Purification and characterization of a dipeptidase from Lactobacillus sake.
A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10-phenanthroline but could be reactivated with CoCl2 and MnCl2.
Montel
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Station de Recherches sur la Viande, Institut National de la Recherche Agronomique, Saint-Genès Champanelle, France.
Seronie
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MP
Talon
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Hébraud
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D000595:Amino Acid Sequence; D002712:Chlorides / Q000494:pharmacology; D003035:Cobalt / Q000494:pharmacology; D004150:Dipeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification*; D004151:Dipeptides / Q000737:chemistry; D004492:Edetic Acid / Q000494:pharmacology; D007526:Isoelectric Point; D007778:Lactobacillus / Q000201:enzymology*; D017895:Manganese Compounds / Q000494:pharmacology; D008461:Meat Products / Q000382:microbiology; D008970:Molecular Weight; D010618:Phenanthrolines / Q000494:pharmacology; D013379:Substrate Specificity
D002712:Chlorides; D004151:Dipeptides; D017895:Manganese Compounds; D010618:Phenanthrolines; D003035:Cobalt; D004492:Edetic Acid; D004150:Dipeptidases; C018021:cobaltous chloride; C025340:manganese chloride; C025205:1,10-phenanthroline