Creative Enzymes is a leading company that provides high-quality bioanalytical services in enzyme activity analysis, serving the needs of clients from the pharmaceutical, biotechnological and diagnostic industries. Herein, we are proud to offer the accurate enzyme assays for ribonuclease T1.

Ribonuclease T1 (EC 3.1.27.3; formerly EC 2.7.7.26 and EC 3.1.4.8; RNase T1) is an enzyme that catalyzes the depolymerization of RNA at guanylyl residues by a transesterification mechanism that yields a 3’-terminal, cyclic 2’,3’-guanosine phosphate residue. This occurs in a two-step process with cleavage of the RNA chain by transesterification of a 5’-phosphoester bond to form a guanosine 2’,3’-cyclic phosphate terminus in the first step, and then it is hydrolyzed to a 3’-phosphate product. RNase T1 is a globular, single-domain protein of 104 amino acids. RNase T1 is the leading representative of an approximately 25-member superfamily of related fungal/bacterial enzymes/toxins, that share sequence and tertiary structural similarities. Because of its small size, high thermal stability, and the availability of an efficient expression system, RNase T1 can act as a model for protein folding studies. The structure of RNase T1 consists of an α helix, an extended antiparallel β-sheet composed of three long and two short β-strands, a short two-stranded antiparallel β-sheet, four wide loops, and various types of turns.

The inhibitors of RNase T1 appear to be promising candidates for therapy of cancer. Besides, RNase T1 may serve as the promising tools for the development of anticancer drugs. Therefore, to elucidate the catalytic mechanism of RNase T1 is vital for the fundamental understanding of this enzyme and also sheds light on the design of new RNase T1 inhibitors. Fortunately, Creative Enzymes is able to perform the highly sophisticated enzymatic measurement for RNase T1. The activity of RNase T1 is determined spectrophotometrically at 260 nm. Our test results are the most trusted and proven. Overall, Creative Enzymes is committed to chasing the highest grade of customers’ satisfaction, and to constantly improving its services and quality management system.

Figure: The crystal structure of RNase T1 from Aspergillus oryzae.
PDB: 3RNT