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Literature summary for 2.1.1.11 extracted from

  • Johnson, E.T.; Schmidt-Dannert, C.
    Characterization of three homologs of the large subunit of the magnesium chelatase from Chlorobaculum tepidum and interaction with the magnesium protoporphyrin IX methyltransferase (2008), J. Biol. Chem., 283, 27776-27784.
    View publication on PubMed

Cloned(Commentary)

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 [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

Organism UniProt Comment Textmining
Chlorobaculum tepidum
-
formerly Chlorobium tepidum
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein, gel filtration and SDS-PAGE Chlorobaculum tepidum

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Chlorobaculum tepidum
-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
More majority of the protein exist as a high-molecular-weight multimer as determined by gel filtration Chlorobaculum tepidum

Synonyms

Synonyms Comment Organism
BchM
-
Chlorobaculum tepidum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Chlorobaculum tepidum

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Chlorobaculum tepidum