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release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
active site structure involving His97, Asp117, Asp179, Glu151, Glu152, and His256
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release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
presence of at least one active Tyr and one carboxyl group demonstrated by chemical modifications of enzyme: nitration, azotization, diethyldirocarbonate treatment, 1-ethyl-3(3-dimethylaminopropyl)-carbodiimide treatment
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
mechanism. Substrate only binds to the first metal binding site
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
catalytic mechanism
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
catalytic mechanism
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure and mechanism
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
substrate binding mechanism and structure
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism involving divalent metal ions, overview
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
active site structure, reaction mechanism involving the two zinc ions
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Glu354 is essential for Zn2+-binding and catalytic activity, Arg356 is involved in catalysis acting as a general base that accepts a proton and activates the water nucleophile, other active site residues are Lys270, Glu354, ASp352, Lys282, Asp275, and Asp293, mechanism
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Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
residues His345 and His378 play an important role in catalysis
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
structure-activity relationship, active site structure involving zinc-binding ligands His97, Asp117, Asp179, Glu151, Glu152, and His256
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