Enzyme

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EC Tree
     3. Hydrolases
        3.2 Glycosylases
            3.2.2 Hydrolysing N-glycosyl compounds
ID:3.2.2.24
Description:ADP-ribosyl-[dinitrogen reductase] hydrolase.
Alternative Name: Dinitrogenase reductase activating glycohydrolase.
ADP-ribosyl glycohydrolase.
Cath: 1.10.4080.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.2.2.24
BRENDA Enzyme Link: BRENDA 3.2.2.24
KEGG Enzyme Link: KEGG3.2.2.24
BioCyc Enzyme Link: BioCyc 3.2.2.24
ExPASy Enzyme Link: ExPASy3.2.2.24
EC2PDB Enzyme Link: EC2PDB 3.2.2.24
ExplorEnz Enzyme Link: ExplorEnz 3.2.2.24
PRIAM enzyme-specific profiles Link: PRIAM 3.2.2.24
IntEnz Enzyme Link: IntEnz 3.2.2.24
MEDLINE Enzyme Link: MEDLINE 3.2.2.24
MSA:

3.2.2.24;

Phylogenetic Tree:

3.2.2.24;

Uniprot:
M-CSA:
RHEA:14493 [dinitrogen reductase]-N(omega)-alpha-(ADP-D-ribosyl)-L-arginine + H2O = [dinitrogen reductase]-L-arginine + ADP-D-ribose
RULE(radius=1) [*:1]-[NH;+0:2]-[CH;+0:3](-[*:4])-[*:5].[OH2;+0:6]>>[*:4]-[CH;+0:3](-[*:5])-[OH;+0:6].[*:1]-[NH2;+0:2]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum.Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP1989 Aug2506427
Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.Berthold CL, Wang H, Nordlund S, Högbom M2009 Aug 2519706507
Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket.Li XD, Huergo LF, Gasperina A, Pedrosa FO, Merrick M, Winkler FK2009 Jul 2419477184
Metabolic regulation of nitrogen fixation in Rhodospirillum rubrum.Wang H, Norén A2006 Feb16417510