Information on EC 2.1.1.151 - cobalt-factor II C20-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: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.1.1.151
-
RECOMMENDED NAME
GeneOntology No.
cobalt-factor II C20-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion)
-
-
vitamin B12 metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:cobalt-factor-II C20-methyltransferase
Involved in the anaerobic biosynthesis of vitamin B12.
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 + Co(II)-cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + Co(II)-precorrin-2
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
show the reaction diagram
S-adenosyl-L-methionine + Co(II)2,7-dimethyl-dipyrrocorphin
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + Co(III)2,7-dimethyl-isobacteriochlorin
S-adenosyl-L-homocysteine + Co(III)-factor-III
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
show the reaction diagram
additional information
?
-
metal-free factor II does not serve as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
Ni2+
-
absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
Zn2+
-
absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of Chlorobium tepidum CbiL and CbiL in complex with S-adenosylhomocysteine (the S-demethyl form of S-adenosylmethionine). CbiL forms a dimer in the crystal, and each subunit consists of N-terminal and C-terminal domains. S-Adenosylhomocysteine binds to a cleft between the two domains, where it is specifically recognized by extensive hydrogen bonding and van der Waals interactions; hanging-drop vapor-diffusion method, complex with S-adenosylhomocystein obtained by soaking of ready crystals in S-adenosylhomocystein solution
crystallized by hanging drop vapor diffusion method in the presence of S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, crystals complemented with substrate by soaking in substrate solution, no crystal growth in the absence of S-adenosyl-L-methionine or S-adenosyl-L-homocysteine
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method, His-tagged CbiL; recombinant protein using His-tag
recombinant proteins from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
cbi genes from the 17.5 kb cob operon subcloned and expressed in Escherichia coli
-
complementation studies with the Salmonella enterica mutant strain AR3711, wild type but non of the mutant proteins complements enzyme deficiency of the host strain; wild type and mutant proteins expressed as His-tag fusion protein in Escherichia coli Rosetta(DE3)pLysS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D104A
inactive in vivo as shown by complementation studies with Salmonella enterica, low in vitro activity, reduced affinity for S-adenosyl-L-methionine
K176A
inactive in vivo as shown by complementation studies with Salmonella enterica, no structural changes compared with crystallized wild-type enzyme
Y220A
inactive in vivo as shown by complementation studies with Salmonella enterica
Show AA Sequence (499 entries)
Please use the Sequence Search for a certain query.