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X‐ray characterisation of an additional binding site in lysozyme
Author(s) -
Veerapandian B.,
Salunke D.M.,
Vijayan M.
Publication year - 1985
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(85)80701-8
Subject(s) - lysozyme , peptidoglycan , muramidase , binding site , bacterial cell structure , chemistry , ribonuclease , cell wall , biochemistry , peptide , enzyme , site of action , biophysics , biology , bacteria , rna , gene , genetics , endocrinology
Bromophenol red (BPR) binds to lysozyme and inhibits its activity against bacterial cell walls, but not against the polysaccharide component of peptidoglycan. The binding site of BPR in the enzyme has been characterised by X‐ray analysis of the complex at 5.5Å resolution. The new binding site, which is outside the cleft close to subsite F, is presumably involved in interactions with the peptide component of peptidoglycan, in the action of lysozyme against bacterial cell walls.