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The role of carbohydrate binding module cooperation in BaAmy7 hydrolysis of resistant starch

Award Number: F31AT011282
ORGANIZATION: CENTER FOR DRUG EVALUATION AND RESEARCH, NIH
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: FELLOWSHIP/SCHOLARSHIP/STUDENT LOANS
PERIOD OF PERFORMANCE START DATE: 01/01/2021
PERIOD OF PERFORMANCE END DATE: 12/31/2022

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The role of carbohydrate binding module cooperation in BaAmy7 hydrolysis of resistant starch - The gut microbiota plays a major role in colonic health and homeostasis. The growth of beneficial bacteria can be promoted by the administration of prebiotics in the human diet. Resistant starch is a prebiotic that preferentially promotes the growth of specialized bacteria, including Bifidobacterium adolescentis. Type 2 resistant starches are raw, granular starches that are inaccessible to most enzymes due to their tightly packed semi-crystalline structure. To break down and utilize resistant starch as a nutrient source, a bacterium must encode proteins that bind to the starch granule components and hydrolyze glycosidic linkages. Starch- specific carbohydrate binding modules (CBMs) are commonly appended to glycoside hydrolase family 13 (GH13) domains, which hydrolyze the glucose linkages in starch. B. adolescentis encodes seven extracellular GH13-containing enzymes including BaAmy7, which is highly active on raw potato and corn starch. BaAmy7 encodes four predicted CBMs, three of which belong to CBM families previously shown to bind raw starch. This proposal aims to understand the mechanism of action of BaAmy7 and how the coordinated effort of these four CBMs permits resistant starch as a substrate. I hypothesize that the binding and proper spatial arrangement of each of the four CBMs is required for maximal catalytic activity. To test this hypothesis, I will (1) dissect the role of individual CBMs in resistant starch hydrolysis by BaAmy7 and (2) elucidate the structural arrangement of BaAmy7 domains. Completion of these aims will lead to a better understanding of the molecular features that set apart BaAmy7 in its ability to hydrolyze resistant starch.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2024 ( Subtotal = $0 )
2024	2022	REGENTS OF THE UNIVERSITY OF MICHIGAN	1109 GEDDES AVE, SUITE 3300	ANN ARBOR	MI	48109	WASHTENAW	USA	Research and Training in Complementary and Integrative Health	000	2	10/31/2023	NON-COMPETING CONTINUATION	$0
														Subtotal = $0

Issue Date FY: 2022 ( Subtotal = $38,665 )
2022	2022	REGENTS OF THE UNIVERSITY OF MICHIGAN	503 THOMPSON ST	ANN ARBOR	MI	48109	WASHTENAW	USA	Research and Training in Complementary and Integrative Health	000	2	1/7/2022	NON-COMPETING CONTINUATION	$38,665
														Subtotal = $38,665

Issue Date FY: 2021 ( Subtotal = $38,149 )
2021	2021	REGENTS OF THE UNIVERSITY OF MICHIGAN	503 THOMPSON ST	ANN ARBOR	MI	48109	WASHTENAW	USA	Research and Training in Complementary and Integrative Health	000	1	12/1/2020	NEW	$38,149
2021	2021	REGENTS OF THE UNIVERSITY OF MICHIGAN	503 THOMPSON ST	ANN ARBOR	MI	48109	WASHTENAW	USA	Research and Training in Complementary and Integrative Health	001	1	12/1/2020	NEW	$0
														Subtotal = $38,149

Grand Total All Awards = $76,814

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The role of carbohydrate binding module cooperation in BaAmy7 hydrolysis of resistant starch

Award Number: F31AT011282

ORGANIZATION: CENTER FOR DRUG EVALUATION AND RESEARCH, NIH

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: FELLOWSHIP/SCHOLARSHIP/STUDENT LOANS

PERIOD OF PERFORMANCE START DATE: 01/01/2021

PERIOD OF PERFORMANCE END DATE: 12/31/2022

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