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Organophosphorus acid anhydrolase OPAA

In addition to phosphotriesterase from P. diminuta (PTE) discussed above, two other types of enzymes were found to exhibit phosphotriesterase activity. Interestingly, both are peptidases - the enzymes which in nature hydrolyse a peptide bond. The first one - organophosphorus acid anhydrolase (OPAA) from Alteromonas sp. JD6.5 - is a proline dipeptidase its original activity is to cleave a dipepfide bond with a prolyl residue at the carboxy terminus. The second one - aminopeptidase P (AMPP) from Escherichia coli - is a proline-specific peptidase that catalyses hydrolysis of N-terminal peptide bonds containing a proline residue. ° ... [Pg.195]

See other pages where Organophosphorus acid anhydrolase OPAA is mentioned: [Pg.136]    [Pg.233]    [Pg.234]    [Pg.250]    [Pg.93]    [Pg.136]    [Pg.233]    [Pg.234]    [Pg.250]    [Pg.93]    [Pg.78]    [Pg.1042]   
See also in sourсe #XX -- [ Pg.767 , Pg.1042 , Pg.1043 ]



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ORGANOPHOSPHORUS

Organophosphorus acid anhydrolases

Organophosphorus acids

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