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Literature summary extracted from

  • Trevino, R.J.; Gliubich, F.; Berni, R.; Cianci, M.; Chirgwin, J.M.; Zanotti, G.; Horowitz, P.M.
    NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions (1999), J. Biol. Chem., 274, 13938-13947.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.1.1 wild-type and DELTA1-7 in polyethyleneglycol 6000, the two-domain structure is not significantly altered by drastically different crystallization conditions or crystal packing, sitting-drop vapour-diffusion method, orthorhombic crystal Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.1 DELTA1-3 no significant change in stability versus wild-type Bos taurus
2.8.1.1 DELTA1-7 measureably destablized but no significantly alteration in contacts at the atomic level of the crystallized protein Bos taurus
2.8.1.1 DELTA1-7 significant destabilization versus wild-type Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.1 thiosulfate + cyanide Bos taurus
-
sulfite + thiocyanate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.1 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.1 thiosulfate + cyanide
-
Bos taurus sulfite + thiocyanate
-
?

Subunits

EC Number Subunits Comment Organism
2.8.1.1 monomer gel filtration yields a single peak with the same shape and same enclosed area eluted at the same volume as expected for monomeric rhodanese Bos taurus