Literature summary for 4.6.1.18 extracted from

Berisio, R.; Sica, F.; Lamzin, V.S.; Wilson, K.S.; Zagari, A.; Mazzarella, L.
Atomic resolution structures of ribonuclease A at six pH values (2002), Acta Crystallogr. Sect. D, D58, 441-450.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	bovine	-

Reaction

Reaction	Comment	Organism	Reaction ID
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA]	the catalytic site of the enzyme is mainly composed of His12, His119, Gln11, Lys41 and Asp121. The conformation of Lys41 and Gln11 are pH dependent and their occurrence is correlated to the release of a sulfate ion from the active site at neutral pH. The sulfate anion is progressively released with pH and water molecules occupy the active site at pH 7.1. The enzyme adopts different conformational states in different pH conditions. In the protonated state, Lys41 points towards the active site both in the presence and in the absence of sulfate and acts as a general base during catalysis	Bos taurus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Bos taurus	-

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Release 2023.1 (January 2023)