| Characterization and kinetic analysis of enzyme-substrate recognition by three recombinant lactococcal tripeptidases. | |
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MedLine Citation:
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PMID: 15752689 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Tripeptidases from Lactococcus lactis subsp. lactis (L9PepTR), L. lactis subsp. cremoris (L6PepTR), and L. lactis subsp. hordniae (hTPepTR) were cloned, overexpressed, purified, and characterized. Although these enzymes contained three to seven naturally occurring amino acid differences, both metal-binding and catalytic sites were highly conserved. The k(cat) values of hTPepTR were approximately 1.5- to 2-fold higher than those of L9PepTR, while, for L6PepTR, they were approximately 0.8- to 1.4-times the L9PepTR values. The K(m) of tripeptidase from subsp. lactis (L9PepTR) was considerably larger when glycine was the amino acid located at both the N- and C-terminus of the peptide substrate. In addition, the K(m) values of L9PepTR increased in the following order for YGG, LGG, FGG, SGG, and alpha-aminoisobutyrylglycylglycine, while the k(cat)/K(m) decreased in the same order. These results suggest that the dipole moment and steric hindrance of the N-terminal amino acid side chain may be the most important factors controlling substrate specificity. |
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Authors:
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Sumiko Mori; Satoru Nirasawa; Shiro Komba; Takafumi Kasumi |
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Publication Detail:
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Type: Journal Article Date: 2005-01-21 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1748 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2005 Apr |
Date Detail:
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Created Date: 2005-03-08 Completed Date: 2005-04-28 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 26-34 Citation Subset: IM |
Affiliation:
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National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Aminopeptidases / chemistry, genetics, metabolism* Bacterial Proteins / chemistry, genetics, metabolism* Hydrogen-Ion Concentration Lactococcus lactis / enzymology* Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Recombinant Proteins / chemistry, genetics, metabolism* Sequence Alignment Substrate Specificity Temperature |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Recombinant Proteins; EC 3.4.11.-/Aminopeptidases; EC 3.4.11.14/PepT tripeptidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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