Kinetic evidence for surface residues influencing the active site of Coprinus cinereus peroxidase: analysis of the pH dependence of G154E, P90H and P90H-G154E substrate entrance mutants.

doi:10.1016/s0167-4838(00)00201-6

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Article

Kinetic evidence for surface residues influencing the active site of Coprinus cinereus peroxidase: analysis of the pH dependence of G154E, P90H and P90H-G154E substrate entrance mutants.

Biochimica et biophysica acta - 12 Jan 2001

Di Cerbo P, Welinder K G, Schiødt C B

Abstract excerpt

Three mutants of Coprinus cinereus peroxidase (CIP) were made to mimic the substrate entrance histidine 82-glutamic acid 146 pair of the substrate channel in lignin peroxidase (LIP). Compound I formation of LIP has a low pH optimum around pH 3, while optimal formation of CIP compound I is obtained at pH 6-11. The mutants were glycine 154-->glutamic acid (G154E), proline 90-->histidine (P90H) and the double mutant...

Topics

Binding Sites
Coprinus
Enzyme Stability
Heme
Hydrogen Peroxide
Kinetics
Mutation
Peroxidases
Substrate Specificity

Source

Open in PubMed

Identifiers

PMID: 11341913
DOI: 10.1016/s0167-4838(00)00201-6

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