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Literature summary extracted from
- Mercury (II) removal by resistant bacterial isolates and mercuric (II) reductase activity in a new strain of Pseudomonas sp. B50A (2016), New Biotechnol., 33, 216-223 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.16.1.1 | gene merA | Pseudomonas putida |
| 1.16.1.1 | gene merA | Pseudomonas entomophila |
| 1.16.1.1 | gene merA | Enterobacter sp. B50C |
| 1.16.1.1 | gene merA | Enterobacter sp. A25B |
| 1.16.1.1 | gene merA | Pseudomonas sp. B50A |
| 1.16.1.1 | gene merA | Pseudomonas sp. B50B |
| 1.16.1.1 | gene merA | Pseudomonas sp. B50D |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.16.1.1 | Ba2+ | slightly inhibiting | Pseudomonas sp. B50A |  |
| 1.16.1.1 | Ca2+ | - |
Pseudomonas sp. B50A | |
| 1.16.1.1 | Cu+ | - |
Pseudomonas sp. B50A | |
| 1.16.1.1 | K+ | - |
Pseudomonas sp. B50A | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Enterobacter sp. A25B | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Enterobacter sp. B50C | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Pseudomonas entomophila | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Pseudomonas putida | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Pseudomonas sp. B50A | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Pseudomonas sp. B50B | |
| 1.16.1.1 | additional information | determination of the organism's minimum inhibitory concentration (MIC) for mercury, with mercury chloride and mercury acetate, overview | Pseudomonas sp. B50D | |
| 1.16.1.1 | NH4+ | slightly inhibiting | Pseudomonas sp. B50A | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.16.1.1 | additional information | - |
additional information | Michaelis-Menten kinetics | Pseudomonas sp. B50A |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.16.1.1 | additional information | ions Sn2+, Ni2+ and Cd2+ neither inhibit nor stimulate the enzyme activity | Pseudomonas sp. B50A |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas putida | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas entomophila | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Enterobacter sp. B50C | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Enterobacter sp. A25B | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas sp. B50A | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas sp. B50B | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas sp. B50D | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas entomophila A50A | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas putida V1 | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | Pseudomonas entomophila B100A | - |
Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | additional information | Pseudomonas sp. B50A | Pseudomonas sp. strain B50A exhibiting Mercuric (II) reductase activity removes 86% of the mercury present in the culture medium. ENzyme activity is measured as capacity to remove mercury from the growth medium, activity profile for Pseudomonas sp. B50A, overview | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.16.1.1 | Enterobacter sp. A25B | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Enterobacter sp. B50C | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas entomophila | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas entomophila A50A | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas entomophila B100A | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas putida | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas putida V1 | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas sp. B50A | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas sp. B50B | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
| 1.16.1.1 | Pseudomonas sp. B50D | - |
from soil samples collected from landfarming and landspreading areas used to treat petrochemical waste contaminated with mercury | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas putida | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas entomophila | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Enterobacter sp. B50C | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Enterobacter sp. A25B | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas sp. B50A | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas sp. B50B | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas sp. B50D | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas entomophila A50A | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas putida V1 | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | Hg2+ + NADPH | - |
Pseudomonas entomophila B100A | Hg + NADP+ + H+ | - |
? | |
| 1.16.1.1 | additional information | Pseudomonas sp. strain B50A exhibiting Mercuric (II) reductase activity removes 86% of the mercury present in the culture medium. ENzyme activity is measured as capacity to remove mercury from the growth medium, activity profile for Pseudomonas sp. B50A, overview | Pseudomonas sp. B50A | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Pseudomonas putida |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Pseudomonas entomophila |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Enterobacter sp. B50C |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Enterobacter sp. A25B |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Pseudomonas sp. B50A |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Pseudomonas sp. B50B |
| 1.16.1.1 | dimer | the enzyme acts as a dimer and is composed of three domains. The active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs. The N-terminal domain has the function of directing the Hg(II) to the active site of MerA | Pseudomonas sp. B50D |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.16.1.1 | MerA | - |
Pseudomonas putida |
| 1.16.1.1 | MerA | - |
Pseudomonas entomophila |
| 1.16.1.1 | MerA | - |
Enterobacter sp. B50C |
| 1.16.1.1 | MerA | - |
Enterobacter sp. A25B |
| 1.16.1.1 | MerA | - |
Pseudomonas sp. B50A |
| 1.16.1.1 | MerA | - |
Pseudomonas sp. B50B |
| 1.16.1.1 | MerA | - |
Pseudomonas sp. B50D |
| 1.16.1.1 | mercuric (II) reductase | - |
Pseudomonas putida |
| 1.16.1.1 | mercuric (II) reductase | - |
Pseudomonas entomophila |
| 1.16.1.1 | mercuric (II) reductase | - |
Enterobacter sp. B50C |
| 1.16.1.1 | mercuric (II) reductase | - |
Enterobacter sp. A25B |
| 1.16.1.1 | mercuric (II) reductase | - |
Pseudomonas sp. B50A |
| 1.16.1.1 | mercuric (II) reductase | - |
Pseudomonas sp. B50B |
| 1.16.1.1 | mercuric (II) reductase | - |
Pseudomonas sp. B50D |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.1 | 40 | 45 | - |
Pseudomonas sp. B50A |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.1 | 1 | 85 | activity range, profile overview | Pseudomonas sp. B50A |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.1 | 8 | - |
- |
Pseudomonas sp. B50A |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.16.1.1 | 5 | 9 | activity range, profile overview | Pseudomonas sp. B50A |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.16.1.1 | FAD | a flavin oxidoreductase | Pseudomonas putida | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Pseudomonas entomophila | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Enterobacter sp. B50C | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Enterobacter sp. A25B | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Pseudomonas sp. B50A | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Pseudomonas sp. B50B | |
| 1.16.1.1 | FAD | a flavin oxidoreductase | Pseudomonas sp. B50D | |
| 1.16.1.1 | NADPH | - |
Pseudomonas putida | |
| 1.16.1.1 | NADPH | - |
Pseudomonas entomophila | |
| 1.16.1.1 | NADPH | - |
Enterobacter sp. B50C | |
| 1.16.1.1 | NADPH | - |
Enterobacter sp. A25B | |
| 1.16.1.1 | NADPH | - |
Pseudomonas sp. B50A | |
| 1.16.1.1 | NADPH | - |
Pseudomonas sp. B50B | |
| 1.16.1.1 | NADPH | - |
Pseudomonas sp. B50D | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Pseudomonas putida |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Pseudomonas entomophila |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Enterobacter sp. B50C |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Enterobacter sp. A25B |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Pseudomonas sp. B50A |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Pseudomonas sp. B50B |
| 1.16.1.1 | additional information | the active site is formed by the interaction of the central domain of a subunit with another C-terminal domain. The central domain, described as a pyridine nucleotide oxidoreductase disulfide group, is where catalysis and the transfer of two electrons from NADPH to Hg(II) via FAD, occurs | Pseudomonas sp. B50D |
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