Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli JM109, constitutive promoter on pUCmod, overexpression improved by using BL21 cells in combination with T7 promoter, subclconing into pET-20b(+) vector, engineered Escherichia coli strain overproducing protoporphyrin for activity assays | Chlorobaculum tepidum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0006 | - |
magnesium protoporphyrin | concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme | Chlorobaculum tepidum | |
0.053 | - |
protoporphyrin | concentrations between 1 and 30 microM in the presence of 200 nM enzyme | Chlorobaculum tepidum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlorobaculum tepidum | - |
formerly Chlorobium tepidum | - |
Purification (Comment) | Organism |
---|---|
recombinant protein, gel filtration and SDS-PAGE | Chlorobaculum tepidum |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | - |
Chlorobaculum tepidum | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity assay in protoporphyrin overproducing Escherichia coli cells, interaction of subunits of the three magnesium chelatase complexes with magnesium protoporphyrin methyltransferase, differences in subunit interactions either increase or decrease methyltransferase activity, vice versa, activity of any of the three magnesium chelatase complexes not affected | Chlorobaculum tepidum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + magnesium protoporphyrin | different substrate specificity, protoporphyrin with or without bound metal as a substrate | Chlorobaculum tepidum | S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester | - |
? | |
S-adenosyl-L-methionine + protoporphyrin | methyl transfer possible without bound metal, slow reaction rate | Chlorobaculum tepidum | S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | majority of the protein exist as a high-molecular-weight multimer as determined by gel filtration | Chlorobaculum tepidum |
Synonyms | Comment | Organism |
---|---|---|
BchM | - |
Chlorobaculum tepidum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Chlorobaculum tepidum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0002 | - |
protoporphyrin | concentrations between 1 and 30 microM in the presence of 200 nM enzyme | Chlorobaculum tepidum | |
0.14 | - |
magnesium protoporphyrin | concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme | Chlorobaculum tepidum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Chlorobaculum tepidum |