Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit

Journal of Nutrition

Volumn 138, Issue 4, 2008, Pages 685-692

  Quezada Calvillo, Roberto ^a,b,c   Sim, Lyann ^d,e   Ao, Zihua ^f   Hamaker, Bruce R ^f   Quaroni, Andrea ^g   Brayer, Gary D ^h   Sterchi, Erwin E ⁱ   Robayo Torres, Claudia C ^b,c   Rose, David R ^d,e   Nichols, Buford L ^b,c  

^a UNIVERSIDAD AUTÓNOMA DE SAN LUIS POTOSÍ   (Mexico)

^b CHILDREN S NUTRITION RESEARCH CENTER   (United States)

^c BAYLOR COLLEGE OF MEDICINE   (United States)

^d UNIVERSITY OF TORONTO   (Canada)

^e PRINCESS MARGARET HOSPITAL   (Canada)

^f PURDUE UNIVERSITY   (United States)

^g Department of Obstetrics Gynecology   (United States)

^h UNIVERSITY OF BRITISH COLUMBIA   (Canada)

ⁱ UNIVERSITY OF BERN   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ACARBOSE; ALPHA GLUCOSIDASE; GLUCAN; GLUCAN 1,4 ALPHA GLUCOSIDASE; GLUCOSE; MALTODEXTRIN; MALTOPENTOSE; MALTOSE; OLIGOMER; STARCH; SUCRASE ISOMALTASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOHYDRATE METABOLISM; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; GLUCOGENESIS; HUMAN; HYDROLYSIS; IMMUNOCHEMISTRY; MUCOSA; PROTEIN FUNCTION; STRUCTURE ACTIVITY RELATION;

EID: 41549159900     PISSN: 00223166     EISSN: 15416100     Source Type: Journal    
DOI: 10.1093/jn/138.4.685     Document Type: Article

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