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Literature summary for 1.14.99.53 extracted from

  • Gregory, R.C.; Hemsworth, G.R.; Turkenburg, J.P.; Hart, S.J.; Walton, P.H.; Davies, G.J.
    Activity, stability and 3-D structure of the Cu(II) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens (2016), Dalton Trans., 45, 16904-16912.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus amyloliquefaciens

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of the copper active site Bacillus amyloliquefaciens

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Cu(II) binds with KD value 43 nM at pH 5. The coordination geometry around the copper is distorted from axial symmetry Bacillus amyloliquefaciens
Zn2+ may substitue for Cu2+. KD value 0.0081 mM at pH 5 Bacillus amyloliquefaciens

Organism

Organism UniProt Comment Textmining
Bacillus amyloliquefaciens
-
-
-
Bacillus amyloliquefaciens DSM 7
-
-
-

Purification (Commentary)

Purification (Comment) Organism
improved expression and purification protocol using Champion pET-SUMO vector, yielding high purity AA10 with yields in excess of 9 mg of protein per litre of culture Bacillus amyloliquefaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-chitin + acceptor + O2
-
Bacillus amyloliquefaciens oligosaccharide aldonic acids + reduced acceptor + H2O
-
?
alpha-chitin + acceptor + O2
-
Bacillus amyloliquefaciens DSM 7 oligosaccharide aldonic acids + reduced acceptor + H2O
-
?
beta-chitin + acceptor + O2 beta chitin from squid pen, best substrate Bacillus amyloliquefaciens oligosaccharide aldonic acids + reduced acceptor + H2O strong preference towards even-numbered products ?
beta-chitin + acceptor + O2 beta chitin from squid pen, best substrate Bacillus amyloliquefaciens DSM 7 oligosaccharide aldonic acids + reduced acceptor + H2O strong preference towards even-numbered products ?

Synonyms

Synonyms Comment Organism
AA10
-
Bacillus amyloliquefaciens
RBAM17540
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Bacillus amyloliquefaciens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
chitin binding increases the thermal stability of the enzyme by 8.3 degrees, copper binding increases melting temperature by 21.6 degrees. Addition of chitin to the copper-bound enzyme increases thermal stability by additional 3.5 degrees Bacillus amyloliquefaciens
68.7
-
melting temperature, presence of both copper and chitin Bacillus amyloliquefaciens