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Ligand adenosylcobalamin

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for adenosylcobalamin

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (14 results)

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Show Natural Product (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.154

2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein

0

-

2.5.1.154

2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]

0

-

2.5.1.17

2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcob(I)alamine

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcob(III)alamin

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcobalamin

0, 652541

-

2.5.1.17

cob(I)alamin + ADP = adenosylcobalamin + diphosphate

0

-

2.5.1.17

cob(I)alamin + ATP + H2O + H+ = adenosylcobalamin + diphosphate + phosphate

0

-

2.5.1.17

cob(I)alamin + ATP = adenosylcobalamin + triphosphate

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + coenzyme B12

0

-

2.5.1.17

cob(I)alamin + dATP + H2O + H+ = deoxyadenosylcobalamin + diphosphate + phosphate

0

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole = adenosylcobalamin + GMP

644450

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole = GMP + adenosylcobalamin

0

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole-5'-phosphate + H2O = GMP + adenosylcobalamin + phosphate + H+

0

-

2.5.1.154

2 entries

2.5.1.17

9 entries

2.7.8.26

3 entries

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.17.4.2

CTP + adenosylcobalamin = ?

714186

-

1.17.4.2

dATP + adenosylcobalamin = ?

714185

-

1.17.4.2

2 entries

2.5.1.151

5'-deoxyadenosylcobalamin + [alkylcobalamin reductase] + glutathione = cob(I)alamin-[alkylcobalamin reductase] + S-5'-deoxyadenosylglutathione

751575, 751024

-

2.7.1.156

ATP + 5'-deoxyadenosylcobinamide = 5'-deoxyadenosylcobinamide phosphate + ADP

644435, 644278, 644438

-

Product in Enzyme-catalyzed Reactions (29 results)

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Show Product (29 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.154

2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein

0

-

2.5.1.154

2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 diphosphate + 2 phosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]

0

-

2.5.1.17

2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcob(I)alamine

0

-

2.5.1.17

ATP + cob(I)alamine = triphosphate + adenosylcob(I)alamine

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcob(III)alamin

0

-

2.5.1.17

ATP + cobalamin = triphosphate + adenosylcob(III)alamin

0

-

2.5.1.17

ATP + cob(I)alamin + H2O = adenosylcobalamin + diphosphate + phosphate

0

-

2.5.1.17

ATP + cob(I)alamin + H2O = phosphate + diphosphate + adenosylcobalamin

0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + adenosylcobalamin

0, 652541

-

2.5.1.17

ATP + cobalamin = triphosphate + adenosylcobalamin

0

-

2.5.1.17

ATP + hydroxycobalamin = adenosylcobalamin + phosphate + diphosphate

0

-

2.5.1.17

ATP + hydroxycobalamin = tripolyphosphate + adenosylcobalamin + H2O

0

-

2.5.1.17

cob(I)alamin + ADP = adenosylcobalamin + diphosphate

0

-

2.5.1.17

cob(I)alamin + ATP + H2O + H+ = adenosylcobalamin + diphosphate + phosphate

0

-

2.5.1.17

cob(I)alamin + ATP = adenosylcobalamin + ?

0

-

2.5.1.17

cob(I)alamin + ATP = adenosylcobalamin + triphosphate

0

-

2.5.1.17

cob(II)alamin + ATP = adenosylcobalamin + ?

0

-

2.5.1.17

cyanocob(I)alamin + ATP = tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide

636864, 0

-

2.5.1.17

ATP + cob(I)alamin = triphosphate + coenzyme B12

0, 636871, 636865, 636866, 636872, 636873, 636874, 636868, 636867, 636864

-

2.5.1.17

ATP + cob(I)alamin = tripolyphosphate + coenzyme B12

0

-

2.5.1.17

cob(I)alamin + dATP + H2O + H+ = deoxyadenosylcobalamin + diphosphate + phosphate

0

-

2.5.1.17

dATP + cob(I)alamin = tripolyphosphate + deoxyadenosylcobalamin

0, 652541

-

2.5.1.17

dATP + cobalamin = triphosphate + deoxyadenosylcobalamin

0

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole = adenosylcobalamin + GMP

644450

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole = GMP + adenosylcobalamin

0

-

2.7.8.26

adenosylcobinamide-GDP + alpha-ribazole-5'-phosphate + H2O = GMP + adenosylcobalamin + phosphate + H+

0

-

2.7.8.26

alpha-ribazole + adenosylcobinamide-GDP = GMP + adenosylcobalamin

0

-

2.5.1.154

2 entries

2.5.1.17

22 entries

2.7.8.26

4 entries

3.1.3.73

adenosylcobalamin 5'-phosphate + H2O = adenosylcobalamin + phosphate

644450

-

Enzyme Cofactor/Cosubstrate (92 results)

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Show Cofactor (92 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.4.1

class II enzymes

715085

-

1.17.4.1

absolutely requires adenosylcobalamin (as a radical generator) for activity, KM: 0.001 mM

723666

-

1.17.4.2

class II enzymes

715085

-

1.17.4.2

-

714185, 714186

-

1.17.4.2

in the course of catalysis, the protein active site presents the reacting molecules with an environment that includes a hydrogen bond to the thiyl radical and intervening residues or solvent mediating an exchange coupling between the thiyl radical and cob(II)alamin

728091

-

1.17.4.2

-

437897, 437898, 437899, 437895, 437888, 437890

-

1.17.4.2

adenosylcobalamin

437897, 437892, 437899, 437889, 437893, 437894, 437896, 437900, 437901, 437902, 437903

-

1.17.4.2

required

681889

-

1.17.4.1

2 entries

1.17.4.2

6 entries

1.3.1.25

required as methyl acceptor for the methyl transfer activity of recombinant enzyme from E. coli

644712

-

2.1.1.106

5'-deoxyadenosylcob(III)alamin may substitute for methylcob(III)alamin, albeit only in the presence of light

757761

-

4.2.1.28

-

672098, 672269, 677025, 673603, 675575, 675716

-

4.2.1.28

i.e. coenzyme B12 or AdoCbl, dependent on

714211

-

4.2.1.28

i.e. coenzyme B12, dependent on

715388

-

4.2.1.28

Km value 0.15 mM for wild-type

746754

-

4.2.1.28

KM: 0.0008 mM

661707

-

4.2.1.28

adenosylcobalamin

651798, 652403, 651140

-

4.2.1.28

adenosylcobalamin, dependent on, two mol of 5'-deoxyadenosine per mol of enzyme are formed as an inactivation product from the coenzyme adenosyl group in presence of inhibitors, overview

698651

-

4.2.1.28

adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the cofactor, ATP and Mg2+

650799

-

4.2.1.28

adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+

649870

-

4.2.1.28

adenosylcobalamin. Glycerol-inactivated enzyme undergoes reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+

649505

-

4.2.1.28

adenosylcobalamin. Radical initiator

649991

-

4.2.1.28

adenosylcobalamin. There is a strict specificity of the enzyme for the coenzyme adenosyl group

653948

-

4.2.1.28

dependent on

729706

-

4.2.1.28

dependent on, Km value of 0.0015 mM

729472

-

4.2.1.30

required

666916

-

4.2.1.30

-

673603

-

4.2.1.30

dependent

652178

-

4.2.1.30

required

33834

-

4.2.1.30

-

675901, 650799, 651436, 652696, 672728, 675575, 666104

-

4.2.1.30

damaged coenzyme B12 is removed by glycerol dehydratase reactivase from glycerol dehydrogenase that has suffered mechanism-based inactivation

653907

-

4.2.1.30

dependent on

746602, 747304

-

4.3.1.7

-

680355, 680364, 682751, 661707, 704362, 729253, 704316

-

4.3.1.7

dependent on

34384, 661191, 34374, 34381

-

4.3.1.7

Km 0.0005 mM

34384

-

4.3.1.7

marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme-Co-C bond. A major structural change upon substrate binding is not observed with this particular enzyme. Glu287, one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond

715530

-

4.3.1.7

pulsed-laser photolysis of substrate-triggered cleavage of the cobalt-carbon bond and formation of the cob(II)alamin-5'-deoxyadenosyl radical pair in the adenosylcobalamin-dependent ethanolamine ammonia-lyase. Visible absorption spectra of holo-ethanolamine ammonia-lyase and ternary complex are comparable, indicating that the binding of substrate does not labilize the cofactor cobalt-carbon bond by significantly distorting the equilibrium structure. Following the substrate trigger, the protein interacts with the cofactor to contiguously guide the cleavage of the Co-C bond, at every step along the cleavage coordinate, starting from the equilibrium configuration of the ternary complex. The cleavage is represented by a diagonal trajectory across a free energy surface, that is defined by chemical, Co-C separation, and protein configuration coordinates

715302

-

4.3.1.7

the holoenzyme of adenosylcobalamin-dependent ethanolamine ammonia lyase undergoes suicidal inactivation during catalysis as well as inactivation in the absence of substrate. The inactivation involves the irreversible cleavage of the Co-C bond of the coenzyme. Inactivated holoenzyme undergoes rapid and continuous reactivation in the presence of ATP, Mg2+ and free adensosylcobalamin. EutA is essential for reactivation. Reactivation and activation occur through the exchange of modified coenzyme for free intact adenosylcobalamin

662021

-

4.3.1.7

vitamine B12 coenzyme

692739

-

4.3.1.7

adenosylcobalamin

690960, 691009, 691337, 692764

-

4.3.1.7

adenosylcobalamin, 70% of the enzyme-bound adenosylcobalamin is cleaved to cob(2)-alamin in the steady state of the reaction

690905

-

4.3.1.7

dependent on

747124, 747568

-

5.4.3.3

-

702340, 746577, 747510, 747193

-

5.4.3.3

dependent on

727339, 727664, 727695

-

5.4.3.3

shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments

727644

-

5.4.3.3

shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal 5'-phosphate

727644

-

5.4.3.3

shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal-5'-phosphate

727644

-

5.4.3.3

-

705339, 714347, 650175

-

5.4.3.3

Km value 6.1 mM, in presence of S-subunit of D-ornithine aminomutase, Km value 3.5 mM, in presence of ATP and S-subunit of D-ornithine aminomutase, Km value 1.9 mM

679913

-

5.4.3.3

-

651982

-

5.4.3.3

tightly bound

3396

-

5.4.3.5

-

747193, 747565, 748182

-

5.4.3.5

Km value 0.00043

652199

-

5.4.3.5

shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments

727644

-

5.4.3.5

-

704658

-

5.4.3.5

binding analysis with recombinant wild-type and mutant enzymes, overview

727036

-

5.4.3.5

dependent on

693191, 727677, 747073

-

5.4.3.5

paramagnetic Co2+ metal center of the cob(II)alamin cofactor

727131

-

5.4.99.1

dependent on

728191

-

5.4.99.1

i.e. coenzyme B12, required for activity

714983

-

5.4.99.1

-

716116, 716014

-

5.4.99.1

dependent on

702376, 692318

-

5.4.99.1

dependent on, binding structure, modeling, overview

727661

-

5.4.99.1

enzyme is dependent on, KM for wild-type enzyme is 0.0055 mM

650824

-

5.4.99.1

investigation of photolysis by transient absorption spectroscopy. Metal-to-ligand charge transfer intermediate decays to form cob(II)alamin with a time constand of 105 ps

662705

-

5.4.99.1

kinetics of homolysis and recombination, ultrafast spectroscopic experiments, no significant activation of coenzyme in absence of substrate

661930

-

5.4.99.1

Km-value for wild-type enzyme is 0.005 mM. No cob(II)alamin detected in UV-visible spectrum of mutant enzymes R100M and R100Y. In mutant enzyme R100K cob(II)alamin accumulates to a concentration similar to that of the wild-type enzyme, homolysis of the coenzyme is slower by an order of magnitude, compared to wild-type enzyme. Mutant does not exhibit the very large deuterium isotope effects that are observed for homolysis of the coenzyme when the wild-type enzyme is reacted with deuterated substrates

650247

-

5.4.99.1

study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals

661176

-

5.4.99.1

study of tritium isotope effects on homolysis of adenosylcobalamin

661116

-

5.4.99.1

-

650929, 650853

-

5.4.99.1

adenosylcobalamin, the concentration of internal coenzyme B12 is crucial for the full activity of B12-dependent enzyme

748550

-

5.4.99.1

binds to subunit SanU with about 0.1 mol Co per mol SanU

662763

-

5.4.99.1

each of the two independent coenzyme B12 molecules is associated with a substrate-binding site

653936

-

5.4.99.1

the alpha2beta2 tetramer consists of two subunits, subunit MutS of 53600 Da and subunit GlmS of 14800 Da, whose assembly is mediated by coenzyme B12. In GlnS and MutS the sequence motif, Asp-Xaa-His-Xaa-Xaa-Gly, which includes the cobalt-coordinating histidine residue, and a predicted alpha-helical region following the motif, are present as an unstructured and highly mobile loop. In the absence of coenzyme, the B12-binding site apparently is only partially formed. Important elements of the binding site only become structured upon binding B12, these include the cobalt-coordinating histidine residue, and an alpha helix that forms one side of the cleft accomodating the nucleotide tail of the coenzyme

651053

-

5.4.99.1

the coenzyme B12-binding subunit traps the nucleotide moiety of coenzyme B12

652857

-

5.4.99.13

AdoCbl, required, affinity for AdoCbl is unaffected by the presence of GDP

748223

-

5.4.99.13

AdoCbl, required, the active sites in the CmIcmF dimer exhibit identical affinity for AdoCbl. Addition of isovaleryl-CoA to wild-type holo-IcmF results in formation of the intermediate cob(II)alamin. AdoCbl is quantitatively converted to cob(II)alamin when isovaleryl-CoA is added to F598A or to the F598I/L or Q742A mutants inactivating the enzyme. Cob(II)alamin formation in activates the enzyme

748193

-

5.4.99.13

AdoCbl, required, two conformations: C3'-endo and C2'-endo, conformational change of the 5'-deoxyadenosyl group from C2'-endo to C3'-endo contributes to initiation of catalysis. Adenosylcobalamin (coenzyme B12) is an organometallic enzyme cofactor for radical chemistry. Its reactivity is based on a unique covalent cobalt-carbon (Co-C) bond that is sufficiently weak to allow for reversible homolytic cleavage in enzyme active sites, generating a 5'-deoxyadenosyl radical in the presence of an appropriate substrate. The radical can then abstract a substrate hydrogen atom and initiate difficult chemical transformations

748200

-

5.4.99.2

P-loop GTPase MeaB increases affinity of the mutase for cofactor twofold, in presence of MeaB and GDP, affinity decreases fivifold

678210

-

5.4.99.2

the 5'-deoxyadenosyl vitamin B12 orAdoCbl, methylmalonyl-CoA mutase (MCM) requires 5'-deoxyadenosylcobalamin as a cofactor

747314

-

5.4.99.2

the apoenzyme is converted to a holoenzyme by incubation for 4 h at 4°C with 0.01 mM 5'-deoxyadenosylcobalamin, the purified enzyme contains one mole of prosthetic 5'-deoxyadenosylcobalamin per mole of subunit

701956

-

5.4.99.2

-

649513, 705936, 716097, 704291, 3514, 649878, 649904, 649999, 650005, 652093, 652252, 652521, 662325, 704957, 690428, 715560

-

5.4.99.2

active form of vitamin B12

746727

-

5.4.99.2

AdoCbl, dependent on

747783

-

5.4.99.2

AdoCbl, the enzyme converts methylmalonyl-CoA to succinyl-CoA employing highly reactive radicals from its cofactor adenosylcobalamin to perform its reaction. Formation and accumulation of OH2Cbl, the oxidized form of the AdoCbl cofactor formed during catalysis, is the cause of hMCM inactivation. GTPase hMMAA is able to remove the damaged cofactor through GTP hydrolysis

747209

-

5.4.99.2

binding analysis with recombinant wild-type and mutant enzymes, overview

727036

-

5.4.99.2

dependent on

694024, 727246, 692859, 726874

-

5.4.99.2

dependent on adenosylcobalamin as prosthetic group, under cobalamin-deficient conditions, (R)-2-methylmalonyl-CoA and its precursor, propionyl-CoA, increase as a result of a decrease in the catalytic activity of MCM due to deficiency of adenosylcobalamin

691535

-

5.4.99.2

dependent on adenosylcobalamin which is delivered by adenosyltransferase

694308

-

5.4.99.2

MCM activity with adenosylcobalamin increases linearly during the first 3-4 min

714049

-

5.4.99.2

the apparent Km value of the apoenzyme is 22.7 nM

701956

-

4.2.1.28

14 entries

4.2.1.30

7 entries

4.3.1.7

10 entries

5.4.3.3

9 entries

5.4.3.5

7 entries

5.4.99.1

17 entries

5.4.99.13

3 entries

5.4.99.2

13 entries

5.4.99.4

-

651581

-

5.4.99.63

dependent on

734100

-

Activator in Enzyme-catalyzed Reactions (10 results)

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Show Activating Compound (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.4.2

-

437889

-

1.17.4.2

-

437891, 437898, 437887, 437902, 437903

-

1.17.4.2

2 entries

2.5.1.17

i.e. adenosylcob(III)alamin, is required for stimulation of eut operon expression

659048

-

4.2.1.30

-

702830

-

4.2.1.30

bound at the interface between the alpha and beta subunits

651133

-

4.2.1.30

activates

33818

-

4.2.1.30

-

706914

-

4.2.1.30

GDHt utilizes adenosylcobalamin, i.e. AdoCbl or CoB12, as a cofactor, Km is 10.03 nM

713813

-

4.2.1.30

is critical to the reactivation of glycerol dehydratase

705190

-

4.2.1.30

6 entries

5.4.99.2

required

677443

-

Inhibitor in Enzyme-catalyzed Reactions (8 results)

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Show Inhibitors (8 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.4.2

-

437892

-

4.2.1.28

analogue where e-propionamide group is converted to carboxylic acid inactivates complex, forms hydroxycobalamine derivative, leaves apoenzyme intact, which indicates that inactivation occurs from one of the intermediates of the normal reaction, mechanism of inactivation

5621

-

4.2.1.28

analogues

5633, 5634

-

4.2.1.28

electron paramagnetic resonance data indicate mechanism based mode of coenzyme analogue inactivation, extinction of radical intermediates

5632

-

4.2.1.28

Ki: 0.8 mM

5623

-

4.2.1.28

with e-propionamide group converted to carboxylic acid, inactivation during catalytic process, analogues inhibit if added prior to coenzyme

5611

-

4.2.1.28

inactivation in absence of substrate

5627

-

4.2.1.28

6 entries

7.6.2.8

is less effective causing about 25% inhibition of cobalmin uptake

750412

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (2 results)

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Show Turnover Number (2 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.151

0.174

-

pH 8.0, 20°C

751024

2.7.1.156

0.251

-

pH 8.8, 37°C

644435

K_M Value (16 results)

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Show KM Value (16 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.17.4.2

0.0003

-

presence of 1.0 mM CTP and 1 mM dATP

437892

1.17.4.2

0.00045

-

presence of 0.1 mM CTP and 1 mM dATP

437892

1.17.4.2

0.0055

-

presence of 2 mM CTP without activator

437892

1.17.4.2

0.06

-

-

437900

1.17.4.2

4 entries

2.7.1.156

0.066

-

pH 8.8, 37°C

644435

4.2.1.28

0.0008

-

-

651798

4.2.1.28

0.008

-

-

651140

4.2.1.30

8

-

37°C, recombinant enzyme, purification method 1 and 2

651133

4.2.1.30

20

-

37°C

651133

4.3.1.7

-999

-

truncated enzymes, value between 0.000041 and 0.000078

704362

4.3.1.7

0.000055

-

wild-type enzyme

704362

5.4.99.2

0.00024

-

37°C, wild-type

652252

5.4.99.2

0.00045

-

37°C, mutant H610A

652252

5.4.99.2

0.00052

-

37°C, mutant H610N

652252

5.4.99.2

0.00064

-

37°C, pH 7, in presence of 3 mM NH4+

649513

5.4.99.2

0.0086

-

37°C, pH 7, without NH4+

649513

4.2.1.28

2 entries

4.2.1.30

2 entries

4.3.1.7

2 entries

5.4.99.2

5 entries

References & Links

Literature References (187)

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Show Reference (187 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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L-beta-Lysine mutase (Clostridium sticklandii)

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1998

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Structure

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Dehydrations requiring vitamin B12 coenzyme

1971

Abeles, R.H.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

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Inactivation of dioldehydrase in the presence of a coenzyme-B12 analog

1980

Toraya, T.; Abeles, R.H.

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5623

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Diol dehydrase

1982

Toraya, T.; Fukui, S.

B12 (Dolphin, D. ed. ) Wiley, New York

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5627

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Purification and properties of propanediol dehydratase from Propionibacterium freudenreichii

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5633

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Biodegradation

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5634

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Adenosylcobinamide methyl phosphate as a pseudocoenzyme for diol dehydrase

1993

Ishida, A.; Toraya, T.

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1962

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33834

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Cloning, sequencing, and high level expression of the genes encoding adenosylcobalamin-dependent glycerol dehydrase of Klebsiella pneumoniae

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1985

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1966

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Ribonucleotide reductase from Thermus X-1, a thermophilic organism

1973

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Biochemistry

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437890

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Substrate and effector binding to ribonucleoside triphosphate reductase of Lactobacillus leichmannii

1974

Chen, A.K.; Bhan, A.; Hopper, S.; Abrams, R.; Franzen, J.S.

Biochemistry

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437891

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Ribonucleotide reductase from Euglena gracilis. A 5-deoxyadenoslycobalamin-dependent enzyme

1974

Hamilton, F.D.

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249

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Ribonucleoside triphosphate reductase from Lactobacillus leichmannii

1978

Blakley, R.L.

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Adenosylcobalamin-dependent ribonucleotide reductase from the blue-green alga, Anabaena sp. Purification and partial characterization

1980

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261

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437896

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1994

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B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli

1997

Jordan, A.; Torrents, E.; Jeanthon, C.; Eliasson, R.; Hellman, U.; Wernstedt, C.; Barbe, J.; Gibert, I.; Reichard, P.

Proc. Natl. Acad. Sci. USA

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The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum

1997

Tauer, A.; Benner, S.A.

Proc. Natl. Acad. Sci. USA

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53-58

437899

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Ribonucleotide reduction in Pseudomonas species: simultaneous presence of active enzymes from different classes

1999

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1999

Licht, S.S.; Booker, S.; Stubbe, J.

Biochemistry

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437901

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Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: The importance of entropy in catalysis

1999

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Biochemistry

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1234-1242

437902

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Ribonucleoside triphosphate reductase from Lactobacillus leichmannii: Kinetic evaluation of a series of adenosylcobalamin competitive inhibitors, [omega-(adenosin-5'-O-yl)alkyl]cobalamins, which mimic the post Co-C homolysis intermediate

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437903

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Adenosylcobalamin-dependent ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Rapid, improved purification involving dGTP-based affinity chromatography plus biophysical characterization studies demonstrating enhanced, crystallographic level purity

1999

Suto, R.K.; Whalen, M.A.; Finke, R.G.

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636864

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Enzymatic conversion of vitamin B-12s to a cobamide coenzyme, alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide (adenosyl-B-12)

1966

Vitols, E.; Walker, G.A.; Huennekens, F.M.

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241

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The adenosyltransferases

1973

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636866

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Ribosome-associated vitamin B12s adenosylating enzyme of Lactobacillus leichmannii

1980

Beck, W.S.

Methods Enzymol.

67

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636867

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Studies of enzyme stereochemistry. Elucidation of the stereochemistry of the reaction catalyzed by cob(I)alamin adenosyltransferase

1985

Parry, R.J.; Ostrander, J.M.; Arzu, I.Y.

J. Am. Chem. Soc.

107

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636868

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Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans

1991

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J. Bacteriol.

173

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636871

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Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium

1995

Suh, S.J.; Escalante-Semerena, J.C.

J. Bacteriol.

177

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636872

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An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin

2001

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276

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636873

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Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene

2001

Johnson, C.L.; Pechonick, E.; Park, S.D.; Havemann, G.D.; Leal, N.A.; Bobik, T.A.

J. Bacteriol.

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636874

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The ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica requires the 2'-OH group of ATP for function and yields inorganic triphosphate as its reaction byproduct

2002

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644278

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The biosynthesis of adenosylcobalamin (vitamin B12)

2002

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Nat. Prod. Rep.

19

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644435

7559521

Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate

1995

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270

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644438

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Analysis of the adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU) enzyme of Salmonella typhimurium LT2. Identification of residue His-46 as the site of guanylylation

2000

Thomas, M.G.; Thompson, T.B.; Rayment, I.; Escalante-Semerena, J.C.

J. Biol. Chem.

275

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644450

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In vitro synthesis of the nucleotide loop of cobalamin by Salmonella typhimurium enzymes

1999

Maggio-Hall, L.A.; Escalante-Semerena, J.C.

Proc. Natl. Acad. Sci. USA

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644712

10217792

Adenosylcobalamin-mediated methyl transfer by toluate cis-dihydrodiol dehydrogenase of the TOL plasmid pWW0

1999

Lee, J.Y.; Park, H.S.; Kim, H.S.

J. Bacteriol.

181

2953-2957

649505

10985746

Specificities of reactivating factors for adenosylcobalamin-dependent diol dehydratase and glycerol dehydratase

2000

Tobimatsu, T.; Kajiura, H.; Toraya, T.

Arch. Microbiol.

174

81-88

649513

12844209

Purification and characterization of homodimeric methylmalonyl-CoA mutase from Sinorhizobium meliloti

2003

Miyamoto, E.; Watanabe, F.; Charles, T.C.; Yamaji, R.; Inui, H.; Nakano, Y.

Arch. Microbiol.

180

151-154

649870

10529189

Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor

1999

Mori, K.; Toraya, T.

Biochemistry

38

13170-13178

649878

10563814

Role of the dimethylbenzimidazole tail in the reaction catalyzed by coenzyme B12-dependent methylmalonyl-CoA mutase

1999

Chowdhury, S.; Banerjee, R.

Biochemistry

38

15287-15294

649904

10387043

Crystal structure of substrate complexes of methylmalonyl-CoA mutase

1999

Mancia, F.; Smith, G.A.; Evans, P.R.

Biochemistry

38

7999-8005

649991

10821701

Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase

2000

Abend, A.; Bandarian, V.; Reed, G.H.; Frey, P.A.

Biochemistry

39

6250-6257

649999

10891081

Thermodynamic and kinetic characterization of Co-C bond homolysis catalyzed by coenzyme B(12)-dependent methylmalonyl-CoA mutase

2000

Chowdhury, S.; Banerjee, R.

Biochemistry

39

7998-8006

650005

10924114

Protection of radical intermediates at the active site of adenosylcobalamin-dependent methylmalonyl-CoA mutase

2000

Thoma, N.H.; Evans, P.R.; Leadlay, P.F.

Biochemistry

39

9213-9221

650175

12093296

Identification of a novel pyridoxal 5'-phosphate binding site in adenosylcobalamin-dependent lysine 5,6-aminomutase from Porphyromonas gingivalis

2002

Tang, K.H.; Harms, A.; Frey, P.A.

Biochemistry

41

8767-8776

650247

15023074

Role of arg100 in the active site of adenosylcobalamin-dependent glutamate mutase

2004

Xia, L.; Ballou, D.P.; Marsh, E.N.

Biochemistry

43

3238-3245

650799

10949584

Radical catalysis of B12 enzymes: structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases

2000

Toraya, T.

Cell. Mol. Life Sci.

57

106-127

650824

11755393

The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase

2001

Madhavapeddi, P.; Marsh, E.N.

Chem. Biol.

8

1143-1149

650853

11828501

A protein pre-organized to trap the nucleotide moiety of coenzyme B12: refined solution structure of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum

2001

Hoffmann, B.; Tollinger, M.; Konrat, R.; Huhta, M.; Marsh, E.N.G.; Krautler, B.

ChemBioChem

2

643-655

650929

12413543

Coenzyme B(12) dependent glutamate mutase

2002

Gruber, K.; Kratky, C.

Curr. Opin. Chem. Biol.

6

598-603

651053

10429202

Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium

1999

Hoffmann, B.; Konrat, R.; Bothe, H.; Buckel, W.; Krautler, B.

Eur. J. Biochem.

263

178-188

651133

12230560

The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol

2002

Yamanishi, M.; Yunoki, M.; Tobimatsu, T.; Sato, H.; Matsui, J.; Dokiya, A.; Iuchi, Y.; Oe, K.; Suto, K.; Shibata, N.; Morimoto, Y.; Yasuoka, N.; Toraya, T.

Eur. J. Biochem.

269

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651140

12423373

Purification, characterization and subunits identification of the diol dehydratase of Lactobacillus collinoides

2002

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Eur. J. Biochem.

269

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651436

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(Hydroxyalkyl)cob(III)alamins as competitive inhibitors in coenzyme B12-dependent enzymic reactions. 1H-NMR structure analysis and kinetic studies with glycerol dehydratase and diol dehydratase

1999

Poppe, L.; Hull, W.E.; Nitsche, R.; Graf, T.; Stupperich, E.; Retey, J.

Helv. Chim. Acta

82

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651581

12440902

Rotation of the exo-methylene group of (R)-3-methylitaconate catalyzed by coenzyme B(12)-dependent 2-methyleneglutarate mutase from Eubacterium barkeri

2002

Pierik, A.J.; Ciceri, D.; Broker, G.; Edwards, C.H.; McFarlane, W.; Winter, J.; Buckel, W.; Golding, B.T.

J. Am. Chem. Soc.

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651798

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Functions of the D-ribosyl moiety and the lower axial ligand of the nucleotide loop of coenzyme B(12) in diol dehydratase and ethanolamine ammonia-lyase reactions

2002

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Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase from Clostridium sticklandii

2000

Chang, C.H.; Frey, P.A.

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275

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The coenzyme b12 analog 5'-deoxyadenosylcobinamide-gdp supports catalysis by methylmalonyl-coa mutase in the absence of trans-ligand coordination

2001

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Characterization and mechanism of action of a reactivating factor for adenosylcobalamin-dependent glycerol dehydratase

2001

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652199

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Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent D-ornithine aminomutase from Clostridium sticklandii

2001

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Importance of the histidine ligand to coenzyme B12 in the reaction catalyzed by methylmalonyl-CoA mutase

2002

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277

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Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase

2003

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278

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MeaB is a component of the methylmalonyl-CoA mutase complex required for protection of the enzyme from inactivation

2004

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279

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652541

15044458

The structural basis for methylmalonic aciduria. The crystal structure of archaeal ATP:cobalamin adenosyltransferase

2004

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J. Biol. Chem.

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Crystal structure of substrate free form of glycerol dehydratase

2003

Liao, D.I.; Dotson, G.; Turner, I.Jr.; Reiss, L.; Emptage, M.

J. Inorg. Biochem.

93

84-91

652857

11397096

The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)

2001

Tollinger, M.; Eichmuller, C.; Konrat, R.; Huhta, M.S.; Marsh, E.N.; Krautler, B.

J. Mol. Biol.

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653907

12517345

Structure of glycerol dehydratase reactivase: a new type of molecular chaperone

2003

Liao, D.I.; Reiss, L.; Turner, I.; Dotson, G.

Structure

11

109-119

653936

10467146

Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights

1999

Reitzer, R.; Gruber, K.; Jogl, G.; Wagner, U.G.; Bothe, H.; Buckel, W.; Kratky, C.

Structure

7

891-902

653948

10903944

How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex

2000

Masuda, J.; Shibata, N.; Morimoto, Y.; Toraya, T.; Yasuoka, N.

Structure Fold. Des.

8

775-788

659048

15317775

The eutT gene of Salmonella enterica encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme

2004

Buan, N.R.; Suh, S.J.; Escalante-Semerena, J.C.

J. Bacteriol.

186

5708-5714

661116

14979711

Pre-steady-state measurement of intrinsic secondary tritium isotope effects associated with the homolysis of adenosylcobalamin and the formation of 5'-deoxyadensosine in glutamate mutase

2004

Cheng, M.C.; Marsh, E.N.

Biochemistry

43

2155-2158

661176

16285720

Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase

2005

Brooks, A.J.; Fox, C.C.; Marsh, E.N.; Vlasie, M.; Banerjee, R.; Brunold, T.C.

Biochemistry

44

15167-15181

661191

15736929

Characterization of the product radical structure in the Co(II)-product radical pair state of coenzyme B12-dependent ethanolamine deaminase by using three-pulse 2H ESEEM spectroscopy

2005

Warncke, K.

Biochemistry

44

3184-3193

661707

16156797

Homoadenosylcobalamins as probes for exploring the active sites of coenzyme B12-dependent diol dehydratase and ethanolamine ammonia-lyase

2005

Fukuoka, M.; Nakanishi, Y.; Hannak, R.B.; Krautler, B.; Toraya, T.

FEBS J.

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Photolysis and recombination of adenosylcobalamin bound to glutamate mutase

2004

Sension, R.J.; Cole, A.G.; Harris, A.D.; Fox, C.C.; Woodbury, N.W.; Lin, S.; Marsh, E.N.G.

J. Am. Chem. Soc.

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Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase

2004

Mori, K.; Bando, R.; Hieda, N.; Toraya, T.

J. Bacteriol.

186

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Nitric oxide inhibits mammalian methylmalonyl-CoA mutase

2005

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J. Biol. Chem.

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Time-resolved measurements of the photolysis and recombination of adenosylcobalamin bound to glutamate mutase

2005

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J. Phys. Chem. B

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Improvement of nikkomycin production by enhanced copy of sanU and sanV in Streptomyces ansochromogenes and characterization of a novel glutamate mutase encoded by sanU and sanV

2005

Li, Y.; Ling, H.; Li, W.; Tan, H.

Metab. Eng.

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666104

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Insights into the genome of the enteric bacterium Escherichia blattae: Cobalamin (B12) biosynthesis, B12-dependent reactions, and inactivation of the gene region encoding B12-dependent glycerol dehydratase by a new Mu-Like prophage

2004

Andres, S.; Wiezer, A.; Bendfeldt, H.; Waschkowitz, T.; Toeche-Mittler, C.; Daniel, R.

J. Mol. Microbiol. Biotechnol.

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Determination of vitamin B12 using the enzyme glycerol dehydrase

2004

Yamada, S.; Yamada, K.; Nishikawa, N.; Hioki, R.; Nirasawa, M.; Kii, K.; Ryugo, H.; Iwama, M.; Fukuda, M.

Scand. J. Clin. Lab. Invest.

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Analysis of the Cob(II)alamin-5-deoxy-3,4-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase

2006

Mansoorabadi, S.O.; Magnusson, O.T.; Poyner, R.R.; Frey, P.A.; Reed, G.H.

Biochemistry

45

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Dioldehydrase: an essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin

2007

Schwartz, P.A.; Frey, P.A.

Biochemistry

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Heterologous expression and characterization of recombinant glycerol dehydratase from Klebsiella pneumoniae in Escherichia coli

2007

Wang, F.; Qu, H.; Tian, P.; Tan, T.

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Molecular basis for specificities of reactivating factors for adenosylcobalamin-dependent diol and glycerol dehydratases

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Kajiura, H.; Mori, K.; Shibata, N.; Toraya, T.

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751575

19447654

Processing of alkylcobalamins in mammalian cells A role for the MMACHC (cblC) gene product

2009

Hannibal, L.; Kim, J.; Brasch, N.E.; Wang, S.; Rosenblatt, D.S.; Banerjee, R.; Jacobsen, D.W.

Mol. Genet. Metab.

97

260-266

757761

26456915

The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction

2015

Benjdia, A.; Pierre, S.; Gherasim, C.; Guillot, A.; Carmona, M.; Amara, P.; Banerjee, R.; Berteau, O.

Nat. Commun.

6

8377

Links to other databases for adenosylcobalamin

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ChEBI

PubChem

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