Document Detail


Specificity for various imino-acid-residues of a proline-specific dipeptidylcarboxypeptidase from a Streptomyces species.
MedLine Citation:
PMID:  8448197     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
S Maruyama; S Miyoshi; G Nomura; M Suzuki; H Tanaka; H Maeda
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1162     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1993 Mar 
Date Detail:
Created Date:  1993-04-13     Completed Date:  1993-04-13     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  72-6     Citation Subset:  IM    
Affiliation:
Fermentation Research Institute, Agency of Industrial Science and Technology, Ibaraki, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Carboxypeptidases / isolation & purification,  metabolism*
Endopeptidases / isolation & purification,  metabolism*
Hydrolysis
Imino Acids / metabolism*
Molecular Sequence Data
Peptide Biosynthesis
Peptides / metabolism
Proline / metabolism*
Stereoisomerism
Streptomyces / enzymology*
Substrate Specificity
Chemical
Reg. No./Substance:
0/Imino Acids; 0/Peptides; 147-85-3/Proline; EC 3.4.-/Carboxypeptidases; EC 3.4.-/Endopeptidases; EC 3.4.15.-/proline-specific dipeptidylcarboxypeptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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