2.1.1.11: magnesium protoporphyrin IX methyltransferase
This is an abbreviated version!
For detailed information about magnesium protoporphyrin IX methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.11
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2.1.1.11
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chlorophyll
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chlm
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chelatase
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tetrapyrrole
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chloroplast
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synechocystis
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plastid
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monomethyl
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branchpoint
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protochlorophyllide
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mg-chelatase
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monomethylester
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5-aminolevulinate
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rhodobacter
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capsulatus
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bacteriochlorophyll
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plastid-to-nucleus
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photosystems
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nonautonomous
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quenched-flow
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chlorophyll-deficient
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ferrochelatase
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analysis
- 2.1.1.11
- chlorophyll
- chlm
- chelatase
- tetrapyrrole
- chloroplast
- synechocystis
- plastid
-
monomethyl
-
branchpoint
- protochlorophyllide
-
mg-chelatase
-
monomethylester
- 5-aminolevulinate
-
rhodobacter
- capsulatus
- bacteriochlorophyll
-
plastid-to-nucleus
-
photosystems
-
nonautonomous
-
quenched-flow
-
chlorophyll-deficient
-
ferrochelatase
- analysis
Reaction
Synonyms
(-)-S-adenosyl-L-methionine:magnesium-protoporphyrin IX methyltransferase, BchM, ChlM, LOC_Os06g04150, magnesium protoporphyrin IX methyltransferase, magnesium protoporphyrin methyltransferase, magnesium protoporphyrin O-methyltransferase, methyltransferase, magnesium protoporphyrin, Mg-protoporphyrin IX methyltransferase, MgPIXMT protein, MgPMT, S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase, Ygl18
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Specific Activity
Specific Activity on EC 2.1.1.11 - magnesium protoporphyrin IX methyltransferase
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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
additional information
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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
additional information
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