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Literature summary for 1.14.99.53 extracted from

  • Bissaro, B.; Isaksen, I.; Vaaje-Kolstad, G.; Eijsink, V.; Rohr, A.
    How a lytic polysaccharide monooxygenase binds crystalline chitin (2018), Biochemistry, 57, 1893-1906 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics interactions between the LPMO and three different surface topologies of crystalline chitin. Most enzyme-substrate interactions involve the polysaccharide chain that is to be cleaved. Enzyme displays a constrained active site geometry as well as a tunnel connecting the bulk solvent to the copper site, through which only small molecules such as H2O, O2, and H2O2 can diffuse. Rearrangement of Cu-coordinating water molecules is necessary when binding the substrate and also provide a rationale for the experimentally observed C1 oxidative regiospecificity Serratia marcescens

Protein Variants

Protein Variants Comment Organism
Y54A mutation of residue at subsite -4, minimal effect on degradation of beta-chitin, about 20% residual activity with substrate [(1->4)-N-acetyl-beta-D-glucosaminyl]6 Serratia marcescens

Metals/Ions

Metals/Ions Comment Organism Structure
copper
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Serratia marcescens

Organism

Organism UniProt Comment Textmining
Serratia marcescens O83009 chitinase, cf. EC 3.2.1.14
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-chitin + ascorbate + O2
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Serratia marcescens C1-oxidized chitooligosaccharides + dehydroascorbate + H2O
-
?
additional information [(1->4)-N-acetyl-beta-D-glucosaminyl]6 is a substrate, but not shorter oligomers Serratia marcescens ?
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?
[(1->4)-N-acetyl-beta-D-glucosaminyl]6 + ascorbate + O2
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Serratia marcescens [(1->4)-N-acetyl-beta-D-glucosaminyl]3-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]2 + dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
AA10A
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Serratia marcescens
CBP21
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Serratia marcescens