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3.2.2.24: ADP-ribosyl-[dinitrogen reductase] hydrolase

This is an abbreviated version!
For detailed information about ADP-ribosyl-[dinitrogen reductase] hydrolase, go to the full flat file.

Word Map on EC 3.2.2.24

Reaction

[dinitrogen reductase]-Nomega-alpha-(ADP-D-ribosyl)-L-arginine
=
ADP-D-ribose
 +
[dinitrogen reductase]-L-arginine

Synonyms

ADP-ribosyl glycohydrolase, ADP-ribosylglycohydrolase, ADP-ribosylhydrolase, azoferredoxin-activating enzymes, dinitrogenase reductase activating glycohydrolase, dinitrogenase reductase ADP-glycohydrolase, dinitrogenase reductase glycohydrolase, dinitrogenase reductase-activating glycohydrolase, DRAG, glycosidase, azoferredoxin, mono-ADP-ribosylhydrolase, More

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.24 ADP-ribosyl-[dinitrogen reductase] hydrolase

Engineering

Engineering on EC 3.2.2.24 - ADP-ribosyl-[dinitrogen reductase] hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C102S
-
enzyme maintains activity after removal of light, shows a significantly poorer affinity for Mn2+, and higher affinity for the calcium site of the hydroxylapatite column than wild-type
D123A
-
reduced catalytic activity and binding of Mn2+
D243G
-
no catalytic activity or binding of Mn2+
E279R
-
catalytic and electron paramagnetic resonance spectral properties like wild type
H142L
-
catalytic and electron paramagnetic resonance spectral properties like wild type
H158N
-
no catalytic activity or binding of Mn2+
N100K
-
enzyme maintains activity after removal of light and does not respond to addition of NH4Cl, shows a significantly poorer affinity for Mn2+ and higher affinity for the calcium site of the hydroxylapatite column than wild-type
V98L
-
enzyme maintains activity after removal of light, and shows higher affinity for the calcium site of the hydroxylapatite column than wild-type
additional information