Information on EC 2.1.1.11 - magnesium protoporphyrin IX methyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
magnesium protoporphyrin IX methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,8-divinyl-chlorophyllide a biosynthesis I (aerobic, light-dependent)
-
-
3,8-divinyl-chlorophyllide a biosynthesis II (anaerobic)
-
-
3,8-divinyl-chlorophyllide a biosynthesis III (aerobic, light independent)
-
-
Biosynthesis of secondary metabolites
-
-
chlorophyll metabolism
-
-
Metabolic pathways
-
-
Porphyrin and chlorophyll metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-82-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Chlorobium tepidum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + calcium protoporphyrin
S-adenosyl-L-homocysteine + calcium protoporphyrin monomethyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + magnesium deuteroporphyrin
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester
show the reaction diagram
S-adenosyl-L-methionine + magnesium deuteroporphyrin IX
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin IX 13-methyl ester
show the reaction diagram
-
activity assay
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
S-adenosyl-L-methionine + magnesium protoporphyrin IX
S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
S-adenosyl-L-methionine + protoporphyrin
S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester
show the reaction diagram
S-adenosyl-L-methionine + tetrapyrrole
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + zinc protoporphyrin
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
P26236
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
S-adenosyl-L-methionine + magnesium protoporphyrin IX
S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Magnesium
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
8-hydroxyquinoline
-
-
chlorophyllide a
-
-
cobalt II-protoporphyrin
non-substrate metalloporphyrin, competitive, assay described
Diphenylthiocarbazone
-
-
Ferric protoporphyrin
-
-
Ferrous protoporphyrin
-
-
Hemin
-
noncompetitive with respect to magnesium protoporphyrin
iodoacetic acid
-
-
magnesium protoporphyrin IX monomethyl ester
-
-
magnesium protoporphyrin monomethyl ester
manganese III-protoporphyrin
non-substrate metalloporphyrin, non-competitive or un-competitive, assay described
Manganic protoporphyrin
-
-
Manganous protoporphyrin
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-
pheophorbide a
-
stronger inhibitor than the corresponding Mg-chelate
protochlorophyllide a
-
-
Protopheophorbide
-
stronger inhibitor than the corresponding Mg-chelate
S-adenosyl-L-homocysteine
S-adenosylethionine
sinefungin
-
selective inhibitor and potentially usefull tool for chlorophyll biosynthetic studies
Sodium azide
-
-
Sodium diethyldithiocarbamate
-
-
additional information
higher magnesium ion concentrations above 3.8 mM inhibit enzyme activity in presence or absence of magnesium-chelatase subunits or BSA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
magnesium chelatase
-
0.004 mM, maximal stimulation of activity
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Phospholipids
increase enzymatic activity 3-4fold
thiol compounds
-
stimulate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
magnesium deuteroporphyrin
determined using 250 microM S-adenosyl-L-methionine
0.001
magnesium mesoporphyrin
determined using 250 microM S-adenosyl-L-methionine
0.0006
magnesium protoporphyrin
-
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
0.036 - 0.048
magnesium protoporphyrin IX
0.053
protoporphyrin
-
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
0.0173 - 0.048
S-adenosyl-L-methionine
0.0008
zinc protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
magnesium deuteroporphyrin
Rhodobacter capsulatus
P26236
determined using 250 microM S-adenosyl-L-methionine
0.04 - 0.14
magnesium protoporphyrin
0.0002
protoporphyrin
Chlorobaculum tepidum
-
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
0.018
zinc protoporphyrin
Rhodobacter capsulatus
P26236
determined using 250 microM S-adenosyl-L-methionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045 - 0.00061
magnesium protoporphyrin monomethyl ester
0.121 - 0.141
S-adenosyl-L-homocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
continuous spectrophotometric assay
7.7
-
phosphate buffer
8
slight preference for Tris/HCl buffer over Tricine/NaOH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 8.8
-
pH 6.7: about 60% of maximal activity, pH 8.8: about 85% of maximal activity
7.5 - 8.5
within activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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8 day plants, different light conditions
Manually annotated by BRENDA team
-
etiolated
Manually annotated by BRENDA team
additional information
-
no activity can be detected in extracts of Rhodopseudomonas sphaeroides grown under high aeration in the dark
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
dual localization in chloroplast envelope membranes as well as in thylakoids
Manually annotated by BRENDA team
-
containing photoactive protochlorophyllide
Manually annotated by BRENDA team
-
embedded within one leaflet of the membrane
Manually annotated by BRENDA team
-
CHLH protein matured and accumulated inside plastids
Manually annotated by BRENDA team
-
enzyme is synthesized in the 80S cytoplasmic ribosomes
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
His6-tagged protein, gel filtration, SDS-PAGE
30000
-
determined by SDS-PAGE and Western Blot analysis
32000
determined by SDS-PAGE and Western Blot analysis
144000
-
mature protein, SDS-PAGE, mutant and wild-type
154000
-
unprocessed precursor protein, mutant
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25681, calculation from nucleotide sequence
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with S-adenosylmethionine and S-adenosylhomocysteine at resolutions of 1.6 and 1.7 A, respectively. Conformational changes of the two arm regions may modulate binding and release of substrates/products to and from the active site. Residues Tyr28 and His 139 play essential roles for methyl transfer reaction but are not indispensable for cofactor/substrate binding
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration
-
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration; recombinant protein, gel filtration and SDS-PAGE
-
from inclusion bodies, gel filtration and SDS-PAGE
recombinant protein, gel filtration and SDS-PAGE
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using a chelating Sepharose Fast Flow resin charged with 50 mM NiSO4
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a cDNA library is constructed
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
expressed in Escherichia coli
-
expressed in Escherichia coli; expression in Escherichia coli, pCambia derivative, binary vector introduced into the GV3121 strain of Agrobacterium tumefaciens, transgenic plants generated, EYFP fusion protein for localization studies, insertion of the T-DNA in single intron present in the coding sequence, deletion of the 5' part of the gene including the entire first exon, null-mutant
-
expression in Escherichia coli
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
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for sequence determination, mutant complementation
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into the vector pET9a for expression in Escherichia coli BL21DE3 cells
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overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the decrease of the methylation index, the S-adenosyl-L-methionine - S-adenosyl-L-homocysteine ratio, reduces the activity of Mg-protoporphyrin IX methyltransferase, gene expression and protein concentration remain unchanged
the H subunit of Mg chelatase, ChlH, stimulates ChlM activity
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L271P
-
naturally occuring mutation, Mg-protoporphyrin IX accumulated in the mutant, a low activity of the mutant protein is not excluded
H139A
loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein
H139N
loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein
H139Q
loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein
Y28A
loss of more than 80% of methyltransferase activity, mutant has comparable Kd values for Mg-phosphate as the wild type protein
Y28F
mutation leads to inclusion body formation during bacterial expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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a continuous enzyme-coupled spectrophotometric assay for ChlM from Synechocystis sp. PCC 6803 is reported
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