Literature summary for 1.6.2.2 extracted from

Saulter, J.Y.; Kurian, J.R.; Trepanier, L.A.; Tidwell, R.R.; Bridges, A.S.; Boykin, D.W.; Stephens, C.E.; Anbazhagan, M.; Hall, J.E.
Unusual dehydroxylation of antimicrobial amidoxime prodrugs by cytochrome b5 and NADH cytochrome b5 reductase (2005), Drug Metab. Dispos., 33, 1886-1893.

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Application

Application	Comment	Organism
medicine	enzyme and cytochrome b5 play a direct role in metabolic activation of antimicrobial prodrug DB289 to furamidine	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
microsome	-	Homo sapiens	-	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	native and recombinant enzyme	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-hydroxybenzenecarboximidamide	metabolite of DB289, an antimicrobial prodrug of furamidine	Homo sapiens	ferrocytochrome b5 + ?	-	?
ferricytochrome b5 + 4-(5-(4-[amino(hydroxyamino)methyl]phenyl)-2-furyl)-N'-methoxybenzenecarboximidamide	metabolite of DB289, an antimicrobial prodrug of furamidine	Homo sapiens	ferrocytochrome b5 + ?	-	?

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Release 2023.1 (January 2023)