Literature summary for 7.2.2.12 extracted from

Dutta, S.J.; Liu, J.; Mitra, B.
Kinetic analysis of metal binding to the amino-terminal domain of ZntA by monitoring metal-thiolate charge-transfer complexes (2005), Biochemistry, 44, 14268-14274.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cd2+	activation energy of binding is similar for both Pb2+ and Cd2+	Escherichia coli
additional information	metal binding to the transmembrane site in ZntA or metal release from the transporter is the slow step in the reaction cycle. metal-binding to the N-terminal domain is not rate-limiting in the overall transport mechanism	Escherichia coli
Pb2+	activation energy of binding is similar for both Pb2+ and Cd2+	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)