Specificity for various imino-acid-residues of a proline-specific dipeptidylcarboxypeptidase from a Streptomyces species.
A proline-specific dipeptidylcarboxypeptidase, which removes diproline from the C-terminus of the proline-containing peptides, such as Boc-Pro-Pro-Pro-Pro and Leu-Pro-Pro-Pro-Pro-Pro, has recently been purified from a Streptomyces sp. The specificity of the enzyme for various imino acid-containing synthetic peptide substrates was further studied. The peptides with proline, hydroxyproline, or dehydroproline at the P2' position were found to be good substrates, while those with pipecolic acid, D-proline or other usual amino acids at the P2' position were scarcely hydrolyzed. The peptides with proline, dehydroproline, pipecolic acid, or N-methyl-alanine at the P1' position were well-hydrolyzed, while those with hydroxyproline or D-proline at the P1' position were not hydrolyzed. Utilizing this high specificity for imino acids, Boc-Pro-Pro-Pro-Pro was synthesized by the enzyme using Boc-Pro-Pro as the acidic component and Pro-Pro as the basic component.
Maruyama
S
S
Fermentation Research Institute, Agency of Industrial Science and Technology, Ibaraki, Japan.
Miyoshi
S
S
Nomura
G
G
Suzuki
M
M
Tanaka
H
H
Maeda
H
H
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D007098:Imino Acids / Q000378:metabolism*; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000378:metabolism; D011392:Proline / Q000378:metabolism*; D013237:Stereoisomerism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D007098:Imino Acids; D010455:Peptides; D011392:Proline; D002268:Carboxypeptidases; D010450:Endopeptidases; C080173:proline-specific dipeptidylcarboxypeptidase