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

BRENDA support

Literature summary extracted from

  • 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 (2007), J. Biol. Chem., 282, 23957-23969.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.151 complementation studies with the Salmonella enterica mutant strain AR3711, wild type but non of the mutant proteins complements enzyme deficiency of the host strain Methanothermobacter thermautotrophicus
2.1.1.151 wild type and mutant proteins expressed as His-tag fusion protein in Escherichia coli Rosetta(DE3)pLysS Methanothermobacter thermautotrophicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.151 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 Methanothermobacter thermautotrophicus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.151 D104A inactive in vivo as shown by complementation studies with Salmonella enterica, low in vitro activity, reduced affinity for S-adenosyl-L-methionine Methanothermobacter thermautotrophicus
2.1.1.151 K176A inactive in vivo as shown by complementation studies with Salmonella enterica, no structural changes compared with crystallized wild-type enzyme Methanothermobacter thermautotrophicus
2.1.1.151 Y220A inactive in vivo as shown by complementation studies with Salmonella enterica Methanothermobacter thermautotrophicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.151 29000
-
 2 * 29000, SDS-PAGE, recombinant His-tagged protein, native mass by gel filtration Methanothermobacter thermautotrophicus
2.1.1.151 51000
-
 gel filtration Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.151 S-adenosyl-L-methionine + cobalt-factor II Methanothermobacter thermautotrophicus key enzyme of the anaerobic cobalamin biosynthesis, important step in ring contraction S-adenosyl-L-homocysteine + cobalt-factor III
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.151 Methanothermobacter thermautotrophicus O27402
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.151 recombinant proteins from Escherichia coli Methanothermobacter thermautotrophicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.151 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 Methanothermobacter thermautotrophicus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.151 0.0041
-
 37°C Methanothermobacter thermautotrophicus
2.1.1.151 0.0136
-
 65°C Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.151 additional information metal-free factor II does not serve as substrate Methanothermobacter thermautotrophicus ?
-
 ?
2.1.1.151 S-adenosyl-L-methionine + Co(II)-cobalt-factor II
-
 Methanothermobacter thermautotrophicus S-adenosyl-L-homocysteine + cobalt-factor III
-
 ?
2.1.1.151 S-adenosyl-L-methionine + Co(II)-precorrin-2 slow reaction with low product yield Methanothermobacter thermautotrophicus S-adenosyl-L-homocysteine + Co(II)-precorrin-3
-
 ?
2.1.1.151 S-adenosyl-L-methionine + cobalt-factor II
-
 Methanothermobacter thermautotrophicus S-adenosyl-L-homocysteine + cobalt-factor III
-
 ?
2.1.1.151 S-adenosyl-L-methionine + cobalt-factor II key enzyme of the anaerobic cobalamin biosynthesis, important step in ring contraction Methanothermobacter thermautotrophicus S-adenosyl-L-homocysteine + cobalt-factor III
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.151 dimer crystal structure analysis Methanothermobacter thermautotrophicus
2.1.1.151 dimer 2 * 29000, SDS-PAGE, recombinant His-tagged protein, native mass by gel filtration Methanothermobacter thermautotrophicus

Synonyms

EC Number Synonyms Comment Organism
2.1.1.151 CbiL belongs to the class III methyltransferases Methanothermobacter thermautotrophicus