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Literature summary for 1.16.1.1 extracted from

  • Schue, M.; Glendinning, K.J.; Hobman, J.L.; Brown, N.L.
    Evidence for direct interactions between the mercuric ion transporter (MerT) and mercuric reductase (MerA) from the Tn501 mer operon (2008), Biometals, 21, 107-116.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
subcloning and expression in strain TG2, bacterial two hybrid assays are performed in strain BTH101 Escherichia coli K-12

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli K-12 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hg2+ + NADPH Escherichia coli K-12 mercuric ion resistance in bacteria requires transport of Hg2+ ions into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury Hg0 by mercuric reductase Hg(0) + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg2+ + NADPH mercuric ion resistance in bacteria requires transport of Hg2+ ions into the cytoplasmic compartment where they are reduced to the less toxic metallic mercury Hg0 by mercuric reductase Escherichia coli K-12 Hg(0) + NADP+
-
r
Hg2+ + NADPH interactions between the inner membrane mercuric ion transporter, MerT, and the N-terminal domain of cytoplasmic mercuric reductase, transport is the rate-limiting step in mercury detoxification, overview Escherichia coli K-12 Hg(0) + NADP+
-
r

Synonyms

Synonyms Comment Organism
mercuric ion reductase
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Escherichia coli K-12
mercuric reductase
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Escherichia coli K-12

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Escherichia coli K-12
NADPH
-
Escherichia coli K-12