Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.5.1.86: mandelamide amidase

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

Reaction

(R)-mandelamide
+
H2O
=
(R)-mandelate
+
NH3

Synonyms

amidase, mandelamide, MAH, mandelamide hydrolase, Pseudomonas mandelamide hydrolase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.86 mandelamide amidase

Engineering

Engineering on EC 3.5.1.86 - mandelamide amidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F150L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
F433A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
F433L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type
G202A
-
site-directed mutagenesis. Gly202 appears to control the preference for aromatic substrates as the G202A variant shows three orders of magnitude decrease in kcat/Km for (R)- and (S)-mandelamide
G202A/Q207H/Q382E
-
site-directed mutagenesis
G202S/Q207H/R236C/R369M/Q382E
-
site-directed mutagenesis
G202V
-
site-directed mutagenesis. Reduction in activity increases to six orders of magnitude for the G202V variant
I437N
-
site-directed mutagenesis
K100A
Q207H/S316N/I437N
-
site-directed mutagenesis
Q207H/S316N/Q382E
-
site-directed mutagenesis
S180A
S181A
significant decrease in kcat value
S204A
S217A
very little enzymic activity
S218A
very little enzymic activity
T31I/I437N
-
site-directed mutagenesis