about
The loop structure of Actinomycete glycoside hydrolase family 5 mannanases governs substrate recognitionPurification and characterization of a chloride ion-dependent α-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis).Efficient synthesis of α-galactosyl oligosaccharides using a mutant Bacteroides thetaiotaomicron retaining α-galactosidase (BtGH97b).Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrateA novel glycoside hydrolase family 97 enzyme: Bifunctional β-l-arabinopyranosidase/α-galactosidase from Bacteroides thetaiotaomicron.Two Novel Glycoside Hydrolases Responsible for the Catabolism of Cyclobis-(1→6)-α-nigerosyl.Effects of mutation of Asn694 in Aspergillus niger α-glucosidase on hydrolysis and transglucosylation.Production of 1,5-anhydro-d-fructose by an α-glucosidase belonging to glycoside hydrolase family 31.Functional characterization of UDP-rhamnose-dependent rhamnosyltransferase involved in anthocyanin modification, a key enzyme determining blue coloration in Lobelia erinus.Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe.Amino acids in conserved region II are crucial to substrate specificity, reaction velocity, and regioselectivity in the transglucosylation of honeybee GH-13 α-glucosidases.Aromatic residue on β→α loop 1 in the catalytic domain is important to the transglycosylation specificity of glycoside hydrolase family 31 α-glucosidaseKey aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substratesEnzymatic synthesis of Acarviosyl-maltooligosaccharides using disproportionating enzyme 1Kinetic properties and substrate inhibition of α-galactosidase from Aspergillus nigerEngineered dextranase from Streptococcus mutans enhances the production of longer isomaltooligosaccharidesNovel α-1,3/α-1,4-Glucosidase from Aspergillus niger Exhibits Unique Transglucosylation to Generate High Levels of Nigerose and Kojibiose
P50
Q27701764-5953D170-2511-49E4-9EC1-31A06E4C2560Q35863232-AE5ADCFA-BF17-4DE1-8C11-3490CD5A50C4Q38289362-09520B8E-D63C-4B27-9820-BCF8372846ABQ38302644-D0C88464-109F-4C28-9051-278107C8A3EAQ38627041-D7F54406-6305-489D-97C6-9010583C2869Q41775071-F96A9500-B2DA-4727-8F7D-C98C2D1C846DQ46674980-A5E5CCE6-1370-43D9-A7F3-54FB21F4F57CQ46816597-265066A9-85EF-47CA-922D-9BFC5D309226Q47857576-91A70350-2169-4298-92B2-1A2548745DB5Q51020900-10D13EAF-833D-4EE5-B262-B86099B62BC8Q52744655-CECF0740-D59D-402B-B62B-F07A1C6CEF83Q57752195-5D4D8730-4093-4525-B2E8-9CCB3095B2E1Q59462201-303C9A8F-A9E7-4337-B2DF-70D635A3E958Q86080363-C6A8E5D6-2D3A-40A4-8CF5-BD188084BF87Q87250054-38C139F4-7FEA-47E8-9429-AD2FE65D0CA6Q88880674-0987F979-ADFD-482C-BFDC-08B0535DA1C1Q91929202-309CA11F-5133-4FA6-ACBB-37A28A4DD4A1
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Takayoshi Tagami
@en
Takayoshi Tagami
@nl
type
label
Takayoshi Tagami
@en
Takayoshi Tagami
@nl
prefLabel
Takayoshi Tagami
@en
Takayoshi Tagami
@nl
P31
P496
0000-0002-4004-1558