ADP-ribosylglycohydrolase
| ADP-ribosylglycohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of ribosylglycohydrolase mj1187 from methanococcus jannaschii | |||||||||
| Identifiers | |||||||||
| Symbol | ADP_ribosyl_GH | ||||||||
| Pfam | PF03747 | ||||||||
| InterPro | IPR005502 | ||||||||
| SCOP | 1t5j | ||||||||
| SUPERFAMILY | 1t5j | ||||||||
| |||||||||
In molecular biology, ADP-ribosylglycohydrolase is a family of enzymes which catalyses ADP-ribosylations. This family includes enzymes such as ADP-ribosylarginine hydrolase (EC 3.2.2.19. which cleaves ADP-ribose-L-arginine.[1] The family also includes dinitrogenase reductase activating glycohydrolase,[2] and most surprisingly jellyfish crystallins,[2] although these proteins appear to have lost the presumed active site residues.
See also
References
- ↑ Takada T, Iida K, Moss J (August 1993). "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase". J. Biol. Chem. 268 (24): 17837–43. PMID 8349667.
- 1 2 Fitzmaurice WP, Saari LL, Lowery RG, Ludden PW, Roberts GP (August 1989). "Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum". Mol. Gen. Genet. 218 (2): 340–7. doi:10.1007/BF00331287. PMID 2506427.
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