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Literature summary for 1.16.1.1 extracted from

  • Hong, B.; Nauss, R.; Harwood, I.M.; Miller, S.M.
    Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved gamma-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione (2010), Biochemistry, 49, 8187-8196.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.16.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene merA and mer operon, expression of MerA catalytic core and NmerA proteins in Escherichia coli strain XL-1 Blue Serratia marcescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetic analysis, overview, apparent second-order rate constant for Hg(II) transfer from MerB to NmerA Serratia marcescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Hg + NADP+ + H+ Serratia marcescens organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview Hg2+ + NADPH
-
 ?
additional information Serratia marcescens proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Serratia marcescens E0XF09 plasmid-encoded mer operon
-

Purification (Commentary)

Purification (Comment) Organism
recombinant MerA catalytic core and NmerA proteins from Escherichia coli strain XL-1 Blue by anion exchange chromatography and gel filtreation, and separation by affinity chromatography Serratia marcescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hg + NADP+ + H+
-
 Serratia marcescens Hg2+ + NADPH
-
 ?
Hg + NADP+ + H+ organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview Serratia marcescens Hg2+ + NADPH
-
 ?
additional information proposed model for reaction of NmerA with HgMerB and of GSH with HgMerB, overview Serratia marcescens ?
-
 ?

Synonyms

Synonyms Comment Organism
MerA
-
 Serratia marcescens
mercuric ion reductase
-
 Serratia marcescens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Serratia marcescens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Serratia marcescens

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Serratia marcescens

General Information

General Information Comment Organism
evolution organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH Serratia marcescens
physiological function organomercurials are converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase MerB and mercuric ion reductase MerA, requiring transfer of Hg(II) from MerB to MerA, with transfer to the metallochaperone-like NmerA domain as the kinetically favored pathway in this coevolved system, overview. Hg(II) removal from MerB by the N-terminal domain, NmerA, and catalytic core C-terminal cysteine pairs of its coevolved MerA and by GSH, the major competing cellular thiol in gamma-proteobacteria. The reaction with a 10fold excess of NmerA over HgMerB removes about 92% of Hg(II), while similar extents of reaction require more than 1000fold excess of GSH. NmerA reacts more completely than GSH with HgMerB Serratia marcescens