Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Phospholipids | increase enzymatic activity 3-4fold | Rhodobacter capsulatus |
Cloned (Comment) | Organism |
---|---|
derived from plasmid pRPS404, consisting of a 46 kb pair section of the photosynthetic gene cluster, overexpression of His6-tagged protein in Escherichia coli, strain BL21DE3, expression plasmid pHisBchM | Rhodobacter capsulatus |
General Stability | Organism |
---|---|
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms | Rhodobacter capsulatus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cobalt II-protoporphyrin | non-substrate metalloporphyrin, competitive, assay described | Rhodobacter capsulatus | |
magnesium protoporphyrin monomethyl ester | non-competitive product inhibition | Rhodobacter capsulatus | |
manganese III-protoporphyrin | non-substrate metalloporphyrin, non-competitive or un-competitive, assay described | Rhodobacter capsulatus | |
additional information | higher magnesium ion concentrations above 3.8 mM inhibit enzyme activity in presence or absence of magnesium-chelatase subunits or BSA | Rhodobacter capsulatus | |
S-adenosyl-L-homocysteine | non-competitive product inhibition | Rhodobacter capsulatus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0006 | - |
magnesium deuteroporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus | |
0.0008 | - |
zinc protoporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus | |
0.001 | - |
magnesium mesoporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus | |
0.045 | - |
S-adenosyl-L-methionine | previously determined constant | Rhodobacter capsulatus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
29000 | - |
His6-tagged protein, gel filtration, SDS-PAGE | Rhodobacter capsulatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + magnesium mesoporphyrin | Rhodobacter capsulatus | - |
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodobacter capsulatus | P26236 | - |
- |
Purification (Comment) | Organism |
---|---|
from inclusion bodies, gel filtration and SDS-PAGE | Rhodobacter capsulatus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | - |
Rhodobacter capsulatus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
effect of detergents and alcohols on activity analyzed, no stimulatory effect by magnesium-chelatase subunits, heat-stable stimulatory component present in S-adenosyl-L-methionine synthetase found to be a phospholipid, kinetic analysis shows a random sequential reaction mechanism | Rhodobacter capsulatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + magnesium deuteroporphyrin | in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins | Rhodobacter capsulatus | S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester | - |
? | |
S-adenosyl-L-methionine + magnesium mesoporphyrin | - |
Rhodobacter capsulatus | S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester | - |
? | |
S-adenosyl-L-methionine + magnesium mesoporphyrin | in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay | Rhodobacter capsulatus | S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester | - |
? | |
S-adenosyl-L-methionine + magnesium protoporphyrin | in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay | Rhodobacter capsulatus | S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester | - |
? | |
S-adenosyl-L-methionine + zinc protoporphyrin | in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins | Rhodobacter capsulatus | S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | disaggregation to lower molecular mass forms, monomeric to multimeric species, gel filtration | Rhodobacter capsulatus |
Synonyms | Comment | Organism |
---|---|---|
BchM | - |
Rhodobacter capsulatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Rhodobacter capsulatus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
magnesium deuteroporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus | |
0.018 | - |
zinc protoporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus | |
0.04 | - |
magnesium protoporphyrin | determined using 250 microM S-adenosyl-L-methionine | Rhodobacter capsulatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
slight preference for Tris/HCl buffer over Tricine/NaOH | Rhodobacter capsulatus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8.5 | within activity range | Rhodobacter capsulatus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00045 | - |
magnesium protoporphyrin monomethyl ester | non-competitive product inhibition, magnesium deuteroporphyrin as substrate | Rhodobacter capsulatus | |
0.00061 | - |
magnesium protoporphyrin monomethyl ester | non-competitive product inhibition, S-adenosyl-L-methionine as substrate | Rhodobacter capsulatus | |
0.121 | - |
S-adenosyl-L-homocysteine | non-competitive, magnesium protoporphyrin as substrate | Rhodobacter capsulatus | |
0.141 | - |
S-adenosyl-L-homocysteine | non-competitive, S-adenosyl-L-methionine as substrate | Rhodobacter capsulatus |