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Lactococcus lactis is a gram-positive bacterium used extensively in the production of buttermilk and cheese, but has also become famous as the first genetically modified organism to be used alive for the treatment of human disease. L. lactis cells are cocci that group in pairs and short chains, and, depending on growth conditions, appear ovoid with a typical length of 0.5 - 1.5 µm. L. lactis does not produce spores (nonsporulating) and are not motile (nonmotile). They have a homofermentative metabolism, meaning they produce lactic acid from sugars. They've also been reported to produce exclusive L-(+)-lactic acid. However, reported D-(−)-lactic acid can be produced when cultured at low pH. The capability to produce lactic acid is one of the reasons why L. lactis is one of the most important microorganisms in the dairy industry. Based on its history in food fermentation, L. lactis has generally recognized as safe (GRAS) status, with few case reports of it being an opportunistic pathogen.
Dipeptidyl peptidase-4 (DPP4), also known as adenosine deaminase complexing protein 2 or CD26 is a protein that, in humans, is encoded by the DPP4 gene. DPP4 is related to FAP, DPP8, and DPP9. The enzyme was discovered in 1966 by Hopsu-Havu and Glenner, and as a result of various studies on chemism, was called dipeptidyl peptidase IV [DP IV].
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli LAP, and the solanaceous-specific acidic LAP (LAP-A) in tomato.
Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.
Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.
Dipeptidyl peptidase 8 is an enzyme that in humans is encoded by the DPP8 gene.
Xaa-Pro aminopeptidase 1 is an enzyme that in humans is encoded by the XPNPEP1 gene.
Dipeptidyl peptidase 9 is an enzyme that in humans is encoded by the DPP9 gene.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Prolyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Xaa-Pro aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Bacterial leucyl aminopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
PepB aminopeptidase is an enzyme which catalyses the following chemical reaction:
Aminopeptidase S is an enzyme. This enzyme catalyses the following chemical reaction
Dipeptidyl-peptidase II is an enzyme. This enzyme catalyses the following chemical reaction:
Xaa-Xaa-Pro tripeptidyl-peptidase is an enzyme. It catalyses the following chemical reaction
Lysosomal Pro-Xaa carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Membrane Pro-Xaa carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Pyroglutamyl-peptidase II is an enzyme. This enzyme catalyses the following chemical reaction
Ligilactobacillus salivarius is a probiotic bacteria species that has been found to live in the gastrointestinal tract and exert a range of therapeutic properties including suppression of pathogenic bacteria.
References
- ↑ Zevaco C, Monnet V, Gripon JC (1990). "Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties". Journal of Applied Bacteriology. 68 (4): 357–366. doi:10.1111/j.1365-2672.1990.tb02886.x.
- ↑ Meyer-Barton EC, Klein JR, Imam M, Plapp R (October 1993). "Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290". Applied Microbiology and Biotechnology. 40 (1): 82–9. doi:10.1007/bf00170433. PMID 7765315.
- ↑ Habibi-Najafi MB, Lee BH (1994). "Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG". Appl. Microbiol. Biotechnol. 42 (2–3): 280–286. doi:10.1007/s002530050250. PMID 7765768.
- ↑ Chich JF, Gripon JC, Ribadeau-Dumas B (January 1995). "Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents". Analytical Biochemistry. 224 (1): 245–9. doi:10.1006/abio.1995.1036. PMID 7710078.
- ↑ Chich JF, Chapot-Chartier MP, Ribadeau-Dumas B, Gripon JC (December 1992). "Identification of the active site serine of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis". FEBS Letters. 314 (2): 139–42. doi: 10.1016/0014-5793(92)80960-o . PMID 1459244.
