Description
Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4.
Abbr
Aminopeptidase I, Native (Streptomyces griseus)
Source
Streptomyces griseus
Applications
Aminopeptidase I from Streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. It may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. The lyophilized powder also contains calcium acetate.
Form
lyophilized powder. Contains calcium acetate
Enzyme Commission Number
EC 3.4.11.22
Activity
> 200 units/mg protein
Unit Definition
One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0, 25°C and 3.0 mM substrate concentration.
Synonyms
aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I
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