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090			_aB-12616
245	1	0	_aWhat distinguishes an esterase from a lipase: A novel structural approach
490	0		_vBiochimie, 82(11), p.1033-1041, 2000
520	3		_aEsterases and lipases both hydrolyse ester bonds. Whereas the lipases display high activity towards the aggregated state of its substrate, the esterases typically show highest activity towards the soluble state of its substrate. We have compared the amino acid sequence, the 3D-structure as well as the pH-dependent electrostatic signature of selected members of the two families, for which 3D-structural information is publicly available. Lipases display a statistically significant enhanced occurrence of non-polar residues close to the surface, clustering around the active-site. Lid opening appears to strengthen this pattern further. As we have proposed earlier the active site of lipases displays negative potential in the pH-range associated with their maximum activity, typically at pH values above 8. The esterases show a very similar pattern, however, at pH values around 6 correlated with their usually lower pH-activity optimum.
650	1	4	_aESTERASES
650	1	4	_aLIPASES
650	1	4	_aPROTEIN ELECTROSTATICS
650	1	4	_aSEQUENCE ANALYSIS
700	1	2	_aFojan, P.
700	1	2	_aJonson, P.H.
700	1	2	_aPetersen, M.T.N.
700	1	2	_aPetersen, S.B.
856	4	0	_uhttps://drive.google.com/file/d/1rxZLgS4yuvMfY3aTZPyxP4mAhJ8NcEP_/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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