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The Biochemical Journal|February 15, 1990
Theoretical approach to the steady-state kinetics of a bi-substrate acyl-transfer enzyme reaction that follows a hydrolysable-acyl-enzyme-based mechanism. Application to the study of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lungJ Martín, J Pérez-Gil, C Acebal, et al.
The Biochemical Journal|September 15, 1990
Chemical mechanism of lysophosphatidylcholine: lysophosphatidylcholine acyltransferase from rabbit lung. pH-dependence of kinetic parametersJ Pérez-Gil, J Martín, C Acebal, et al.
International Journal of Peptide and Protein Research|May 1, 1984
Lysolecithin:lysolecithin acyltransferase from rabbit lung. A conformational studyR Arche, C Acebal, C Casals, et al.
The Biochemical Journal|December 15, 1991
Chemical modification of serine at the active site of penicillin acylase from Kluyvera citrophilaJ Martín, A Slade, A Aitken, et al.
Archives of Biochemistry and Biophysics|February 15, 1990
Essential residues in lysolecithin:lysolecithin acyltransferase from rabbit lung: assessment by chemical modificationJ Pérez-Gil, J J Martín, C Acebal, et al.
Biotechnology and Applied Biochemistry|June 1, 1993
pH studies to elucidate the chemical mechanism of penicillin acylase from Kluyvera citrophilaJ Martín, I Prieto, J M Mancheño, et al.
Biochemistry International|April 1, 1989
Evidence of a pH-dependent conformational change at the active site of lysolecithin:lysolecithin acyltransferase from rabbit lungJ Pérez-Gil, J J Martín, J M Mancheño, et al.
Applied Microbiology and Biotechnology|August 1, 1990
Penicillin acylase mutants with altered site-directed activity from Kluyvera citrophilaI Prieto, J Martín, R Arche, et al.
Biochimica Et Biophysica Acta|February 9, 1990
Thermodynamic profiles of penicillin G hydrolysis catalyzed by wild-type and Met----Ala168 mutant penicillin acylases from Kluyvera citrophilaJ Martín, I Prieto, J L Barbero, et al.
Mbio|March 14, 2019
Glycolysis Is an Intrinsic Factor for Optimal Replication of a NorovirusKarla D Passalacqua, Jia Lu, Ian Goodfellow, et al.
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