Change in substrate preference of Streptomyces aminopeptidase through modification of the environment around the substrate binding site

Article Abstract:

Substrate preference of wild-type Streptomyces septatus TH-2 (SSAP) and 38 SSAP variants with the D198X or F221X mutation toward several aminoacyl-p nitroanilides (pNAs) is examined and various D198X / F21X mutants are constructed to transform SSAP into an amnopeptidase with a different substrate preference. The examination provided two enzymes, one specifically hydrolyzed an arginyl derivative, and the other specifically hydrolyzed a cystinyl derivative.

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Dipeptide synthesis by an aminopeptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides

Article Abstract:

Dipeptide synthesis by aminopeptidase from Streptomyces septatus TH-2 (SSAP) was demonstrated using free amino acid as an acyl donor and aminoacyl methyl ester as an acyl acceptor in 98% methanol (MeOH). In an investigation of the specificity of SSAP toward acyl donors and acyl acceptors, SAP showed a broad specificity toward various free amino acids and aminoacyl methyl esters.

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Alteration of leucine aminopeptidase from Streptomyces septatus TH-2 to phenylalanine aminopeptidase by site-directed mutagenesis

Article Abstract:

The feasibility of altering the performance of Streptomyces septatus TH-2 is evaluated by using saturation mutagenesis. The mechanism underlying the alteration in the preference of Streptomyces septatus TH-2 from leucine to phenylalanine is discussed based on a comparative kinetic study.

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