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Ligand Cobalamin
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Basic Ligand Information
KEGG
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
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2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
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In Vivo Product in Enzyme-catalyzed Reactions (1 result)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Substrate in Enzyme-catalyzed Reactions (63 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
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2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
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2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
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Product in Enzyme-catalyzed Reactions (2 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin = (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
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Enzyme Cofactor/Cosubstrate (130 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
vitamin B12-requiring mutants of the bluE and bluB genes of Rhodobacter capsulatus, grown without B12, accumulate Mg-protoporphyrin monomethyl ester and its 3-vinyl-8-ethyl derivative. Cyclase activity in the B12-dependent mutants requires vitamin B12 but not protein synthesis
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cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms
cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms
cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms
cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms
cobalamin serves as an intermediary in methyl transfer reactions, and it cycles between the methylcob(III)alamin and cob(I)alamin forms
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket
preparation of a synthetic conjugate between apomyoglobin and cobalt tetradehydrocorrin to replicate the coordination behavior of cob(I)alamin in methionine synthase. The tetracoordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket
interaction of Co(II)cobalamin and cob(II)inamide (Co(II)Cbi+) with EutT in the absence and presence of cosubstrate ATP. EutT displays a similar substrate specificity as Salmonella enterica EutT and can bind both Co(II)cobalamin and Co(II)Cbi+ when complexed with MgATP, though it exclusively converts Co(II)cobalamin to a four-coordinate species. Listeria monocytogenes EutT achieves a more than 98% conversion yield of the five-coordinate to four-coordinate state on addition of just over one molar equivalent of cosubstrate MgATP
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the reduced catalytic activity of EutT wild-type in complex with Co relative to the Fe(II)-containing enzyme arises from the incomplete incorporation of Co(II) ions and, thus, a decrease in the relative population of four-coordinate Co(II)Cbl. The Co(II) ions reside in a distorted tetrahedral coordination environment with direct cysteine sulfur ligation. Residues in the HX11CCX2C(83) motif are required for the tight binding of the divalent metal ion and are critical for the formation of a four-coordinate cob(II)alamin intermediate. Residue Cys80 coordinates to the Co(II) ion, while the additional residues are important for maintaining the structural integrity and/or high affinity of the metal binding site
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roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
required, directly involved in the catalysis of the amino group migration
and at least seven analogs containing bases other than dimethylbenzimidazolyl can serve as coenzymes
and at least seven analogs containing bases other than dimethylbenzimidazolyl can serve as coenzymes
and at least seven analogs containing bases other than dimethylbenzimidazolyl can serve as coenzymes
coenzyme binding and catalysis is very sensitive to mutations at position 15
coenzyme binding and catalysis is very sensitive to mutations at position 15
coenzyme binding and catalysis is very sensitive to mutations at position 15
requires Co(II) for coordination of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product
requires Co(II) for coordination of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product
requires Co(II) for coordination of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product
the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
the weakly associated subunits E and S combine to form the coenzyme binding site. Interactions between the protein and the adenosyl moiety do not serve to weaken the cobalt-carbon bond in the ground state, variation of the apparent Km-value for adenosylcobalamine with protein concentration. Km: 0.0055 mM in the reaction with L-Glu, Km: 0.0031 mM in the reaction with (2S,3S)-3-methylaspartate, genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment
the weakly associated subunits E and S combine to form the coenzyme binding site. Interactions between the protein and the adenosyl moiety do not serve to weaken the cobalt-carbon bond in the ground state, variation of the apparent Km-value for adenosylcobalamine with protein concentration. Km: 0.0055 mM in the reaction with L-Glu, Km: 0.0031 mM in the reaction with (2S,3S)-3-methylaspartate, genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment
the weakly associated subunits E and S combine to form the coenzyme binding site. Interactions between the protein and the adenosyl moiety do not serve to weaken the cobalt-carbon bond in the ground state, variation of the apparent Km-value for adenosylcobalamine with protein concentration. Km: 0.0055 mM in the reaction with L-Glu, Km: 0.0031 mM in the reaction with (2S,3S)-3-methylaspartate, genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
dependent on, 2 mol of cobalamin bound per mol of enzyme, are covalently attached
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
essential to the function of methylmalonyl-CoA mutase, cobalamin is conversed to adenosylcobalamin
Activator in Enzyme-catalyzed Reactions (6 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Inhibitor in Enzyme-catalyzed Reactions (1 result)
Metals and Ions (5 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
3D Structure of Enzyme-Ligand-Complex (PDB) (64 results)
EC NUMBER
ENZYME 3D STRUCTURE
Enzyme Kinetic Parameters
kcat Value (Turnover Number) (23 results)
EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
0.05
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mutant D110N, pH not specified in the publication, temperature not specified in the publication
0.06
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mutant R200K, pH not specified in the publication, temperature not specified in the publication
0.18
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mutant K98Q, pH not specified in the publication, temperature not specified in the publication
0.21
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wild-type, pH not specified in the publication, temperature not specified in the publication
0.22
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mutant E207Q, pH not specified in the publication, temperature not specified in the publication
0.26
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mutant T88V, pH not specified in the publication, temperature not specified in the publication
KM Value (19 results)
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0042
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wild-type, Khalf value, Hill coefficient 1.9, pH not specified in the publication, temperature not specified in the publication
0.0092
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mutant D110N, Khalf value, Hill coefficient 2.5, pH not specified in the publication, temperature not specified in the publication
0.0094
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mutant R200K, Khalf value, Hill coefficient 1.9, pH not specified in the publication, temperature not specified in the publication
0.0105
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mutant T88V, Khalf value, Hill coefficient 1.8, pH not specified in the publication, temperature not specified in the publication
0.0427
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mutant K98Q, Khalf value, Hill coefficient 1.7, pH not specified in the publication, temperature not specified in the publication
0.0448
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mutant E207Q, Khalf value, Hill coefficient 2.4, pH not specified in the publication, temperature not specified in the publication
Ki Value (2 results)
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
References & Links
Literature References (73)
Links to other databases for Cobalamin
ChEBI
PubChem
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Release 2023.1 (January 2023)
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