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Literature summary for 3.4.24.40 extracted from

  • Oberholzer, A.E.; Bumann, M.; Hege, T.; Russo, S.; Baumann, U.
    Metzincins canonical methionine is responsible for the structural integrity of the zinc-binding site (2009), Biol. Chem., 390, 875-881.
    View publication on PubMed
Search for more literature for 3.4.24.40

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Dickeya chrysanthemi

Protein Variants

Protein Variants Comment Organism
M226A using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants Dickeya chrysanthemi
M226A/E189A introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain Dickeya chrysanthemi
M226H mutant could not be purified, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants Dickeya chrysanthemi
M226H/E189A introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain Dickeya chrysanthemi
M226I M226I possesses 50% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants Dickeya chrysanthemi
M226I/E189A introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain Dickeya chrysanthemi
M226L M226L possesses 85% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants Dickeya chrysanthemi
M226L/E189A introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain Dickeya chrysanthemi
M226N mutant could not be purified Dickeya chrysanthemi
M226N/E189A introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain Dickeya chrysanthemi

Organism

Organism UniProt Comment Textmining
Dickeya chrysanthemi
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-
-

Synonyms

Synonyms Comment Organism
protease C
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 Dickeya chrysanthemi
PrtC
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 Dickeya chrysanthemi