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Inside Cover: Different Active‐Site Loop Orientation in Serine Hydrolases versus Acyltransferases (ChemBioChem 5/2011)
Author(s) -
Jiang Yun,
Morley Krista L.,
Schrag Joseph D.,
Kazlauskas Romas J.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201190016
Subject(s) - active site , oxyanion hole , hydrolase , pseudomonas fluorescens , chemistry , serine , acyltransferases , acyltransferase , esterase , stereochemistry , serine hydrolase , biochemistry , enzyme , biology , biosynthesis , bacteria , genetics
The inside cover picture shows a hydrolysis on–off gate. The oxyanion loop conformation near the active site distinguishes a hydrolase ( Pseudomonas fluorescens esterase) from an acyltransferase (mycolyltransferase from Mycobacterium tuberculosis ). For further details, see the paper by R. J. Kazlauskas et al. on p. 768 ff.