Information on EC 2.1.1.272 - cobalt-factor III methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacillus megaterium

EC NUMBER
COMMENTARY hide
2.1.1.272
-
RECOMMENDED NAME
GeneOntology No.
cobalt-factor III methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cobalt-factor III + reduced acceptor = S-adenosyl-L-homocysteine + cobalt-precorrin-4 + acceptor
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
vitamin B12 metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:cobalt-factor III 17-methyltransferase (ring contracting)
Isolated from Bacillus megaterium. The enzyme catalyses both methylation at C-17 and ring contraction. Contains a [4Fe-4S] cluster. It can also convert cobalt-precorrin-3 to cobalt-precorrin-4. The reductant may be thioredoxin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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 + cobalt(II)-factor-III + dithiothreitol
S-adenosyl-L-homocysteine + cobalt(II)-precorrin-4 + oxidized dithiothreitol
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + cobalt(II)-precorrin-3
S-adenosyl-L-homocysteine + cobalt(II)-factor-IV
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
enzyme contains a [4Fe-4S]-center required for ring contraction reaction. Iron content is 4.8 mol of iron/mol of enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, SDS-PAGE of recombinant enzyme including His-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Bacillus megaterium DSM319
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C402A
mutation introduced to disrupt the iron-sulfur center. Mutant lacks any visible coloration and has decreased absorbance between 350 and 420 nm and less than 95% of wild-type activity
C443A
mutation introduced to disrupt the iron-sulfur center. Mutant lacks any visible coloration and has decreased absorbance between 350 and 420 nm and less than 95% of wild-type activity