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Literature summary for 7.2.2.12 extracted from

  • Roberts, C.; Muralidharan, S.; Ni, F.; Mitra, B.
    Structural role of the first four transmembrane helices in ZntA, a P1B-Type ATPase from Escherichia coli (2020), Biochemistry, 59, 4488-4498.
    View publication on PubMed
Search for more literature for 7.2.2.12

Protein Variants

Protein Variants Comment Organism
C392A mutant DELTA231-ZntA(C392A), binds Pb2+ and Zn2+ with a stoichiometry of 0.5 and with similar or slightly higher affinity than DELTA231-ZntA. Cd2+ does not bind to the mutant enzyme Escherichia coli
C394A mutant DELTA231-ZntA(C394A), binds Pb2+ and Zn2+ with a stoichiometry of 0.5 and with similar or slightly higher affinity than DELTA231-ZntA. The mutant enzyme binds Cd2+ with unchanged affinity and with a stoichiometry of 0.5 Escherichia coli
D714A mutant DELTA231-ZntA(D714A), binds Pb2+ and Zn2+ with a stoichiometry of 0.5 and with similar or slightly higher affinity than DELTA231-ZntA. Cd2+ does not bind to the mutant enzyme Escherichia coli
additional information DELTA231-ZntA has no in vivo and greatly reduced in vitro activity. It binds one metal ion per dimer at the transmembrane site, with a 15-19000-fold higher binding affinity, indicating highly significant changes in the dimer structure of DELTA231-ZntA relative to that of ZntA. Cd2+ has the highest affinity for DELTA231-ZntA, in contrast to ZntA, which has the highest affinity for Pb2+. DELTA231-ZntA is unable to confer resistance to Pb2+, Zn2+, and Cd2+ salts in LMG194(zntA::cat) and behaves like the zntA deletion strain Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0048
-
 Pb2+[side 1] pH 7.0, 37°C, wild-type enzyme Escherichia coli
0.0103
-
 Zn2+[side 1] pH 7.0, 37°C, wild-type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Zn2+[side 1] Escherichia coli
-
 ADP + phosphate + Zn2+[side 2]
-
 ?
ATP + H2O + Zn2+[side 1] Escherichia coli K12
-
 ADP + phosphate + Zn2+[side 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P37617 cf. EC 7.2.2.21
-
Escherichia coli K12 P37617 cf. EC 7.2.2.21
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Pb2+[side 1]
-
 Escherichia coli ADP + phosphate + Pb2+[side 2]
-
 ?
ATP + H2O + Pb2+[side 1]
-
 Escherichia coli K12 ADP + phosphate + Pb2+[side 2]
-
 ?
ATP + H2O + Zn2+[side 1]
-
 Escherichia coli ADP + phosphate + Zn2+[side 2]
-
 ?
ATP + H2O + Zn2+[side 1]
-
 Escherichia coli K12 ADP + phosphate + Zn2+[side 2]
-
 ?

Subunits

Subunits Comment Organism
dimer the first four transmembrane helices in ZntA and P1B-type ATPases play an important role in maintaining the correct dimer structure Escherichia coli

Synonyms

Synonyms Comment Organism
P1B-type ATPase
-
 Escherichia coli
ZntA
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function ZntA confers resistance to wild-type Escherichia coli strains against toxic levels of Pb2+, Cd2+, and Zn2+ in the growth medium Escherichia coli