| 词条 | Lactocepin |
| 释义 |
| Name = Lactocepin | EC_number = 3.4.21.96 | CAS_number = 205510-58-3 | IUBMB_EC_number = 3/4/21/96 | GO_code = | image = | width = | caption = }}Lactocepin ({{EC number|3.4.21.96}}, CEP, extracellular lactococcal proteinase, lactococcal cell wall-associated proteinase, lactococcal cell envelope-associated proteinase, lactococcal proteinase, PrtP) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction Endopeptidase activity with very broad specificity, although some subsite preferences have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position [1,2]. Best known for its action on caseins, although it has been shown to hydrolyse hemoglobin and oxidized insulin B chain This enzyme is associated with the cell envelope of Lactococcus lactis and attached via a C-terminal membrane anchor sequence. References1. ^{{cite journal | title = Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine β-casein | vauthors = Visser S, Robben AJ, Slangen CJ |journal = Appl. Microbiol. Biotechnol. |year = 1991 |volume = 35 |issue = 4 |pages = 477–483 |pmid = 1367552 |doi=10.1007/bf00169753}} 2. ^{{cite journal | vauthors = Exterkate FA, Alting AC, Bruinenberg PG | title = Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region | journal = Applied and Environmental Microbiology | volume = 59 | issue = 11 | pages = 3640–7 | date = November 1993 | pmid = 8285671 | pmc = 182510 }} 3. ^{{cite journal | vauthors = Pritchard GG, Coolbear T | title = The physiology and biochemistry of the proteolytic system in lactic acid bacteria | journal = FEMS Microbiology Reviews | volume = 12 | issue = 1-3 | pages = 179–206 | date = September 1993 | pmid = 8398214 | doi = 10.1111/j.1574-6976.1993.tb00018.x }} External links
1 : EC 3.4.21 |
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