Probing Enzyme Promiscuity of SGNH Hydrolases (pages 2158–2167)
Dr. Ivana Leščić Ašler, Nives Ivić, Dr. Filip Kovačić, Dr. Sabrina Schell, Dr. Janina Knorr, Dr. Ulrich Krauss, Dr. Susanne Wilhelm, Dr. Biserka Kojić-Prodić and Prof. Dr. Karl-Erich Jaeger
Article first published online: 7 OCT 2010 | DOI: 10.1002/cbic.201000398
Absolute activities [U mg−1] of SGNH hydrolases against selected substrates—p-nitrophenyl butyrate (esterase activity), p-nitrophenyl palmitate (lipase), diheptanoyl glycerophosphocholine (phospholipase B) and thioesterase (palmitoyl-coenzyme A)—were studied. SrLip and EstPN were found to be much more active than the other enzymes (and so their activities are expressed as one tenth of the measured activities).