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IUBMB Comments This enzyme participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway. See EC 2.1.1.130 , precorrin-2 C 20
Synonyms
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20-methyl transferase of corrin biosynthesis
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precorrin-2 methyltransferase
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CbiL
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CbiL
belongs to the class III methyltransferases
CbiL
belongs to the class III methyltransferases
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CbiL
belongs to the class III methyltransferases
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S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III
S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III
Involved in the anaerobic biosynthesis of vitamin B12
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S-adenosyl-L-methionine + cobalt-factor II = S-adenosyl-L-homocysteine + cobalt-factor III
Gly11, Gly103 and Asp104 involved in S-adenosyl-L-methionine binding
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
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
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methyl group transfer
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MetaCyc
cob(II)yrinate a,c-diamide biosynthesis I (early cobalt insertion)
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S-adenosyl-L-methionine:cobalt-factor-II C20-methyltransferase
This enzyme participates in the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway. See EC 2.1.1.130, precorrin-2 C20-methyltransferase, for the equivalent enzyme that participates in the aerobic cobalamin biosynthesis pathway.
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S-adenosyl-L-methionine + Co(II)-cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: -
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S-adenosyl-L-methionine + Co(II)-precorrin-2
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
S-adenosyl-L-methionine + Co(II)2,7-dimethyl-dipyrrocorphin
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
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Substrates: -
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S-adenosyl-L-methionine + Co(III)2,7-dimethyl-isobacteriochlorin
S-adenosyl-L-homocysteine + Co(III)-factor-III
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Substrates: -
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
additional information
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Substrates: metal-free factor II does not serve as substrate
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S-adenosyl-L-methionine + Co(II)-precorrin-2
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
Substrates: slow reaction with low product yield
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S-adenosyl-L-methionine + Co(II)-precorrin-2
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
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Substrates: -
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S-adenosyl-L-methionine + Co(II)-precorrin-2
S-adenosyl-L-homocysteine + Co(II)-precorrin-3
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Substrates: C-methylation at C-20
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
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Substrates: -
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, important step in ring contraction
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: -
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
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Substrates: -
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
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Substrates: involved in anaerobic biosynthesis of vitamin B12
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, key modification for the ring contraction process
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
Substrates: key enzyme of the anaerobic cobalamin biosynthesis, important step in ring contraction
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
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Substrates: -
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S-adenosyl-L-methionine + cobalt-factor II
S-adenosyl-L-homocysteine + cobalt-factor III
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Substrates: involved in anaerobic biosynthesis of vitamin B12
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Co2+
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absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
Ni2+
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absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
Zn2+
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absolute requirement for the presence of a metal ion within the tetrapyrrole substrate
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UniProt
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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28000
2 * 28000, SDS-PAGE, native mass by gel filtration
29000
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SDS-PAGE
29000
2 * 29000, SDS-PAGE, recombinant His-tagged protein, native mass by gel filtration
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dimer
2 * 28000, SDS-PAGE, native mass by gel filtration
dimer
crystal structure analysis
dimer
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2 * 28000, SDS-PAGE, native mass by gel filtration
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dimer
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crystal structure analysis
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dimer
2 * 29000, SDS-PAGE, recombinant His-tagged protein, native mass by gel filtration
dimer
crystal structure analysis
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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
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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
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hanging-drop vapor-diffusion method, His-tagged CbiL
recombinant protein using His-tag
recombinant proteins from Escherichia coli
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cbi genes from the 17.5 kb cob operon subcloned and expressed in Escherichia coli
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complementation studies with the Salmonella enterica mutant strain AR3711, wild type but non of the mutant proteins complements enzyme deficiency of the host strain
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
wild type and mutant proteins expressed as His-tag fusion protein in Escherichia coli Rosetta(DE3)pLysS
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Roessner, C.A.; Warren, M.J.; Santander, P.J.; Atshaves, B.P.; Ozaki, S.i.; Stolowich, N.J.; Iida, K.
Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis. Identification of the 11-methyl and 20-methyl transferases of corrin biosynthesis
FEBS Lett.
301
73-78
1992
Salmonella enterica subsp. enterica serovar Typhimurium
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Spencer, P.; Stolowich, N.J.; Sumner, L.W.; Scott, A.I.
Definition of the redox states of cobalt-precorrinoids: investigation of the substrate and redox specificity of CbiL from Salmonella typhimurium
Biochemistry
37
14917-14927
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Frank, S.; Brindley, A.A.; Deery, E.; Heathcote, P.; Lawrence, A.D.; Leech, H.K.; Pickersgill, R.W.; Warren, M.J.
Anaerobic synthesis of vitamin B(12): characterization of the early steps in the pathway
Biochem. Soc. Trans.
33
811-814
2005
Methanothermobacter thermautotrophicus
brenda
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
FEBS J.
274
563-573
2007
Chlorobaculum tepidum, Chlorobaculum tepidum (Q8KFD9), Chlorobaculum tepidum ATCC 49652 (Q8KFD9)
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Frank, S.; Deery, E.; Brindley, A.A.; Leech, H.K.; Lawrence, A.; Heathcote, P.; Schubert, H.L.; Brocklehurst, K.; Rigby, S.E.; Warren, M.J.; Pickersgill, R.W.
Elucidation of substrate specificity in the cobalamin (vitamin B12) biosynthetic methyltransferases. Structure and function of the C20 methyltransferase (CbiL) from Methanothermobacter thermautotrophicus
J. Biol. Chem.
282
23957-23969
2007
Methanothermobacter thermautotrophicus (O27402)
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