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Literature summary for 3.2.1.17 extracted from

  • Goto, T.; Ohkuri, T.; Shioi, S.; Abe, Y.; Imoto, T.; Ueda, T.
    Crystal structures of K33 mutant hen lysozymes with enhanced activities (2008), J. Biochem., 144, 619-623.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae Gallus gallus

Crystallization (Commentary)

Crystallization (Comment) Organism
mutants K33A and K33N. The side chain of K33 in wild-type hydrogen bonds with N37 involved in the substrate-binding region. Orientation of N37 differs in mutants K33A and K33N Gallus gallus

Protein Variants

Protein Variants Comment Organism
K33A 140% of wild-type lytic activity, 116% of wild-type activity on glycol chitin Gallus gallus
K33N 130% of wild-type lytic activity, 111% of wild-type activity on glycol chitin Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus P00698
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycol chitin + H2O
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Gallus gallus ?
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?
additional information measurement of activity by lytic activity against Micrococcus luteus Gallus gallus ?
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?