Exploring substrate binding in homoprotocatechuate 2,3-dioxygenase using isothermal titration calorimetry

2012 ◽  
Vol 17 (7) ◽  
pp. 991-994 ◽  
Author(s):  
Kate L. Henderson ◽  
Vu H. Le ◽  
Edwin A. Lewis ◽  
Joseph P. Emerson
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Substrate Binding ◽  
Titration Calorimetry

Alternating Sites Reactivity Is a Common Feature of Thiamin Diphosphate-Dependent Enzymes As Evidenced by Isothermal Titration Calorimetry Studies of Substrate Binding

Biochemistry ◽  
2013 ◽  
Vol 52 (15) ◽  
pp. 2505-2507 ◽  
Author(s):  
Kathrin Schröder-Tittmann ◽  
Danilo Meyer ◽  
Johannes Arens ◽  
Cindy Wechsler ◽  
Michael Tietzel ◽  
...  
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Substrate Binding ◽  
Titration Calorimetry ◽  
Thiamin Diphosphate

scholarly journals Substrate binding properties of potato tuber ADP-glucose pyrophosphorylase as determined by isothermal titration calorimetry

FEBS Letters ◽  
2015 ◽  
Vol 589 (13) ◽  
pp. 1444-1449 ◽  
Author(s):  
Bilal Cakir ◽  
Aytug Tuncel ◽  
Abigail R. Green ◽  
Kaan Koper ◽  
Seon-Kap Hwang ◽  
...  
Keyword(s):  
Potato Tuber ◽  
Isothermal Titration Calorimetry ◽  
Substrate Binding ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Adp Glucose Pyrophosphorylase

scholarly journals Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway

PLoS ONE ◽  
2020 ◽  
Vol 15 (11) ◽  
pp. e0241912
Author(s):  
Masaki Kohno ◽  
Takatoshi Arakawa ◽  
Naoki Sunagawa ◽  
Tetsuya Mori ◽  
Kiyohiko Igarashi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Isothermal Titration Calorimetry ◽  
Molecular Analysis ◽  
Metabolic Pathway ◽  
Binding Protein ◽  
Substrate Binding ◽  
Structural Features ◽  
Titration Calorimetry ◽  
Arthrobacter Globiformis ◽  
Substrate Binding Protein

Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC importer system of the bacteria Arthrobacter globiformis. Isothermal titration calorimetry analysis revealed that CMMBP specifically bound to CMM with a Kd value of 9.6 nM. The crystal structure of CMMBP was determined at a resolution of 1.47 Å, and a panose molecule was bound in a cleft between two domains. To delineate its structural features, the crystal structure of CMMBP was compared with other SBPs specific for carbohydrates, such as cyclic α-nigerosyl-(1→6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.

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