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Volumn 596, Issue , 2016, Pages 51-62

Structure of the thermophilic l-Arabinose isomerase from Geobacillus kaustophilus reveals metal-mediated intersubunit interactions for activity and thermostability

(12) Choi, Jin Myung a Lee, Yong Jik b Cao, Thinh Phat a Shin, Sun Mi b Park, Min Kyu b Lee, Han Seung c Di Luccio, Eric b Kim, Seong Bo d Lee, Sang Jae c Lee, Sang Jun e Lee, Sung Haeng a Lee, Dong Woo b

a Chosun University College of Medicine (South Korea)

b Kyungpook National University (South Korea)

c Silla University (South Korea)

d CJ Corporation (South Korea)

e Korea Research Institute of Bioscience and Biotechnology (KRIBB) (South Korea)

Author keywords

Crystal structure; Intersubunit interaction; l arabinose isomerase; Substrate specificity; Thermostability

Indexed keywords

ARABINITOL; ARABINOSE ISOMERASE; ISOMERASE; MANGANESE; UNCLASSIFIED DRUG; WATER; BACTERIAL PROTEIN; L-ARABINOSE ISOMERASE;

ARTICLE; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; GEOBACILLUS; GEOBACILLUS KAUSTOPHILUS; HYDROGEN BOND; ISOMERIZATION; METAL BINDING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; THERMOSTABILITY; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; HEAT; PROTEIN QUATERNARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ALDOSE-KETOSE ISOMERASES; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GEOBACILLUS; HOT TEMPERATURE; HYDROGEN BONDING; MANGANESE; PROTEIN STRUCTURE, QUATERNARY;

EID: 84960474733 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2016.02.033 Document Type: Article

Times cited : (30)

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