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
2.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
magnesium protoporphyrin IX methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
ping-pong mechanism
-
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
equilibrium-ordered bi bi mechanism
-
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
random bi-bi mechanism with 2 dead-end ternary complexes
-
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
ternary complex is likely to be formed either by a random or ordered addition of substrates
-
S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
ternary complex is likely to be formed either by a random or ordered addition of substrates
Synechocystis sp. PCC6803
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
methyl group transfer
-
-
methyl group transfer
-
-
methyl group transfer
B5U883, -
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chlorophyllide a biosynthesis I (aerobic, light-dependent)
-
chlorophyllide a biosynthesis II (anaerobic)
-
chlorophyllide a biosynthesis III (aerobic, light independent)
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase
-
-
-
-
ChlM
B5U883
-
ChlM
Synechocystis sp. PCC6803
-
-
-
magnesium protoporphyrin IX methyltransferase
-
-
-
-
magnesium protoporphyrin IX methyltransferase
-
-
magnesium protoporphyrin methyltransferase
-
-
magnesium protoporphyrin methyltransferase
Synechocystis sp. PCC6803
-
-
-
magnesium protoporphyrin O-methyltransferase
-
-
-
-
methyltransferase, magnesium protoporphyrin
-
-
-
-
Mg-protoporphyrin IX methyltransferase
-
-
Mg-protoporphyrin IX methyltransferase
-
-
Mg-protoporphyrin IX methyltransferase
B5U883
-
MgPIXMT protein
-
-
S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-82-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; chlm mutant (ABN42 line) of the ecotype Wassilewskija (WS)
-
-
Manually annotated by BRENDA team
formerly Chlorobium tepidum
-
-
Manually annotated by BRENDA team
strain PCC6803
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
PCC6803
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
strain PCC6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
Mg-protoporphyrin IX methyltransferase activity is the link between methyl cycle and chlorophyll synthesis
physiological function
B5U883, -
Mg-protoporphyrin IX methyltransferase activity is the link between methyl cycle and chlorophyll synthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester
show the reaction diagram
P26236
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
-
-
?
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 mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
P26236
-, in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
-
-
?
S-adenosyl-L-methionine + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
Synechocystis sp. PCC6803
-
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin 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
S-adenosyl-L-homocysteine + magnesium protoporphyrin 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
S-adenosyl-L-homocysteine + magnesium protoporphyrin 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
S-adenosyl-L-homocysteine + magnesium protoporphyrin 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
S-adenosyl-L-homocysteine + magnesium protoporphyrin 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
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
transfer of methyl group from S-adenosylmethionine to the propanoic acid side chain on the third pyrrole ring of magnesium protoporphyrin IX
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
enzyme in the chlorophyll biosynthetic pathway
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
enzyme in the Mg branch of the tetrapyrrole biosynthetic pathway
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
the enzyme is involved in inverse activation of Mg porphyrin and protoheme synthesis
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
rapid binding step is preceded by a slower isomerization of the enzyme
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
reaction proceeds through a ternary complex, substrate binding is not ordered
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
different substrate specificity, protoporphyrin with or without bound metal as a substrate
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
P26236
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
key gene for chlorophyll biosynthesis and chloroplast development, reaction products probably involved in retrograde chloroplast-to-nucleus signalling
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
Synechocystis sp. PCC6803
-
-
-
-
?
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 + magnesium protoporphyrin IX
S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl 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
B5U883, -
-
-
-
?
S-adenosyl-L-methionine + protoporphyrin
S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + protoporphyrin
S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester
show the reaction diagram
-
methyl transfer possible without bound metal, slow reaction rate
-
-
?
S-adenosyl-L-methionine + tetrapyrrole
?
show the reaction diagram
Synechocystis sp., Synechocystis sp. PCC6803
-
-
-
-
?
S-adenosyl-L-methionine + zinc protoporphyrin
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + zinc protoporphyrin
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
show the reaction diagram
P26236
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
-
-
?
additional information
?
-
-
enzyme is involved in bacteriochlorophyll biosynthesis
-
-
-
additional information
?
-
-
chlorophyll-forming enzyme
-
-
-
additional information
?
-
-
enzyme is involved in chlorophyll biosynthesis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
enzyme in the chlorophyll biosynthetic pathway
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
enzyme in the Mg branch of the tetrapyrrole biosynthetic pathway
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
the enzyme is involved in inverse activation of Mg porphyrin and protoheme synthesis
-
-
?
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 + magnesium protoporphyrin IX
S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl 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
B5U883, -
-
-
-
?
additional information
?
-
-
enzyme is involved in bacteriochlorophyll biosynthesis
-
-
-
additional information
?
-
-
chlorophyll-forming enzyme
-
-
-
additional information
?
-
-
enzyme is involved in chlorophyll biosynthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
B5U883, -
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Magnesium
B5U883, -
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
8-hydroxyquinoline
-
-
chlorophyllide a
-
-
cobalt II-protoporphyrin
P26236
non-substrate metalloporphyrin, competitive, assay described
Diphenylthiocarbazone
-
-
Ferric protoporphyrin
-
-
Ferrous protoporphyrin
-
-
Hemin
-
noncompetitive with respect to magnesium protoporphyrin
magnesium protoporphyrin IX monomethyl ester
-
-
magnesium protoporphyrin monomethyl ester
-
noncompetitive inhibitor of S-adenosyl-L-methionine
magnesium protoporphyrin monomethyl ester
P26236
non-competitive product inhibition
manganese III-protoporphyrin
P26236
non-substrate metalloporphyrin, non-competitive or un-competitive, assay described
Manganic protoporphyrin
-
-
Manganous protoporphyrin
-
-
pheophorbide a
-
stronger inhibitor than the corresponding Mg-chelate
protochlorophyllide a
-
-
Protopheophorbide
-
stronger inhibitor than the corresponding Mg-chelate
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
non-competitive inhibitor of Mg protoporphyrin
S-adenosyl-L-homocysteine
-
competitive with S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
competitive with S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
competitive with respect to S-adenosyl-L-methionine and mixed inhibition with respect to magnesium protoporphyrin
S-adenosyl-L-homocysteine
P26236
non-competitive product inhibition
S-adenosylethionine
-
competitive with S-adenosyl-L-methionine
S-adenosylethionine
-
competitive with S-adenosyl-L-methionine
Sinefungin
-
selective inhibitor and potentially usefull tool for chlorophyll biosynthetic studies
Sodium diethyldithiocarbamate
-
-
additional information
P26236
higher magnesium ion concentrations above 3.8 mM inhibit enzyme activity in presence or absence of magnesium-chelatase subunits or BSA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
magnesium chelatase
-
0.004 mM, maximal stimulation of activity
-
Phospholipids
P26236
increase enzymatic activity 3-4fold
thiol compounds
-
stimulate
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0006
-
magnesium deuteroporphyrin
P26236
determined using 250 microM S-adenosyl-L-methionine
0.001
-
magnesium mesoporphyrin
P26236
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
-
magnesium protoporphyrin IX
-
pH 7.7, 25C
0.048
-
magnesium protoporphyrin IX
-
-
0.053
-
protoporphyrin
-
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
0.0173
-
S-adenosyl-L-methionine
-
at 30C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the presence of 0.004 mM magnesium chelatase
0.0243
-
S-adenosyl-L-methionine
-
at 30C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the absence of magnesium chelatase
0.038
-
S-adenosyl-L-methionine
-
-
0.038
-
S-adenosyl-L-methionine
-
-
0.039
-
S-adenosyl-L-methionine
-
-
0.045
-
S-adenosyl-L-methionine
P26236
previously determined constant
0.048
-
S-adenosyl-L-methionine
-
pH 7.7, 25C
0.0008
-
zinc protoporphyrin
P26236
determined using 250 microM S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.003
-
magnesium deuteroporphyrin
P26236
determined using 250 microM S-adenosyl-L-methionine
0.04
-
magnesium protoporphyrin
P26236
determined using 250 microM S-adenosyl-L-methionine
0.14
-
magnesium protoporphyrin
-
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
0.0002
-
protoporphyrin
-
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
0.018
-
zinc protoporphyrin
P26236
determined using 250 microM S-adenosyl-L-methionine
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00045
-
magnesium protoporphyrin monomethyl ester
P26236
non-competitive product inhibition, magnesium deuteroporphyrin as substrate
0.00061
-
magnesium protoporphyrin monomethyl ester
P26236
non-competitive product inhibition, S-adenosyl-L-methionine as substrate
0.121
-
S-adenosyl-L-homocysteine
P26236
non-competitive, magnesium protoporphyrin as substrate
0.141
-
S-adenosyl-L-homocysteine
P26236
non-competitive, S-adenosyl-L-methionine as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
knock-out mutant characterized, tetrapyrole intermediate analysis, RT-PCR and immunoblot analysis, CHLM gene essential for formation of chlorophyll, photosystems I and II and cyt b6f complexes, negative effector of nuclear photosynthetic gene expression, product of CHLM possibly involved in retrograde signaling, post-transcriptional up-regulation in chlm mutants, specific accumulation inside plastids determined, regulatory role of CHLH subunit
additional information
-
P26236
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
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
continuous spectrophotometric assay
7.5
-
-
assay at
7.5
-
-
HPLC-based assay
7.7
-
-
phosphate buffer
8
-
P26236
slight preference for Tris/HCl buffer over Tricine/NaOH
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
P26236
within activity range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
P26236
assay at
30
-
-
assay at
30
-
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
8 day plants, different light conditions
Manually annotated by BRENDA team
-
; chlorophyll fluorescence
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 ACCESSION NO.
COMMENTARY
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
-
dual localization in chloroplast envelope membranes as well as in thylakoids
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
P26236
His6-tagged protein, gel filtration, SDS-PAGE
30000
-
-
determined by SDS-PAGE and Western Blot analysis
32000
-
B5U883, -
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 25681, calculation from nucleotide sequence
additional information
P26236
disaggregation to lower molecular mass forms, monomeric to multimeric species, gel filtration
additional information
-
majority of the protein exist as a high-molecular-weight multimer as determined by gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
the full-length polypeptide exhibits a chloroplast transit peptide which is processed during import into the chloroplast
proteolytic modification
-
processing of transit peptide during import into chloroplast
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms
P26236
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration; recombinant protein, gel filtration and SDS-PAGE
-
recombinant protein, gel filtration and SDS-PAGE
-
from inclusion bodies, gel filtration and SDS-PAGE
P26236
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration
-
using a chelating Sepharose Fast Flow resin charged with 50 mM NiSO4
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
for sequence determination, mutant complementation
-
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
-
overexpression in Escherichia coli
-
a cDNA library is constructed
B5U883, -
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
P26236
expression in Escherichia coli
-
overexpression in Escherichia coli
-
expressed in Escherichia coli
-
into the vector pET9a for expression in Escherichia coli BL21DE3 cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
B5U883, -
the H subunit of Mg chelatase, ChlH, stimulates ChlM activity
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L271P
-
naturally occuring mutation, Mg-protoporphyrin IX accumulated in the mutant, a low activity of the mutant protein is not excluded
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
a continuous enzyme-coupled spectrophotometric assay for ChlM from Synechocystis sp. PCC 6803 is reported