Literature summary extracted from

Noguchi, S.
Isomerization mechanism of aspartate to isoaspartate implied by structures of Ustilago sphaerogena ribonuclease U2 complexed with adenosine 3'-monophosphate (2010), Acta Crystallogr. Sect. D, 66, 843-849.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.6.1.20	ribonuclease U2 complexed with adenosine 3'-monophosphate, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 20 mg/ml RNase U2A and 8 mM adenosine 3'-monophosphate, pH 4.5, is mixed with 0.005 ml of reservoir solution containing 12.5% w/w PEG 8000, 200 mM calcium acetate, 100 mM sodium cacodylate, pH 3.75, 12.5% w/w PEG 8000, equilibration against 0.4 ml reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 0.96-0.99 A resolution	Ustilago sphaerogena

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.6.1.20	Ustilago sphaerogena	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
4.6.1.20	native RNase U2A by anion-exchange and 5'-adenylate aminohexyl affinity chromatography	Ustilago sphaerogena

Synonyms

EC Number	Synonyms	Comment	Organism
4.6.1.20	RNase U2A	-	Ustilago sphaerogena

General Information

EC Number	General Information	Comment	Organism
4.6.1.20	additional information	mechanism of isoaspartate formation within the Asp45-Glu46 sequence of ribonuclease U2, overview. In the succinimide-formation reaction water 219 receives a proton from the N atom of Glu46 as a general base and waters 190 and 220 stabilize the tetrahedral intermediate, and in the succinimide-hydrolysis reaction water 219 provides a proton for the N atom of Glu46 as a general acid	Ustilago sphaerogena

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Release 2023.1 (January 2023)