Literature summary for 7.6.2.2 extracted from

Golin, J.; Kon, Z.N.; Wu, C.; Martello, J.; Hanson, L.; Supernavage, S.; Ambudkar, S.V.; Sauna, Z.E.
Complete Inhibition of the Pdr5p multidrug efflux pump ATPase activity by its transport substrate clotrimazole suggests that GTP as well as ATP may be used as an energy source (2007), Biochemistry, 46, 13109-13119.

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Inhibitors

Inhibitors	Comment	Organism	Structure
beryllium fluoride	0.25 mM, 86% inhibition of ATPase, 89% inhibition of UTPase, and 50% inhibition of GTPase activity	Saccharomyces cerevisiae
clotrimazole	noncompetitive, inhibitor interacts with the transporter at a site distinct from the ATP-binding domains. Transport of clotrimazole by the enzyme continues at intracellular concentrations of clotrimazole that should eliminate all ATPase activity. GTPase and UTPase activites of the enzyme are rather resistant to clotrimazole	Saccharomyces cerevisiae
orthovanadate	0.3 mM, 93% inhibition of ATPase, 66% inhibition of UTPase, and 45% inhibition of GTPase activity	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0019	-	ATP	-	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	isoform Pdr5	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Saccharomyces cerevisiae	ADP + phosphate	-	?
clotrimazole/in + ATP + H2O	-	Saccharomyces cerevisiae	clotrimazole/out + ADP + phosphate	-	?
GTP + H2O	-	Saccharomyces cerevisiae	GDP + phosphate	-	?
UTP + H2O	-	Saccharomyces cerevisiae	UDP + phosphate	-	?

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Release 2023.1 (January 2023)