycoside hydrolase family 13; GH 13) contains enzymes with approximately 30 specificities. Six types of enzyme from the family can possess a C-terminal starch-binding domain (SBD): alpha-amylase, maltotetraohydrolase, malto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3d2feff92108d28218b84bd15be08b4
https://doi.org/10.1046/j.1432-1033.2003.03404.x
https://doi.org/10.1046/j.1432-1033.2003.03404.x
Autor:
E. Ann MacGregor
Publikováno v:
Journal of Protein Chemistry. 21:297-306
A group of enzymes that include muscle glycogen phosphorylase and sugar transferases involved in, for example, the glucosylation of DNA and the synthesis of peptidoglycan are known to possess the same basic three-dimensional fold. Here the possibilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6e739cfa2a30a0af9d6b15f86e924a3
https://doi.org/10.1023/a:1019701621256
https://doi.org/10.1023/a:1019701621256
Publikováno v:
Carbohydrate Research. 313:139-143
The action of barley malt alpha-amylase 2 (E.C. 3.2.1.1) on p-nitrophenyl derivatives of maltodextrins was studied at pH 4.8, 6.0 and 7.8. Distributions of products from any one substrate changed little with pH, but a difference in behaviour was obse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0188550569db27166056967483a952bc
https://doi.org/10.1016/s0008-6215(98)00228-6
https://doi.org/10.1016/s0008-6215(98)00228-6
Publikováno v:
Journal of Biological Chemistry. 273:11134-11143
A beta-glucosidase, designated isoenzyme betaII, from germinated barley (Hordeum vulgare L.) hydrolyzes aryl-beta-glucosides and shares a high level of amino acid sequence similarity with beta-glucosidases of diverse origin. It releases glucose from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4391fe79f84dd0a8158d9e8e05b18cc0
https://doi.org/10.1074/jbc.273.18.11134
https://doi.org/10.1074/jbc.273.18.11134
Autor:
E Ann, MacGregor
Publikováno v:
Annals of internal medicine. 159(9)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e123a81e382c99f8caf4267c6860c82a
https://pubmed.ncbi.nlm.nih.gov/24189604
https://pubmed.ncbi.nlm.nih.gov/24189604
Publikováno v:
Cellular and molecular life sciences : CMLS. 71(7)
α-Amylase (EC 3.2.1.1) represents the best known amylolytic enzyme. It catalyzes the hydrolysis of α-1,4-glucosidic bonds in starch and related α-glucans. In general, the α-amylase is an enzyme with a broad substrate preference and product specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ab013932309b9633dd4a60fea1003ff
https://pubmed.ncbi.nlm.nih.gov/23807207
https://pubmed.ncbi.nlm.nih.gov/23807207