Literature summary extracted from

Chao, W.C.; Shen, J.Y.; Lu, J.F.; Wang, J.S.; Yang, H.C.; Wee, K.; Lin, L.J.; Kuo, Y.C.; Yang, C.H.; Weng, S.H.; Huang, H.C.; Chen, Y.H.; Chou, P.T.
Probing water environment of Trp59 in ribonuclease T1: insight of the structure-water network relationship (2014), J. Phys. Chem. B, 119, 2157-2167.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.6.1.24	expression of the enzyme in Trp-auxotrophic Escherichia coli, resulting in site-specifically replacement of Trp residues with (2,7-aza)Trp	Aspergillus oryzae

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.6.1.24	RNase T1 crystal structure analysis, PDB ID 9RNT	Aspergillus oryzae

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
4.6.1.24	extracellular	-	Aspergillus oryzae	-	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.6.1.24	Aspergillus oryzae	-	-	-

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
4.6.1.24	the enzyme can be reversibly unfolded and refolded by heating and high concentration of denaturants, such as urea and guanidine hydrochloride, without forming noticeable amounts of aggregates	Aspergillus oryzae

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.6.1.24	additional information	the enzyme cleaves single-stranded RNA by catalyzing the hydrolysis of phosphodiester bonds specifically at the 3'-side of guanosine nucleotides	Aspergillus oryzae	?	-	?

Subunits

EC Number	Subunits	Comment	Organism
4.6.1.24	More	the secondary structure of RNase T1 includes a long alpha-helix and two beta-sheets connected by extended loop regions, structure of hydrated RNase T1 in loop-close and loop-open forms, overview	Aspergillus oryzae

Synonyms

EC Number	Synonyms	Comment	Organism
4.6.1.24	ribonuclease T1	-	Aspergillus oryzae
4.6.1.24	RNase T1	-	Aspergillus oryzae

General Information

EC Number	General Information	Comment	Organism
4.6.1.24	additional information	Trp59 may play an important role in folding as well as in modulating the geometry of the RNase T1 active site. Trp59-water pairs appear to preferentially participate in a hydrogen bond network incorporating polar amino acid moieties on the protein surface and bulk waters, providing the structural dynamic features of the connecting loop region in RNase T1, molecular dynamic simulations, overview	Aspergillus oryzae

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Release 2023.1 (January 2023)