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Literature summary for 1.14.99.53 extracted from

  • Aachmann, F.; Sorlie, M.; Skjak-Brak, G.; Eijsink, V.; Vaaje-Kolstad, G.
    NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions (2012), Proc. Natl. Acad. Sci. USA, 109, 18779-18784.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Serratia marcescens

Crystallization (Commentary)

Crystallization (Comment) Organism
calculation of solution structure. Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ ions show binding to an interaction site located between His28 and His114 Serratia marcescens

Inhibitors

Inhibitors Comment Organism Structure
cyanide mimic of molecular oxygen, binds to the metal ion only Serratia marcescens

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Kd value 55 nM, from isothermal titration calorimetry, and for Cu1+, Kd value 1 nM from the experimentally determined redox potential Serratia marcescens
additional information residues His28 and His114 in the catalytic center bind a variety of divalent metal ions such as Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ with a clear preference for Cu2+ Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens O83009
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitin + acceptor + O2
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 Serratia marcescens ? + reduced acceptor + H2O
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 ?
additional information mechanistic model, copper is reduced on the enzyme by an externally provided electron and followed by oxygen binding and activation by internal electron transfer. Substrate binding involves an extended planar binding surface, including the metal binding site. Chitin binding protects two regions from 2H/1H exchange, Gln53-Ser58 and Leu110-Thr116 Serratia marcescens ?
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 ?

Synonyms

Synonyms Comment Organism
CBP21
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 Serratia marcescens