Literature summary for 4.6.1.2 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.

Search for more literature for 4.6.1.2

Activating Compound

Activating Compound	Comment	Organism	Structure
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)

Cloned (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)