Document Detail

Characterization and kinetic analysis of enzyme-substrate recognition by three recombinant lactococcal tripeptidases.
MedLine Citation:
PMID:  15752689     Owner:  NLM     Status:  MEDLINE    
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.
Sumiko Mori; Satoru Nirasawa; Shiro Komba; Takafumi Kasumi
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Publication Detail:
Type:  Journal Article     Date:  2005-01-21
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1748     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-03-08     Completed Date:  2005-04-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  26-34     Citation Subset:  IM    
National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan.
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MeSH Terms
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
Reg. No./Substance:
0/Bacterial Proteins; 0/Recombinant Proteins; EC 3.4.11.-/Aminopeptidases; EC tripeptidase

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

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