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Literature summary for 4.6.1.18 extracted from

  • Sica, F.; Di Fiore, A.; Merlino, A.; Mazzarella, L.
    Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease: an enzyme tailored to evade ribonuclease protein inhibitor (2004), J. Biol. Chem., 279, 36753-36760.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization in presence of 2'-deoxycitidylyl(3'-5')-2'-deoxyadenosine at 4°C by using sitting drop vapor diffusion method. Crystal structure of the MxM isomer of the enzyme in the non-covalent dimer form, carboxyamidomethylated at residues Cys31 and Cys32, in a complex with 2'-deoxycitidylyl(3'-5')-2'-deoxyadenosine Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ribonuclease protein inhibitor the native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of the cytosol, isoform M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras isoform MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
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Subunits

Subunits Comment Organism
dimer BS-RNase is covalent dimer with two intersubunit disulfide bridges between Cys31 of one chain and Cys32 of the second and vice versa. The native enzyme is an equilibrium mixture of two isomers, MxM and M=M. In the former the two subunits swap their N-terminal helices. In the reducing environment of cytosol, M=M dissociates into monomers, which are strongly inhibited by ribonuclease protein inhibitor, wheras MxM remains as a non-covalent dimer which evades ribonuclease protein inhibitor Bos taurus

Synonyms

Synonyms Comment Organism
BS-RNase
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Bos taurus
seminal ribonuclease
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Bos taurus