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Literature summary extracted from

  • Takahashi, K.
    Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidases (2013), Proc. Jpn. Acad. Ser. B Phys. Biol. Sci., 89, 201-225.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.6.1.24 carboxymethylated RNase T1 crystal structure analysis, PDB ID 1DET Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.24 2'-guanylic acid substrate analogue Aspergillus oryzae
4.6.1.24 3'-guanylic acid substrate analogue Aspergillus oryzae
4.6.1.24 citrate
-
 Aspergillus oryzae
4.6.1.24 Cu2+
-
 Aspergillus oryzae
4.6.1.24 iodoacetamide iodoacetamide, but not iodoacetate, reacts with these His residues at pH 8.0, but not at pH 5.5 Aspergillus oryzae
4.6.1.24 iodoacetate reaction of iodoacetate with the gamma-carboxyl group of Glu58 in RNase T1. The iodoacetate reaction is inhibited by substrate analogues 2- or 3-guanylic acid, by phosphate or citrate ions, and by Zn2+ or Cu2+ Aspergillus oryzae
4.6.1.24 additional information carboxymethylated-RNase T1 possesses almost the same binding ability toward guanosine as intact RNase T1, whereas the binding ability toward 2' or 3'-guanylic acid is considerably lowered by carboxymethylation of Glu58 Aspergillus oryzae
4.6.1.24 Phenylglyoxal inactivates the enzyme by specific reaction with Arg77 at the active site Aspergillus oryzae
4.6.1.24 phosphate
-
 Aspergillus oryzae
4.6.1.24 Zn2+
-
 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
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.24 additional information the enzyme hydrolyzes specifically the 3'-phosphodiester bond of guanylic acid in RNA, mechanism of interaction of RNase T1 with its substrates, overview. His40 and His92 are deduced to be involved in the active site, overview. Carboxymethylated-RNase T1 possesses almost the same binding ability toward guanosine as intact RNase T1, whereas the binding ability toward 2' or 3'-guanylic acid is considerably lowered by carboxymethylation of Glu58 Aspergillus oryzae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.6.1.24 More comparisons of primary enzyme structure, overview Aspergillus oryzae

Synonyms

EC Number Synonyms Comment Organism
4.6.1.24 RNase T1
-
 Aspergillus oryzae