Aminopeptidases A, B, and N and Dipeptidase D Are the Four Cysteinylglycinases of Escherichia coli K-12

Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12.

Aminopeptidases A, B, and N and dipeptidase D, with broad substrate specificity, are the four cysteinylglycinases of Escherichia coli K-12, and there is no peptidase specific for the cleavage of cysteinylglycine.

the investigation of the relationship between type a and type b personalities and quality of translation

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Purification and properties of dipeptidase M from Escherichia coli B.

A peptidase from Escherichia coli B has been prepared in a highly pure form and characterized with respect to its substrate specificity, requirements for activity, size and subunit structure. This enzyme preferentially catalyzes the hydrolysis of certain methionyl dipeptides and for this reason is referred to as dipeptidase M. Of the substrates tested with the homogeneous enzyme methionylalanin...

The D-allose operon of Escherichia coli K-12.

Escherichia coli K-12 can utilize D-allose, an all-cis hexose, as a sole carbon source. The operon responsible for D-allose metabolism was localized at 92.8 min of the E. coli linkage map. It consists of six genes, alsRBACEK, which are inducible by D-allose and are under the control of the repressor gene alsR. This operon is also subject to catabolite repression. Three genes, alsB, alsA, and al...

The beta-d-galactosidase of Escherichia coli, strain K-12.