Literature summary for 2.1.1.151 extracted from

Wada, K.; Harada, J.; Yaeda, Y.; Tamiaki, H.; Oh-Oka, H.; Fukuyama, K.
Crystal structures of CbiL, a methyltransferase involved in anaerobic vitamin B biosynthesis, and CbiL in complex with S-adenosylhomocysteine - implications for the reaction mechanism (2007), FEBS J., 274, 563-573.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Chlorobaculum tepidum
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)	Chlorobaculum tepidum

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Chlorobaculum tepidum
hanging-drop vapor-diffusion method, complex with S-adenosylhomocystein obtained by soaking of ready crystals in S-adenosylhomocystein solution	Chlorobaculum tepidum

Crystallization (Comment)

Organism

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

Chlorobaculum tepidum

hanging-drop vapor-diffusion method, complex with S-adenosylhomocystein obtained by soaking of ready crystals in S-adenosylhomocystein solution

Chlorobaculum tepidum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	2 * 28000, SDS-PAGE, native mass by gel filtration	Chlorobaculum tepidum
56000	-	gel filtration	Chlorobaculum tepidum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + cobalt-factor II	Chlorobaculum tepidum	key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process	S-adenosyl-L-homocysteine + cobalt-factor III	-	?
S-adenosyl-L-methionine + cobalt-factor II	Chlorobaculum tepidum ATCC 49652	key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process	S-adenosyl-L-homocysteine + cobalt-factor III	-	?

Organism

Organism	UniProt	Comment	Textmining
Chlorobaculum tepidum	-	-	-
Chlorobaculum tepidum	Q8KFD9	-	-
Chlorobaculum tepidum ATCC 49652	Q8KFD9	-	-

Purification (Commentary)

Purification (Comment)	Organism
hanging-drop vapor-diffusion method, His-tagged CbiL	Chlorobaculum tepidum
recombinant protein using His-tag	Chlorobaculum tepidum

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III	the conserved Tyr226 residue in CbiL catalyzes the direct transfer of a methyl group from S-adenosylmethionine to the substrate through an SN2-like mechanism, S-adenosyl-L-homocysteine binds to Pro14, Asp106, Phe109, Ala135, and Val205, as well as to Val104 and Phe136 via a water molecule	Chlorobaculum tepidum	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + cobalt-factor II	key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process	Chlorobaculum tepidum	S-adenosyl-L-homocysteine + cobalt-factor III	-	?
S-adenosyl-L-methionine + cobalt-factor II	key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process	Chlorobaculum tepidum ATCC 49652	S-adenosyl-L-homocysteine + cobalt-factor III	-	?

Subunits

Subunits	Comment	Organism
dimer	crystal structure analysis	Chlorobaculum tepidum
dimer	2 * 28000, SDS-PAGE, native mass by gel filtration	Chlorobaculum tepidum

Synonyms

Synonyms	Comment	Organism
CbiL	-	Chlorobaculum tepidum
CbiL	belongs to the class III methyltransferases	Chlorobaculum tepidum