Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.11 - magnesium protoporphyrin IX methyltransferase and Organism(s) Synechocystis sp. and UniProt Accession Q55467

for references in articles please use BRENDA:EC2.1.1.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Synechocystis sp.
UNIPROT: Q55467 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
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
-
-
-
-
magnesium protoporphyrin IX methyltransferase
-
-
-
-
magnesium protoporphyrin methyltransferase
-
-
magnesium protoporphyrin O-methyltransferase
-
-
-
-
methyltransferase, magnesium protoporphyrin
-
-
-
-
S-adenosyl-L-methionine:Mg protoporphyrin 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
ternary complex is likely to be formed either by a random or ordered addition of substrates
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-82-7
-
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
-
-
-
-
?
S-adenosyl-L-methionine + magnesium protoporphyrin
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + tetrapyrrole
?
show the reaction diagram
-
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
magnesium chelatase
-
0.004 mM, maximal stimulation of activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0173 - 0.038
S-adenosyl-L-methionine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chelating Sepharose fast-flow resin column chromatography and P-6 desalting gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shepherd, M.; Reid, J.D.; Hunter, C.N.
Purification and kinetic characterisation of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803
Biochem. J.
371
351-360
2003
Synechocystis sp., Synechocystis sp. PCC 6803
Manually annotated by BRENDA team
Shepherd, M.; McLean, S.; Hunter, C.N.
Kinetic basis for linking the first two enzymes of chlorophyll biosynthesis
FEBS J.
272
4532-4539
2005
Synechocystis sp.
Manually annotated by BRENDA team
Chen, X.; Wang, X.; Feng, J.; Chen, Y.; Fang, Y.; Zhao, S.; Zhao, A.; Zhang, M.; Liu, L.
Structural insights into the catalytic mechanism of Synechocystis magnesium protoporphyrin IX O-methyltransferase (ChlM)
J. Biol. Chem.
289
25690-25698
2014
Synechocystis sp. (Q55467)
Manually annotated by BRENDA team