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Alteration of the substrate specificity of human lysozyme by site‐specific intermolecular cross‐linking
Author(s) -
Muraki Michiro,
Jigami Yoshifumi,
Harata Kazuaki
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01168-0
Subject(s) - lysozyme , dimer , chemistry , substrate (aquarium) , monomer , active site , maleimide , oligomer , divalent , chitin , stereochemistry , hydrolase , enzyme , polymer chemistry , polymer , biochemistry , organic chemistry , biology , ecology , chitosan
Human lysozyme dimers were prepared by the intermolecular cross‐linking of the monomer that contained the mutation of either Arg 41 to Cys or Ala 73 to Cys with a divalent maleimide compound. Among the three kinds of possible dimers only R41C–R41C dimer, in which the two catalytic clefts can come close to each other due to the proximity of the conjugation site to the active sites, turned out to be 2.3 times more specific to a polymer substrate, ethylene glycol chitin, as compared to an oligomer substrate, PNP‐(GlcNAc) 5 . The result indicates that it is possible to alter the substrate specificity of an enzyme by artificially controlling the orientation of the active sites.