BRENDA - Enzyme Database
show all sequences of 2.5.1.17

Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate

St Maurice, M.; Mera, P.; Park, K.; Brunold, T.C.; Escalante-Semerena, J.C.; Rayment, I.; Biochemistry 47, 5755-5766 (2008)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
ACA-mediated catalysis provides insights in molecular basis for dysfunction in methylmalonic aciduria
Lactobacillus reuteri
Crystallization (Commentary)
Crystallization
Organism
trimer of three independent five-helix bundles, active sites at the interface between adjacent monomers, no significant structural changes accompany catalysis, precatalytic complex with ATP: cob(II)alamin (PDB: 3CI1, four-coordinate, base-off cob(II)alamin intermediate, enzyme with fully ordered six C-terminal residues and potassium ion in active site), complex with tripolyphosphate: adenosylcobalamin (PDB: 3CI3, partially occupied with five-coordinate adenosylcobalamin), precatalytic complex with ATP: cob(II)inamide (PDB: 3CI4, cob(II)inamide-binding structurally indistinguishable from cob(II)alamin-binding), binding of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) in identical positions and orientation, space group R3, one molecule in asymmetric unit, unit cell parameters: a: 67.8-68, b: 67.8-68, c: 110.9-111.3, beta: 90°, molecular replacement using PDB: 2NT8 as model; vapour-diffusion with tag-cleaved protein solution (18-22 mg/ml, in presence of hydroxycobalamin and/or adenosylcobalamin or dicyanocobinamide, ATP etc.) and reservoir solution (10-13% (w/v) PEG 8000, pH 6), cubic crystals, crystallisation under anoxic conditions in presence of flavin-dependent reducing system
Lactobacillus reuteri
Inhibitors
Inhibitors
Commentary
Organism
Structure
cobinamide
substrate inhibition
Lactobacillus reuteri
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactobacillus reuteri
-
-
-
Reaction
Reaction
Commentary
Organism
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein
not yet confimed
Lactobacillus reuteri
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0005
-
in presence of 1 mM ATP, 20 mM NADH, 2 mM FMN, 0.5 mM hydroxycobalamin and NAD(P)H: flavin oxidoreductase, 1.5 mM MgCl2, 100 mM KCl, pH 6
Lactobacillus reuteri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + hydroxycobalamin
coenzyme B12 synthesis from vitamin B12, dimethylbenzimidazole arm of vitamin B12 plays no role in substrate positioning, corrinoid adenosylation assay: anaerobic, pH 6, 25°C, 1 or 2 mM FMN, 10 or 20 mM NADH, NAD(P)H: flavin oxidoreductase, 2 h incubation for complete reduction of hydroxycobalamin to cob(II)alamin before initiation of adenosyltransfer
690964
Lactobacillus reuteri
tripolyphosphate + adenosylcobalamin + H2O
measuring difference in absorbance by adenosylcobalamin at 525 nm
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
adenosylation of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) at similar rates
Lactobacillus reuteri
Application (protein specific)
Application
Commentary
Organism
medicine
ACA-mediated catalysis provides insights in molecular basis for dysfunction in methylmalonic aciduria
Lactobacillus reuteri
Crystallization (Commentary) (protein specific)
Crystallization
Organism
trimer of three independent five-helix bundles, active sites at the interface between adjacent monomers, no significant structural changes accompany catalysis, precatalytic complex with ATP: cob(II)alamin (PDB: 3CI1, four-coordinate, base-off cob(II)alamin intermediate, enzyme with fully ordered six C-terminal residues and potassium ion in active site), complex with tripolyphosphate: adenosylcobalamin (PDB: 3CI3, partially occupied with five-coordinate adenosylcobalamin), precatalytic complex with ATP: cob(II)inamide (PDB: 3CI4, cob(II)inamide-binding structurally indistinguishable from cob(II)alamin-binding), binding of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) in identical positions and orientation, space group R3, one molecule in asymmetric unit, unit cell parameters: a: 67.8-68, b: 67.8-68, c: 110.9-111.3, beta: 90°, molecular replacement using PDB: 2NT8 as model; vapour-diffusion with tag-cleaved protein solution (18-22 mg/ml, in presence of hydroxycobalamin and/or adenosylcobalamin or dicyanocobinamide, ATP etc.) and reservoir solution (10-13% (w/v) PEG 8000, pH 6), cubic crystals, crystallisation under anoxic conditions in presence of flavin-dependent reducing system
Lactobacillus reuteri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
cobinamide
substrate inhibition
Lactobacillus reuteri
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0005
-
in presence of 1 mM ATP, 20 mM NADH, 2 mM FMN, 0.5 mM hydroxycobalamin and NAD(P)H: flavin oxidoreductase, 1.5 mM MgCl2, 100 mM KCl, pH 6
Lactobacillus reuteri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + hydroxycobalamin
coenzyme B12 synthesis from vitamin B12, dimethylbenzimidazole arm of vitamin B12 plays no role in substrate positioning, corrinoid adenosylation assay: anaerobic, pH 6, 25°C, 1 or 2 mM FMN, 10 or 20 mM NADH, NAD(P)H: flavin oxidoreductase, 2 h incubation for complete reduction of hydroxycobalamin to cob(II)alamin before initiation of adenosyltransfer
690964
Lactobacillus reuteri
tripolyphosphate + adenosylcobalamin + H2O
measuring difference in absorbance by adenosylcobalamin at 525 nm
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
adenosylation of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) at similar rates
Lactobacillus reuteri
Other publictions for EC 2.5.1.17
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738459
Pallares
Spectroscopic Studies of the E ...
Salmonella enterica
J. Am. Chem. Soc.
138
3694-3704
2016
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737450
Park
Unprecedented mechanism employ ...
Salmonella enterica
Angew. Chem. Int. Ed. Engl.
54
7158-7161
2015
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737702
Pallares
Spectroscopic studies of the S ...
Salmonella enterica
Biochemistry
53
7969-7982
2014
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6
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5
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2
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2
2
738536
Moore
The EutT enzyme of Salmonella ...
Salmonella enterica, Salmonella enterica JE6583
J. Bacteriol.
196
903-910
2014
1
-
1
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4
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1
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1
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721682
Moore
Structural insights into the m ...
Salmonella enterica
Biochemistry
51
9647-9657
2012
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1
12
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18
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14
1
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3
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18
18
722386
Park
Spectroscopic characterization ...
Lactobacillus reuteri
Inorg. Chem.
51
4482-4494
2012
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721492
Park
Crystal structure of PduO-Type ...
Bacillus cereus
Biochem. Biophys. Res. Commun.
408
417-421
2011
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704686
Mera
Dihydroflavin-driven adenosyla ...
Homo sapiens, Lactobacillus reuteri
J. Biol. Chem.
285
2911-2917
2010
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2
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8
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701946
Medina
Mutation in the cobO gene gene ...
Sinorhizobium fredii
Arch. Microbiol.
191
11-21
2009
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1
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702286
Mera
Residue Phe112 of the human-ty ...
Lactobacillus reuteri
Biochemistry
48
3138-3145
2009
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1
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7
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29
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2
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1
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2
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1
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1
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29
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2
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1
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29
1
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29
29
702311
Padovani
A rotary mechanism for coenzym ...
Methylorubrum extorquens
Biochemistry
48
5350-5357
2009
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1
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705758
Zhang
Ligand-binding by catalyticall ...
Homo sapiens
Mol. Genet. Metab.
98
278-284
2009
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690265
Park
Crystallization and preliminar ...
Bacillus cereus
Acta Crystallogr. Sect. F
64
648-650
2008
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1
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690933
Fan
Functional characterization an ...
Homo sapiens
Biochemistry
47
2806-2813
2008
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1
1
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32
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32
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690964
St Maurice
Structural characterization of ...
Lactobacillus reuteri
Biochemistry
47
5755-5766
2008
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695036
Moon
Crystal structure of a PduO-ty ...
Burkholderia thailandensis
Proteins
72
1066-1070
2008
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1
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702245
Park
Kinetic and spectroscopic stud ...
Lactobacillus reuteri
Biochemistry
47
9007-9015
2008
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674853
St.Maurice
Structural characterization of ...
Lactobacillus reuteri, Lactobacillus reuteri CRL1098
J. Biol. Chem.
282
2596-2605
2007
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675180
Erger
In vivo expression of human AT ...
Homo sapiens
J. Gene Med.
9
462-469
2007
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682763
Tanaka
Molecular properties of two pr ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
Proteins
68
446-457
2007
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1
1
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3
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1
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7
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1
6
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1
1
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2
1
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1
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8
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6
2
1
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1
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690887
Mera
Structural and functional anal ...
Lactobacillus reuteri
Biochemistry
46
13829-13836
2007
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1
1
7
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2
7
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5
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1
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7
1
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29
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The adenosyltransferases ...
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