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Information on EC 2.1.1.11 - magnesium protoporphyrin IX methyltransferase and Organism(s) Rhodobacter capsulatus and UniProt Accession P26236

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This record set is specific for:
Rhodobacter capsulatus
UNIPROT: P26236 not found.
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The taxonomic range for the selected organisms is: Rhodobacter capsulatus
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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S-adenosyl-L-methionine:Mg protoporphyrin methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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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 deuteroporphyrin
S-adenosyl-L-homocysteine + magnesium deuteroporphyrin monomethyl ester
show the reaction diagram
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
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-
?
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
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay
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-
?
S-adenosyl-L-methionine + zinc protoporphyrin
S-adenosyl-L-homocysteine + zinc protoporphyrin monomethyl ester
show the reaction diagram
in situ generated S-adenosyl-L-methionine substrate reveals higher enzymatic activity in assay, substrate specificity limited to 5-co-ordinate squarepyramidal metalloporphyrins
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-
?
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
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-
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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 mesoporphyrin
S-adenosyl-L-homocysteine + magnesium mesoporphyrin monomethyl ester
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cobalt II-protoporphyrin
non-substrate metalloporphyrin, competitive, assay described
magnesium protoporphyrin monomethyl ester
non-competitive product inhibition
manganese III-protoporphyrin
non-substrate metalloporphyrin, non-competitive or un-competitive, assay described
S-adenosyl-L-homocysteine
non-competitive product inhibition
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
Phospholipids
increase enzymatic activity 3-4fold
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
0.045
S-adenosyl-L-methionine
previously determined constant
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
determined using 250 microM S-adenosyl-L-methionine
0.04
magnesium protoporphyrin
determined using 250 microM S-adenosyl-L-methionine
0.018
zinc protoporphyrin
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
slight preference for Tris/HCl buffer over Tricine/NaOH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
within activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BCHM_RHOCA
224
0
25225
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
His6-tagged protein, gel filtration, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
disaggregation to lower molecular mass forms, monomeric to multimeric species, gel filtration
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
phosphatidylglycerol stabilizes enzymatic activity causing disaggregation to lower molecular mass forms
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from inclusion bodies, gel filtration and SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bollivar, D.W.; Jiang, Z.Y.; Bauer, C.E.; Beale, S.I.
Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-l-methionine:Mg-protoporphyrin IX methyltransferase
J. Bacteriol.
176
5290-5296
1994
Rhodobacter capsulatus
Manually annotated by BRENDA team
Sawicki, A.; Willows, R.D.
S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase from Rhodobacter capsulatus: mechanistic insights and stimulation with phospholipids
Biochem. J.
406
469-478
2007
Rhodobacter capsulatus (P26236)
Manually annotated by BRENDA team