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Literature summary for 6.6.1.1 extracted from

  • Adams, N.B.; Reid, J.D.
    The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803 (2013), J. Biol. Chem., 288, 28727-28732.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Synechocystis sp.

Protein Variants

Protein Variants Comment Organism
E152Q mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows low activity but assembles into complexes much like wild-type. Mutant shows 25% of wild-type activity. kcat/K0.5 for Mg2+ is 30% of wild-type. kcat and Km for deuteroporphyrin are reduced to the same extent Synechocystis sp.
K49A mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows no activity. Mutant forms detecable amount of ChlID complexes Synechocystis sp.
R208A mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows reduced binding affinity to ChlI.Mutant shows 50% of wild-type activity (least impaired mutant). Effect on substrate handling is modest compared to wild-type. Specifictiy constants for Mg2+ and porphyrin are 70% of wild-type Synechocystis sp.
R289A mutation in the AAA+ domain of ChlD binds to ChlI. Mutant shows reduced binding affinity to ChlI. Mutant shows 13% of wild-type activity. Mutant does not show a cooperative response to MgATP2- and has much weaker specificity toward Mg2+ than wild-type. Mutant has a lower specificity toward free porphyrin than wild-type Synechocystis sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00099
-
deuteroporphyrin mutant R289A, pH 7.7, 34°C Synechocystis sp.
0.0012
-
deuteroporphyrin mutant E152Q, pH 7.7, 34°C Synechocystis sp.
0.0057
-
deuteroporphyrin wild-type, pH 7.7, 34°C Synechocystis sp.
0.00631
-
deuteroporphyrin mutant R208A, pH 7.7, 34°C Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Synechocystis sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + deuteroporphyrin + Mg2+ + H2O
-
Synechocystis sp. ADP + phosphate + Mg-deuteroporphyrin + H+
-
?

Synonyms

Synonyms Comment Organism
magnesium chelatase
-
Synechocystis sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
34
-
assay at Synechocystis sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0009
-
ATP mutant R289A, pH 7.7, 34°C Synechocystis sp.
0.0013
-
deuteroporphyrin mutant R289A, pH 7.7, 34°C Synechocystis sp.
0.0018
-
ATP mutant E152Q, pH 7.7, 34°C Synechocystis sp.
0.0028
-
Mg2+ mutant E152Q, pH 7.7, 34°C Synechocystis sp.
0.003
-
deuteroporphyrin mutant E152Q, pH 7.7, 34°C Synechocystis sp.
0.0043
-
ATP mutant R208A, pH 7.7, 34°C Synechocystis sp.
0.0067
-
ATP wild-type, pH 7.7, 34°C Synechocystis sp.
0.0081
-
Mg2+ wild-type, pH 7.7, 34°C Synechocystis sp.
0.0083
-
Mg2+ mutant R208A, pH 7.7, 34°C Synechocystis sp.
0.014
-
deuteroporphyrin mutant R208A, pH 7.7, 34°C Synechocystis sp.
0.0188
-
deuteroporphyrin wild-type, pH 7.7, 34°C Synechocystis sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.7
-
assay at Synechocystis sp.