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Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: A member of a new subclass of lipolytic enzymes

โœ Scribed by Ta-hsien Lin; Chinpan Chen; Rong-Fong Huang; Ya-Lin Lee; Jei-Fu Shaw; Tai-huang Huang


Book ID
110260430
Publisher
Springer Netherlands
Year
1998
Tongue
English
Weight
296 KB
Volume
11
Category
Article
ISSN
0925-2738

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## Abstract Owing to the hydrogenโ€bond interaction and rapid exchange rate with the bulk water, the transverse relaxation time for the N^ฮด1^๏ฃฟH proton of the catalytic histidine in __Escherichia coli__ thioesterase I/protease I/lysophospholipase L~1~ (TEPโ€I) is rather short. Because of its catalytic