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

Thermophilic l-arabinose isomerase (AI), which catalyzes the interconversion of l-arabinose and l-ribulose, can be used to produce d-tagatose, a sugar substitute, from d-galactose. Unlike mesophilic AIs, thermophilic AIs are highly dependent on divalent metal ions for their catalytic activity and th...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2016-04, Vol.596, p.51-62
Hauptverfasser:	Choi, Jin Myung, Lee, Yong-Jik, Cao, Thinh-Phat, Shin, Sun-Mi, Park, Min-Kyu, Lee, Han-Seung, di Luccio, Eric, Kim, Seong-Bo, Lee, Sang-Jae, Lee, Sang Jun, Lee, Sung Haeng, Lee, Dong-Woo
Format:	Artikel
Sprache:	eng
Schlagworte:	Aldose-Ketose Isomerases - chemistry Bacterial Proteins - chemistry Crystal structure Crystallography, X-Ray Enzyme Stability Geobacillus - enzymology Hot Temperature Hydrogen Bonding Intersubunit interaction l-arabinose isomerase Manganese - chemistry Protein Structure, Quaternary Substrate specificity Thermostability
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