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Literature summary extracted from

  • Karow, D.S.; Pan, D.; Davis, J.H.; Behrends, S.; Mathies, R.A.; Marletta, M.A.
    Characterization of functional heme domains from soluble guanylate cyclase (2005), Biochemistry, 44, 16266-16274.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.2 NO binds to the heme cofactor in the beta1 subunit, forming a five-coordinate NO complex that activates the enzyme several hundred-fold Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.2 N-terminal heme-binding regions of subunit beta1 from soluble guanylate cyclase are generated by subcloning specific constructs into the Escherichia coli expression vector pET-20b. The shortest region that is subcloned, has heme-bound, and is expressed well is beta1(1-194) Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.2 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.2
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
4.6.1.2 heme heme domain is localized to the N-terminal 194 residues of the beta1 subunit. Characterization of the minimum functional ligand-binding heme domain derived from soluble guanylate cyclase Rattus norvegicus