2.5.1.17: corrinoid adenosyltransferase
This is an abbreviated version!
For detailed information about corrinoid adenosyltransferase, go to the full flat file.
Word Map on EC 2.5.1.17
-
2.5.1.17
-
adenosylcobalamin
-
cobialamin
-
enterica
-
adenosylation
-
atp:cobialamin
-
adocbl
-
atp:coirrinoid
-
corrinoids
-
four-coordinate
-
1,2-propanediol
-
reuteri
-
acats
-
supernucleophilic
-
cobinamide
-
b12-dependent
-
adenosylcobinamide
-
5\'-deoxyadenosyl
-
cyanocobalamin
-
medicine
- 2.5.1.17
- adenosylcobalamin
-
cobialamin
- enterica
-
adenosylation
-
atp:cobialamin
-
adocbl
-
atp:coirrinoid
- corrinoids
-
four-coordinate
- 1,2-propanediol
- reuteri
-
acats
-
supernucleophilic
- cobinamide
-
b12-dependent
- adenosylcobinamide
-
5\'-deoxyadenosyl
- cyanocobalamin
- medicine
Reaction
2 ATP
+
2 cob(II)alamin
+
Synonyms
ACAT, adenosyltransferase, vitamin B12s, aquacob(I)alamin adenosyltransferase, aquocob(I)alamin adenosyltransferase, ATP: cobalamin adenosyltransferase, ATP:co(I)rrinoid adenosyltransferase, ATP:cob(I)alamin adenosyltransferase, ATP:cob(I)alamin Cobeta-adenosyltransferase, ATP:cob(I)alamin transferase (ATR), ATP:Cob(I)alaminadenosyltransferase, ATP:cobalamin adenosyltransferase, ATP:cobalt(I) corrinoid adenosyltransferase, ATP:corrinoid adenosyltransferase, ATP:corrinoid adenosyltransferase PduO, ATR, cob(I)alamin adenosyltransferase, cob(I)yrinic acid a,c-diamide adenosyltransferase, CobA, CobA-type ATP:Co(I)rrinoid adenosyltransferase, cobalamin adenosyltransferase, CobAMm, cobO mutant SVQ336, cobO mutant SVQ524, cobO mutantSVQ336, EC 1.16.8.1, EutT, EutT adenosyltransferase, hATR, homologeous to PduO-type ATP: cob(I)alamin adenosyltransferase, human adenosyltransferase, human ATP: cob(I)alamin adenosyltransferase, human-type ACA, human-type ATP: co(I)rrinoid adenosyltransferase, human-type ATP: cob(I)alamin adenosyltransferase, LrPduO, methylmalonic aciduria type B, MMAB, MMAB protein, PduO, PduO adenosyltransferase, PduO enzyme, PduO protein, PduO-type ACA, PduO-type adenosine 5'-triphosphate:corrinoid adenosyltransferase, PduO-type ATP: cobalamin adenosyltransferase, PduO-type ATP:Co(I)rrinoid adenosyltransferase, PduO-type ATP:cob(I)alamin adenosyltransferase, PduO-type ATP:corrinoid adenosyltransferase, PduO-type corrinoid adenosyltransferase, ST1454, ST2180, TA1434, vitamin B12s adenosyltransferase
ECTree
2.5.1.17 corrinoid adenosyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.5.1.17 - corrinoid adenosyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
ATP + cob(I)alamin + H2O
?
anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate
ATP-dependent cob(I)alamin consumption to a yet unknown compound
-
?
ATP + cob(I)alamin + H2O
adenosylcobalamin + diphosphate + phosphate
-
37°C
monitoring adenosylcobalamin formation at 388 nm in continous spectrophotometric assay
-
?
ATP + cob(I)alamin + H2O
phosphate + diphosphate + adenosylcobalamin
anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate
measured by decrease in light absorbance by cob(I)alamin at 388 nm and increase of light absorbance by presumably adenosylcobalamin at 525 nm
-
?
ATP + cob(I)yrinic acid a,c-diamide
triphosphate + adenosylcob(III)yrinic acid a,c-diamide
-
-
-
?
ATP + cob(II)alamine
triphosphate + adenosylcob(II)alamine
-
-
-
?
ATP + cob(II)inamide
triphosphate + adenosylcob(II)inamide
-
-
-
?
ATP + cobalamin
triphosphate + adenosylcob(III)alamin
-
enzyme is absolutely specific for ATP or dATP as adenosyl donors, ATP is the preferred adenosyl donor
-
-
?
ATP + cobalamin
triphosphate + adenosylcobalamin
enzyme is absolutely specific for ATP or dATP as adenosyl donors
-
-
ir
ATP + hydroxycobalamin
adenosylcobalamin + phosphate + diphosphate
37°C, pH 8, 0.5 mM ATP, 0.05 mM hydroxycobalamin, in presence of 1 mM titanium(III)citrate
measured by decrease in absorbance at 388 nm
-
?
ATP + hydroxycobalamin
tripolyphosphate + adenosylcobalamin + H2O
-
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
measuring difference in absorbance by adenosylcobalamin at 525 nm
-
?
cob(I)alamin + ATP
adenosylcobalamin + ?
-
in the co+ assay the cobalt ion of cobalamin is chemically reduced in solution to cob(I)alamin by Ti(III)citrate, allowing the cob(I)alamin adenosylation reaction to be measured directly. The Co+ assay is performed under anoxic conditions
-
-
?
cob(I)alamin + CTP + H2O + H+
cytosylcobalamin + diphosphate + phosphate
-
-
-
-
?
cob(I)alamin + dATP + H2O + H+
deoxyadenosylcobalamin + diphosphate + phosphate
-
-
-
-
?
cob(I)alamin + GTP + H2O + H+
guanosylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)alamin + ITP
hypoxanthosylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)alamin + UTP
uranylcobalamin + diphosphate + phosphate
-
low activity
-
-
?
cob(I)inamide + ATP
5'-deoxy-5'-adenosyl-cob(I)inamide + polyphosphate
-
-
?
cob(I)yric acid + ATP
5'-deoxy-5'-adenosyl-cob(I)yric acid + polyphosphate
-
-
?
cob(I)yrinic acid a,c-diamide + ATP
5'-deoxy-5'-adenosyl-cob(I)yrinic acid a,c-diamide + polyphosphate
-
-
?
cob(II)alamin
cob(I)alamin
G97, T161, and H183 possible role in stabilizing four-coordinate, cob(II)alamin C-terminal His-tagged enzyme binds cob(II)alamin base-off while N-terminal His-tagged enzyme binds it base-on (impaired base-off transition), only mutants S68F, K78Q, K78R, R186W, and R190C also bind cob(II)alamin base-off
-
-
?
cob(II)alamin + ATP
adenosylcobalamin + ?
-
in the Co2+ assay the NADPH-dependent flavodoxin protein reductase/flavodoxin system is used to reduce Co2+ to Co+. In this Co2+ assay, the PduO enzyme must bind cob(II)alamin and facilitate the generation of cob(I)alamin in its active site
-
-
?
CTP + cob(I)alamin
triphosphate + cytosylcobalamin
-
polymorphic variants 239K and 239M, 9% activity compared to ATP with enzyme variant 239K, 6% activity compared to ATP with enzyme variant 239M
-
-
?
CTP + cob(I)alamin + H2O
cytidylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
dATP + cob(I)alamin
tripolyphosphate + deoxyadenosylcobalamin
-
-
?
dATP + cobalamin
triphosphate + deoxyadenosylcob(III)alamin
-
enzyme is absolutely specific for ATP or dATP as adenosyl donors, dATP results in 21% of the activity with ATP
-
-
?
dATP + cobalamin
triphosphate + deoxyadenosylcobalamin
enzyme is absolutely specific for ATP or dATP as adenosyl donors
-
-
ir
GTP + cob(I)alamin
triphosphate + guanosylcobalamin
-
polymorphic variants 239K and 239M, 16% activity compared to ATP with enzyme variant 239K, 14% activity compared to ATP with enzyme variant 239M
-
-
?
GTP + cob(I)alamin + H2O
guanosylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
ITP + cob(I)alamin + H2O
inosylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
UTP + cob(I)alamin
triphosphate + uridylcobalamin
-
polymorphic variants 239K and 239M, 8% activity compared to ATP with enzyme variant 239K, 6% activity compared to ATP with enzyme variant 239M
-
-
?
UTP + cob(I)alamin + H2O
uridylcobalamin + diphosphate + phosphate
-
37°C
-
-
?
2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
-
-
-
?
2 ATP + 2 cob(II)alamin + a reduced flavoprotein
2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein
Listeria monocytogenes LL195
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(I)alamine
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
-
adenosyltransferase enzymes lower the thermodynamic barrier of the Co2+ toCo+ reduction needed for the formation of the unique organometalic Co-C bond of adenosylcobalamin
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
reaction mechanism: assimilated cobalamin is reduced to co(II)alamin, that then binds to the enzyme-ATP complex, further reduction yields a nucleophilic four coordinated Co1+ intermediate that attacks the 5'-carbon of the cosubstrate ATP to generate adenosylcobalamin and triphosphate, spectroscopic analysis, enzyme-induced base-on/base-off conversion activating the cobalamin substrate for reduction
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
-
adenosyltransferase enzymes lower the thermodynamic barrier of the Co2+ to Co+ reduction needed for the formation of the unique organometalic Co-C bond of adenosylcobalamin
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
binding of the substrate ATP to ATR that is fully loaded with 5'-deoxyadenosylcobalamin leads to the ejection of 1 equivalent of the cofactor into solution. In the presence of methylmalonyl-CoA mutase and ATP, 5'-deoxyadenosylcobalamin is transferred from ATR to the acceptor protein in a process that exhibits an 3.5fold lower Kact for ATP compared to the one in which cofactor is released into solution. ATP favorably influences cofactor transfer in the forward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery of 1 equivalent of 5'-deoxyadenosylcobalamin, from 4 to 1. A rotary rotary mechanism for ATR function is proposed in which, at any given time, only two of its active sites are used for 5'-deoxyadenosylcobalamin synthesis and where binding of ATP to the vacant site leads to the transfer of the high value 5'-deoxyadenosylcobalamin product to the acceptor mutase
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
final step in the conversion of vitamin B12 to coenzyme B12, the latter being required for degradation of 1,2-propanediol
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
last step in the corrinoid adenosylation pathway, EutT and CobA
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
mechanism of adenosylcobalamin biosynthesis
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
CobA has an ATP-binding P-loop motif, while EutT has a cysteine-rich region reminiscent of a conserved S-adenosylmethionine Fe-S cluster motif
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
-
formation of the the essential C-Co bond by transferring the adenosyl group from a molecule of ATP to a transient Co1+ corrinoid species generated by the active site
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
last step in the corrinoid adenosylation pathway, EutT and CobA
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcob(III)alamin
CobA has an ATP-binding P-loop motif, while EutT has a cysteine-rich region reminiscent of a conserved S-adenosylmethionine Fe-S cluster motif
-
-
ir
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
polymorphic variants 239K and 239M, biosynthesis of adenosylcobalamin
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
polymorphic variants 239K and 239M, ATP is highly preferred as adenosyl donor
-
-
?
ATP + cob(I)alamin
triphosphate + adenosylcobalamin
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
r
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
stereospecific process which proceeds with overall inversion of configuration at C-5' of the adenosyl moiety
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
transfers the adenosyl-group of ATP to the reduced cobalt atom of the cobalamin molecule
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
involved in vitamin B12 metabolism
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
-
-
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
-
adenosylcobalamin, B12-coenzyme or deoxyadenosyl-B12
?
ATP + cob(I)alamin
triphosphate + coenzyme B12
the main role of this enzyme is apparently the conversion of inactive cobalamins to adenosyl cobalamin for 1,2 propanediol degradation
-
-
?
ATP + cob(II)alamin
triphosphate + adenosylcob(II)alamine
-
-
-
-
?
ATP + cob(II)alamin
triphosphate + adenosylcob(II)alamine
-
-
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylcobalamin is a cofactor required by the methylmalonyl-CoA mutase
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
cobalamin assimilation and recycling pathway, overview, enzyme deficiency causes methylmalonic aciduria, MMA, is an autosomal recessive disease with symptoms that include ketoacidosis, lethargy, recurrent vomiting, dehydration, respiratory distress, muscular hypotonia and death due to methylmalonic acid levels that are up to 1000fold greater than normal, overview
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
dissociation constant (Kd) of wild-type MMAB for hydroxomethylcobalamin is 0.051 mM and for ATP is 0.365 mM, cobalamin enhances the affinity of MMAB for ATP, while ATP does not show detectable effects on cobalamin binding
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin generates coenzyme B12, i.e. adenosylcobalamin or AdoCbl, an essential cofactor used by enzymes that catalyze intramolecular rearrangements, deaminations, dehydrations, reductions, and reductive dehalogenations
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
adenosylation of the corrinoid ring of cob(I)alamin, active site structure, ATP binding motif at the protein N terminus
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
Limosilactobacillus reuteri CRL1098
-
adenosylation of the corrinoid ring of cob(I)alamin generates coenzyme B12, i.e. adenosylcobalamin or AdoCbl, an essential cofactor used by enzymes that catalyze intramolecular rearrangements, deaminations, dehydrations, reductions, and reductive dehalogenations
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
Limosilactobacillus reuteri CRL1098
-
adenosylation of the corrinoid ring of cob(I)alamin, active site structure, ATP binding motif at the protein N terminus
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
cobalamin is a better substrate than cobinamide, the beta-phosphate of ATP is required for binding to the enzyme
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
the enzyme is required to adenosylate de novo biosynthetic intermediates of adenosylcobalamin and to salvage incomplete and complete corrinoids from the environment of this bacterium
-
-
?
cob(I)alamin + ATP
adenosylcobalamin + triphosphate
-
in vitro reduced flavodoxin provides an electron to generate the co(I)rrinoid substrate in the CobA active site, modeling of enzyme ligand interaction, residues R9 and R165 are important for CobA-FldA docking but not to catalysis, overview
-
-
?
cob(I)alamin + ATP + H2O + H+
adenosylcobalamin + diphosphate + phosphate
-
-
-
-
?
cob(I)alamin + ATP + H2O + H+
adenosylcobalamin + diphosphate + phosphate
-
FMN and NADH are used to reduce cob(III)alamin to cob(I)alamin, the enzyme shows ATP hydrolyzing activity to adenosine and triphosphate in absence of cob(I)alamin
-
-
?
cob(I)inamide + ATP
adenosylcobinamide + triphosphate
-
upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital
-
-
?
cob(I)inamide + ATP
adenosylcobinamide + triphosphate
-
cobalamin is a better substrate than cobinamide, the beta-phosphate of ATP is required for binding to the enzyme
-
-
?
cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
-
-
-
?
cyanocob(I)alamin + ATP
tripolyphosphate + alpha-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide
-
-
-
-
?
additional information
?
-
-
ATP:Cobalamin adenosyltransferases catalyze the transfer a 5'-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B12
-
-
?
additional information
?
-
-
MgATP and Cob(II)alamin binding sites, structure comparison overview
-
-
?
additional information
?
-
-
UTP, GTP, ITP are poor substrates
-
-
?
additional information
?
-
-
S-adenosylmethionine, vitamin B12r or B12a, AMP, ADP are no substrates
-
-
?
additional information
?
-
-
S-adenosylmethionine, vitamin B12r or B12a, AMP, ADP are no substrates
-
-
?
additional information
?
-
-
hydroxocobamides or cyanocobamides in which benzimidazole replaces 5,6-dimethylbenzimidazole, or cyanocobamide in which an adenine group replaces 5,6-dimethylbenzimidazole, can also act as substrates
-
-
?
additional information
?
-
-
the enzyme interacts with the methionine synthase reductase MSR, which catalyzes the reduction of cob(II)almin to cob(I)alamin, both enzymes activate each other, stoichiometry of the MSR-ATR system, overview
-
-
?
additional information
?
-
-
enzyme defects cause methylmalonic aciduria type B, regulation, overview
-
-
?
additional information
?
-
the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step in the conversion of cyanocobalamin, i.e. vitamin B12, to the essential human cofactor adenosylcobalamin, defects in the enzyme through mutations in the gene encoding the enzyme can result in the metabolic disorder known as methylmalonic aciduria, MMA
-
-
?
additional information
?
-
only two of the three active sites within the trimer contain the bound ATP substrate, twenty residues at the enzymes N-terminus become ordered upon binding of ATP to form an ATP-binding site and an extended cleft that likely binds cobalamin, cobalamin binding site structure involving residue R186, overview
-
-
?
additional information
?
-
-
only two of the three active sites within the trimer contain the bound ATP substrate, twenty residues at the enzymes N-terminus become ordered upon binding of ATP to form an ATP-binding site and an extended cleft that likely binds cobalamin, cobalamin binding site structure involving residue R186, overview
-
-
?
additional information
?
-
no in vitro activity by mutants R215K, R225K as well as K78Q, E84K, G87R, D90N, E91K, L92S, S94L, R186W, C189Y, R190C, R191W, E193K, R194G, F212S, S217R, L220P, and L223P
-
-
?
additional information
?
-
-
no in vitro activity by mutants R215K, R225K as well as K78Q, E84K, G87R, D90N, E91K, L92S, S94L, R186W, C189Y, R190C, R191W, E193K, R194G, F212S, S217R, L220P, and L223P
-
-
?
additional information
?
-
no mediation of base-off transition of adenosylcobalamin (key step of catalytic mechanism) by mutants D64G, F83S, G87R, D90N, E91K, L92S, S94L, C189Y, R191W, E193K, R194G, F212S, S217R, L220P, and L223P
-
-
?
additional information
?
-
-
no mediation of base-off transition of adenosylcobalamin (key step of catalytic mechanism) by mutants D64G, F83S, G87R, D90N, E91K, L92S, S94L, C189Y, R191W, E193K, R194G, F212S, S217R, L220P, and L223P
-
-
?
additional information
?
-
-
TTP does not serve as substrate
-
-
?
additional information
?
-
-
The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively
-
-
?
additional information
?
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to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl
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additional information
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hydroxocobamides or cyanocobamides in which benzimidazole replaces 5,6-dimethylbenzimidazole, or cyanocobamide in which an adenine group replaces 5,6-dimethylbenzimidazole, can also act as substrates
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cobyrinic acid is not a substrate
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cobyrinic acid is not a substrate
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crucial role of the 2'-OH group of the ribosyl moiety of ATP, the gamma-phosphate of ATP is critical for positioning the target for nucleophilic attack, differences in the base of the nucleotide have no effect on enzyme activity, 2'-deoxynucleotides fails to serve as substrates
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EutT is necessary and sufficient for growth of a cobA eutT strain on ethanolamine as a carbon and energy or nitrogen source
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the flavodoxin in vivo reducing agent that serves as the electron donor to the enzyme possesses a reduction potential that is considerably more positive than that of the Co2+/1+ couple of the corrinoid substrate, the enzyme overcomes this challenge by formation of an ATP-activated unique paramagnetic Co2+ corrinoid species by partial conversion, overview
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enzyme-substrate interactions, intermediate/transition structures, spectroscopic mechanism analysis, computational modeling, overview
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random or ordered ternary complex mechanism, the N-terminal domain is responsible for the catalytic activity and substrate binding and has similar biochemical properties and kinetic constants as the full-length enzyme
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EuT substrate specificity, overview, reaction cycle involving EutT and CobA, overview
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the enzyme can use free dihydroflavins to drive the adenosylation of cob(II)alamin
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the enzyme is unable to remove the axial solvent ligand from cob(II)inamide and fails to accomplish the Co(II) to Co(I)rrinoid reduction under physiologically relevant conditions
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in the active site, the corrin ring of Co(II)rrinoids is firmly locked in place by several amino acid side chains so as to facilitate the dissociation of the axial ligand
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in the active site, the corrin ring of Co(II)rrinoids is firmly locked in place by several amino acid side chains so as to facilitate the dissociation of the axial ligand
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additional information
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the enzyme can use free dihydroflavins to drive the adenosylation of cob(II)alamin
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additional information
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EutT is necessary and sufficient for growth of a cobA eutT strain on ethanolamine as a carbon and energy or nitrogen source
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GTP, CTP show only small activity as substrates
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indications for cob(I)alamin-binding due to decrease in light absorbance by cob(I)alamin at 388 nm and conversion to a compound with absorbance maximum at 485 nm, different from adenosylcobalamin
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indications for cob(I)alamin-binding due to decrease in light absorbance by cob(I)alamin at 388 nm and conversion to a compound with absorbance maximum at 485 nm, different from adenosylcobalamin
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no ATP: cob(I)alamin adenosyltransferase activity detectable (anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate), no increase in light absorbance by presumably adenosylcobalamin at 525 nm
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no ATP: cob(I)alamin adenosyltransferase activity detectable (anaerobic, 20 min, 80°C, pH 8, in presence of 1 mM titanium (III) citrate), no increase in light absorbance by presumably adenosylcobalamin at 525 nm
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conserved residues are R119, R124, and E126
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conserved residues are R119, R124, and E126
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