1.1.99.31: (S)-mandelate dehydrogenase

This is an abbreviated version!
For detailed information about (S)-mandelate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.99.31

Reaction

(S)-Mandelate
+
acceptor
=
phenylglyoxylate
+
reduced acceptor

Synonyms

(S)-mandelate dehydrogenase, L-mandelate dehydrogenase, L-MDH, MDH, SManDH, SMDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                1.1.99.31 (S)-mandelate dehydrogenase

Engineering

Engineering on EC 1.1.99.31 - (S)-mandelate dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G81D
-
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN
G81S
-
the rate of the first half-reaction is slower than the wild-type rate. The rate of the first half-reaction is slower than the wild-type rate. Affinity for O2 increases 10-15fold
G81V
-
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN
H274A
-
inactive mutant, activity can partially be restored by the addition of exogenous imidazole
H274D
-
inactive mutant
H274G
-
inactive mutant, activity can be restored by the addition of exogenous imidazole
R165E
-
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 81.8fold decrease in kcat for (S)-mandelate, 199fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165G
-
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 27.3fold decrease in kcat for (S)-mandelate, 48.3fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165G/R277G
-
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
R165G/R277K
-
double mutant is less stable than single Arg165 mutant in term of long-term storage. 9000fold decrease in kcat for (S)-mandelate, 261.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165K
-
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 3fold decrease in kcat for (S)-mandelate, 12.5fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165K/R277G
-
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
R165K/R277K
-
double mutant is less stable than single Arg165 mutant in term of long-term storage. 327fold decrease in kcat for (S)-mandelate, 126.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165M
-
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 19.6fold decrease in kcat for (S)-mandelate, 36.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R277G
R277H
-
kcat for (S)-mandelate is 1000fold lower than wild-type value, KM-value for (S)-mandelate is 608fold higher than wild-type value
R277K
R277L
-
kcat for (S)-mandelate is 421fold lower fold than wild-type value, KM-value for (S)-mandelate is 392fold higher than wild-type value
additional information