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3.4.17.12: carboxypeptidase M

This is an abbreviated version!
For detailed information about carboxypeptidase M, go to the full flat file.

Word Map on EC 3.4.17.12

Reaction

cleavage of C-terminal arginine or lysine residues from polypeptides =

Synonyms

carboxypeptidase M, carboxypeptidase-M, CPM, M14006 (Merops-ID), More

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.12 carboxypeptidase M

Engineering

Engineering on EC 3.4.17.12 - carboxypeptidase M

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E260A
-
mutation reduces the ratio of turnover-numver to Km-value by 104fold and further decreases stability.Addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wild-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
E260Q
-
mutation has minimal effects on kinetic parameters, but decreased heat stability
E264Q
S406A
-
very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C
S406P
-
the wild-type and S406A and S406T mutants are expressed on the plasma membrane in glycosylphosphatidylinositol-anchored form, the S406P mutant is not and is retained in a perinuclear location
S406T
-
very similar to the wild-type enzyme with regard to expression and release by phosphatidylinositol-specific phospholipase C