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Information on EC 2.1.1.11 - magnesium protoporphyrin IX methyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SW18

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Arabidopsis thaliana
UNIPROT: Q9SW18 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mg-protoporphyrin ix methyltransferase, mgpmt, magnesium protoporphyrin ix methyltransferase, magnesium protoporphyrin methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase
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magnesium protoporphyrin IX methyltransferase
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magnesium protoporphyrin O-methyltransferase
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methyltransferase, magnesium protoporphyrin
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Mg-protoporphyrin IX methyltransferase
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MgPIXMT protein
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S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9029-82-7
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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 + magnesium mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
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-
-
-
?
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
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-
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin IX
S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
about 80% increase in activity in presence of dithiothreitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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8 day plants, different light conditions
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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dual localization in chloroplast envelope membranes as well as in thylakoids
Manually annotated by BRENDA team
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embedded within one leaflet of the membrane
Manually annotated by BRENDA team
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CHLH protein matured and accumulated inside plastids
Manually annotated by BRENDA team
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dual localization in chloroplast envelope membranes as well as in thylakoids
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
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Mg-protoporphyrin IX methyltransferase activity is the link between methyl cycle and chlorophyll synthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CHLM_ARATH
312
0
33796
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
PAGE, part of protein
70000
PAGE, part of protein
144000
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mature protein, SDS-PAGE, mutant and wild-type
154000
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unprocessed precursor protein, mutant
30000
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determined by SDS-PAGE and Western Blot analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C111S
0.1% of wild-type activity
C111S/C115S
only residual in vitro activity under reducing conditions, almost complete loss of activity under non-reducing conditions
C115S
20% of wild-type activity, strong stimulation by dithiothreitol
C115S/C177S
only residual in vitro activity under reducing conditions, almost complete loss of activity under non-reducing conditions
C177S
residue is responsible for redox-dependent enzyme activation. In absence of dithiothreitol, increased activity compared with wild-type. Only slight activation by dithiothreitol
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration
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recombinant protein, gel filtration and SDS-PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
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expression in Escherichia coli
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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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Block, M.A.; Tewari, A.K.; Albrieux, C.; Marechal, E.; Joyard, J.
The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes
Eur. J. Biochem.
269
240-248
2002
Arabidopsis thaliana, Spinacia oleracea
Manually annotated by BRENDA team
Pontier, D.; Albrieux, C.; Joyard, J.; Lagrange, T.; Block, M.A.
Knock-out of the magnesium protoporphyrin IX methyltransferase gene in Arabidopsis. Effects on chloroplast development and on chloroplast-to-nucleus signaling
J. Biol. Chem.
282
2297-2304
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Van Wilder, V.; De Brouwer, V.; Loizeau, K.; Gambonnet, B.; Albrieux, C.; Van Der Straeten, D.; Lambert, W.E.; Douce, R.; Block, M.A.; Rebeille, F.; Ravanel, S.
C1 metabolism and chlorophyll synthesis: the Mg-protoporphyrin IX methyltransferase activity is dependent on the folate status
New Phytol.
182
137-145
2009
Arabidopsis thaliana, Pisum sativum (B5U883), Pisum sativum
Manually annotated by BRENDA team
Tomiyama, M.; Inoue, S.; Tsuzuki, T.; Soda, M.; Morimoto, S.; Okigaki, Y.; Ohishi, T.; Mochizuki, N.; Takahashi, K.; Kinoshita, T.
Mg-chelatase I subunit 1 and Mg-protoporphyrin IX methyltransferase affect the stomatal aperture in Arabidopsis thaliana
J. Plant Res.
127
553-563
2014
Arabidopsis thaliana (Q9SW18), Arabidopsis thaliana
Manually annotated by BRENDA team
Richter, A.S.; Wang, P.; Grimm, B.
Arabidopsis Mg-protoporphyrin IX methyltransferase activity and redox regulation depend on conserved cysteines
Plant Cell Physiol.
57
519-527
2016
Arabidopsis thaliana (Q9SW18)
Manually annotated by BRENDA team