Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.6.1.24 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
Search for more literature for 4.6.1.24

Crystallization (Commentary)

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

Inhibitors

Inhibitors Comment Organism Structure
2'-guanylic acid substrate analogue Aspergillus oryzae
3'-guanylic acid substrate analogue Aspergillus oryzae
citrate
-
 Aspergillus oryzae
Cu2+
-
 Aspergillus oryzae
iodoacetamide iodoacetamide, but not iodoacetate, reacts with these His residues at pH 8.0, but not at pH 5.5 Aspergillus oryzae
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
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
Phenylglyoxal inactivates the enzyme by specific reaction with Arg77 at the active site Aspergillus oryzae
phosphate
-
 Aspergillus oryzae
Zn2+
-
 Aspergillus oryzae

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Aspergillus oryzae
-
-

Organism

Organism UniProt Comment Textmining
Aspergillus oryzae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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

Synonyms

Synonyms Comment Organism
RNase T1
-
 Aspergillus oryzae