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3-butene-1,2-diol
-
holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
3-butyne-1,2-diol
-
holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
adenosylcobinamide 3-(2-methylbenzimidazolyl)propyl phosphate
-
competitive inhibitor with respect to coenzyme B12. Irreversible cleavage of the coenzyme Co-C bond during the inactivation
-
adenosylethylcobalamin
-
strong competitive inhibitor
adenosylmethylcobalamin
-
catalytic efficiency (turnover number to Km-value) of the holoenzyme with adenosylmethylcobalamin is 0.15% of that for the regular coenzyme adenosylcobalamin, Km: 0.0017 mM
adenosylpentylcobalamin
-
strong competitive inhibitor
Chloroacetaldehyde
-
inactivates
coenzyme B12
-
inactivation in absence of substrate
ethylene glycol bis -N,N,N,N-tetraacetic acid
-
beta-aminoethyl ether
glycoaldehyde
-
inactivates
glycolaldehyde hydrate
-
induces the formation of cob(II)alamin and 5'-deoxyadenosine from adenosylcobalamin at the active site of the enzyme, and the resulting complex is inactive
K+
-
16% inhibition at 40 mM
N-ethylmaleimide
-
apoenzyme completely inactivated
O2
-
irreversible inactivation
p-chloromercuriphenylsulfonic acid
-
complete inhibition at 0.1 mM
p-hydroxymercuribenzoate
-
ternary complex stable, apoenzyme unstable
Rb+
-
35% inhibition at 40 mM
styrene glycol
-
competitive inhibitor, Ki: 50.2 mM
thioglycerol
-
holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
1,2-Butanediol
-
-
2,3-Butanediol
-
competitive inhibitor, Ki: 2.08 mM
2,3-Butanediol
-
meso isomer strong inactivator and good substrate, Ki: 0.2 mM, same stereospecificity as in normal catalysis, D- and L-isomers competitive inhibitors, Ki: 0.55 mM and 0.59 mM, respectively
adenosylcobalamin
-
analogues
adenosylcobalamin
-
with e-propionamide group converted to carboxylic acid, inactivation during catalytic process, analogues inhibit if added prior to coenzyme
adenosylcobalamin
-
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
adenosylcobalamin
-
Ki: 0.8 mM
adenosylcobalamin
-
electron paramagnetic resonance data indicate mechanism based mode of coenzyme analogue inactivation, extinction of radical intermediates
adenosylcobalamin
-
analogues
Ca2+
-
-
Ca2+
-
10 mM, complete inhibition
cyanocobalamin
a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor
cyanocobalamin
-
competitive inhibitor
EDTA
-
-
EDTA
-
EDTA inhibition of apoenzyme is reversible at least in the initial phase
EGTA
-
-
EGTA
-
62% inhibition at 0.05 mM
glycerol
-
complete inhibition at 50-100 mM
glycerol
-
reaction ceases within several min
glycerol
adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact adenosylcobalamin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact adenosylcobalmin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact Ado-Cbl, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview
glycerol
-
suicide inactivation in vitro, reactivation possible in presence of coenzyme, Mg2+, ATP in vivo
glycerol
-
stereospecificity: enzyme-R-glycerol complex responsible for product-formation, enzyme-S-glycerol complex responsible for inactivation, several molecules of glycerol per enzyme molecule involved, active-site inhibition, C3-methyl group plays crucial role; suicide inactivation in vitro, reactivation possible in presence of coenzyme, Mg2+, ATP in vivo
glycerol
-
stereospecificity: enzyme-R-glycerol complex responsible for product-formation, enzyme-S-glycerol complex responsible for inactivation, several molecules of glycerol per enzyme molecule involved, active-site inhibition, C3-methyl group plays crucial role
glycerol
-
reactivation in vivo effected by DdrA, DdrB reactivating factor in the presence of coenzyme, ATP, and Mg2+, reactivation by cobalamin exchange, both genes that produce reactivating factor cloned and expressed in E. coli
glycerol
-
reaction ceases within several min
glycerol
-
suicide inactivation, Km value of 5.8 mM
glycerol
-
suicide inhibitor. The linear increase in beta-hydroxypropionaldehyde formation ceases after 4 min
iodoacetamide
-
apoenzyme completely inactivated
iodoacetamide
-
component S, 95% inhibition after pretreatment in 1 mM
iodoacetamide
-
complete inhibition at 5 mM
Mg2+
-
69% inhibition at 40 mM
Mg2+
-
10 mM, slight inhibitor
Mn2+
-
-
Mn2+
-
highest inhibition
Na+
-
41% inhibition at 40 mM
Na+
-
10 mM, complete inhibition
p-chloromercuribenzoate
-
apoenzyme completely inactivated
p-chloromercuribenzoate
-
reversed by thiols
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
92% inhibition by 1 mM
Propane-1,2-diol
-
mechanism-based inactivation obeying first-order reaction kinetics
Propane-1,2-diol
-
leads to inactivation of wild-type and mutant enzymes during catalysis, kinetics, overview
sulfhydryl compounds
-
-
additional information
-
inactivated holoenzymes undergo reactivation by diol dehydratase-reactivating factor in the presence of ATP, Mg2+ and adenosylcobalamin
-
additional information
-
no inhibition by 5 mM of 1,10-phenanthroline, 2,2'-dipyridyl, citrate, succinate, tartrate, malate, and salicylate
-
additional information
-
Asp335 has a strong anticatalytic effect on the OH group migration despite its important role in substrate binding. The synergistic interplay of the O-C bond cleavage by Ca2+ ion and the deprotonation of the spectator OH-group by Glu170 is required to overcome the anticatalytic effect of Asp335
-
additional information
-
-
-
additional information
-
substrate analogues
-
additional information
-
various chemicals and substrate analogues
-
additional information
-
no inhibition with Li+ and NH4+
-
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14000
-
F consisits of one polypeptide, S of at least four subunits, x * 60000, x * 23000, x * 15500, x * 14000, Cys, Lys, His, andArg residues essential for catalysis
15500
-
F consisits of one polypeptide, S of at least four subunits, x * 60000, x * 23000, x * 15500, x * 14000, Cys, Lys, His, andArg residues essential for catalysis
19000
-
alpha2beta2gamma2, 2 * 60000, 2 * 30000, 2 * 19000, SDS-PAGE, recombinant enzyme, beta2 is F component, alpha2gamma2 is S component, mutual effects on folding
19173
-
x * 28071, x * 60348, x * 24113, x * 19173, estimated from nucleotide sequences of cloned genes
19800
-
2 * 61100 + 2 * 35000 + 2 * 19800, SDS-PAGE
200000
-
1 * 26000, 1 * 200000, components F, S
22000
-
alpha2beta2gamma2, 2 * 63000 + 2 * 28000 + 2 * 22000, SDS-PAGE
220000
-
gel filtration, membrane-associated recombinant enzyme
220000 - 240000
-
gel filtration, sedimentation equilibrium of cell-free extracts
23000
-
F consisits of one polypeptide, S of at least four subunits, x * 60000, x * 23000, x * 15500, x * 14000, Cys, Lys, His, andArg residues essential for catalysis
24113
-
x * 28071, x * 60348, x * 24113, x * 19173, estimated from nucleotide sequences of cloned genes
250000
-
gel filtration of membrane extracts
26000
-
1 * 26000, 1 * 200000, components F, S
28000
-
alpha2beta2gamma2, 2 * 63000 + 2 * 28000 + 2 * 22000, SDS-PAGE
28071
-
x * 28071, x * 60348, x * 24113, x * 19173, estimated from nucleotide sequences of cloned genes
30000
-
alpha2beta2gamma2, 2 * 60000, 2 * 30000, 2 * 19000, SDS-PAGE, recombinant enzyme, beta2 is F component, alpha2gamma2 is S component, mutual effects on folding
35000
-
2 * 61100 + 2 * 35000 + 2 * 19800, SDS-PAGE
60348
-
x * 28071, x * 60348, x * 24113, x * 19173, estimated from nucleotide sequences of cloned genes
61100
-
2 * 61100 + 2 * 35000 + 2 * 19800, SDS-PAGE
63000
-
alpha2beta2gamma2, 2 * 63000 + 2 * 28000 + 2 * 22000, SDS-PAGE
15000
-
1 * 60000, 1 * 51000, 1 * 29000, 1 * 15000, SDS-PAGE
15000
-
2 * 60000, 1 * 51000, 2 * 29000, 2 * 15000, SDS-PAGE, subunit stoichiometry confirmed by N-terminal amino acid analysis
207000
-
gel filtration
207000
-
molecular weight of hexamer
230000
-
gel filtration
230000
-
gel filtration, ultracentrifugal sedimentation equilibrium
29000
-
1 * 60000, 1 * 51000, 1 * 29000, 1 * 15000, SDS-PAGE
29000
-
2 * 60000, 1 * 51000, 2 * 29000, 2 * 15000, SDS-PAGE, subunit stoichiometry confirmed by N-terminal amino acid analysis
51000
-
1 * 60000, 1 * 51000, 1 * 29000, 1 * 15000, SDS-PAGE
51000
-
2 * 60000, 1 * 51000, 2 * 29000, 2 * 15000, SDS-PAGE, subunit stoichiometry confirmed by N-terminal amino acid analysis
60000
-
1 * 60000, 1 * 51000, 1 * 29000, 1 * 15000, SDS-PAGE
60000
-
2 * 60000, 1 * 51000, 2 * 29000, 2 * 15000, SDS-PAGE, subunit stoichiometry confirmed by N-terminal amino acid analysis
60000
-
alpha2beta2gamma2, 2 * 60000, 2 * 30000, 2 * 19000, SDS-PAGE, recombinant enzyme, beta2 is F component, alpha2gamma2 is S component, mutual effects on folding
60000
-
F consisits of one polypeptide, S of at least four subunits, x * 60000, x * 23000, x * 15500, x * 14000, Cys, Lys, His, andArg residues essential for catalysis
additional information
-
-
additional information
-
-
additional information
-
-
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E170A E170Q
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme
E170H
-
does not form (alpha-beta-gamma)complex
E170Q
computational mutation study. The spectator OH group is not fully activated in the Glu170Gln and Glu170Ala mutants during the OH group migration, and thus the activation energies in the Glu170Gln and Glu170Ala mutants are higher than that in the wild-type enzyme
E221A
-
does not form (alpha-beta-gamma)complex
Halpha143A
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme
Halpha143E
-
site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes
Halpha143K
-
site-directed mutagenesis, the mutant is inactive and does not form (alphabeta)2 complexes
Halpha143L
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme
Halpha143Q
-
site-directed mutagenesis, the mutant shows residual activity compared to the wild-type enzyme, irreversible inactivation by O2 in the absence of substrate at a much lower rate than the wild type, preference of the Halpha143Q mutant for (R)- and (S)-1,2-propanediols, kinetic parameters for each enantiomer, overview
Kbeta135A
-
site-directed mutagenesis, the mutant shows 42% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin
Kbeta135E
-
site-directed mutagenesis, the mutant shows 98% reduced activity compared to the wild-type enzyme
Kbeta135Q
-
site-directed mutagenesis, the mutant shows 27% reduced activity compared to the wild-type enzyme, the mutant is less sensitive to inhibitor CN-cobalamin
Kbeta135R
-
site-directed mutagenesis, the mutant shows 24% reduced activity compared to the wild-type enzyme
Q296A
-
increased Km for substrate(1,2-propanediol) by a factor of 250
Q336A
the mutant shows decreased activity (21%) compared to the wild type enzyme
S224A
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 5fold reduction in kcat/Km
S224C
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. About 100fold reduction in kcat/Km
S224N
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 100fold reduction in kcat/Km
S301A
the mutant shows decreased activity (76%) compared to the wild type enzyme
S301A/Q336A
the mutant shows lowest activity (9.8%) compared to the wild type enzyme
Salpha224A
-
site-directed mutagenesis, the mutant shows 81% reduced activity compared to the wild-type enzyme, mechanism-based complete inactivation of the Salpha224A holoenzyme during catalysis by propan-1,2-diol leading to accumulation of cobalamin, mechanism, overview
Salpha224N
-
site-directed mutagenesis, the mutant shows 95% reduced activity compared to the wild-type enzyme
T172A
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 100fold reduction in kcat/Km
T172S
mutation in alpha-subunit, a key residue for stabilizing the post-homolysis state of the adenosyl group. More than 10fold reduction in kcat/Km
Q336A
-
the mutant shows decreased activity (21%) compared to the wild type enzyme
-
S301A
-
the mutant shows decreased activity (76%) compared to the wild type enzyme
-
S301A/Q336A
-
the mutant shows lowest activity (9.8%) compared to the wild type enzyme
-
D335A
-
inactive mutant
D335A
-
does not form (alpha-beta-gamma)complex
D335A
computational mutation study. The OH group migration is accelerated in the Asp335Ala mutant, due to the absence of the electric repulsion between Asp335 and the migrating OH group
H143A
-
only very little activity
H143A
computational mutation study. The resonance stabilization of the transition state in the OH group migration is observed in the wild-type enzyme while not in the His143Ala mutant. Since the cleavage of the C2-oxygen bond of 1,2-diol radical proceeds in a more homolytic manner in the His143Ala mutant, Glu170 cannot effectively deprotonate the spectator OH group in the transition state, leading to increased activation energy of the OH group migration in the His143Ala mutant
additional information
-
construction of chimeric enzymes with subunit compositions alphaGbetaD2GgammaG and alphaGbetaGgammaDG, overview
additional information
-
construction of chimeric enzymes with subunit compositions alphaGbetaD2GgammaG and alphaGbetaGgammaDG, overview
additional information
-
construction of chimeric enzymes with subunit compositions alphaGbetaD2GgammaG and alphaGbetaGgammaDG, overview
additional information
-
construction of a fusion protein PduD1-18-eGFP
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Abeles, R.H.
Dehydrations requiring vitamin B12 coenzyme
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
481-497
1971
Klebsiella pneumoniae
-
brenda
Toraya, T.; Fukui, S.
Coenzyme B12-dependent propanediol dehydratase system. Ternary complex between apoenzyme, coenzyme, and substrate analog
Biochim. Biophys. Acta
284
536-548
1972
Klebsiella pneumoniae
brenda
Toraya, T.; Uesaka, M.; Kondo, M.; Fukui, S.
Dissociation of diol dehydrase into two different protein components
Biochem. Biophys. Res. Commun.
52
350-355
1973
Klebsiella pneumoniae
brenda
Toraya, T.
Diol dehydrase and glycerol dehydrase, coenzyme B12-dependent isozymes
Met. Ions Biol. Syst.
30
217-254
1994
Flavobacterium sp., Klebsiella pneumoniae, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Jensen, F.R.; Neese, R.A.
Relative enantiomer binding and reaction rates with propanediol dehydrase
Biochem. Biophys. Res. Commun.
62
816-821
1975
Klebsiella pneumoniae
brenda
Toraya, T.; Shirakashi, T.; Kosuga, T.; Fukui, S.
Substrate specificity of coenzyme B12-dependent diol dehydrase: glycerol as both a good substrate and a potent inactivator
Biochem. Biophys. Res. Commun.
69
475-480
1976
Klebsiella pneumoniae
brenda
Bachovchin, W.W.; Eagar Jr., R.G.; Moore, K.W.; Richards, J.H.
Mechanism of action of Adenosylcobalamin: glycerol and other substrate analogues as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanism
Biochemistry
16
1082-1092
1977
Klebsiella pneumoniae
brenda
Poznanskaja, A.A.; Tanizawa, K.; Soda, K.; Toraya, T.; Fukui, S.
Coenzyme B12-dependent diol dehydrase: purification, subunit heterogeneity, and reversible association
Arch. Biochem. Biophys.
194
379-386
1979
Klebsiella pneumoniae
brenda
Moore, K.W.; Richards, J.H.
Stereospecificity and mechanism of adenosylcobalamin-dependent diol dehydratase. Catalysis and inactivation with meso- and DL-2,3-butanediols as substrates
Biochem. Biophys. Res. Commun.
87
1052-1057
1979
Klebsiella pneumoniae
brenda
Poppe, L.; Retey, J.
Kinetic investigations with inhibitors that mimic the posthomolysis intermediate in the reactions of coenzyme-B12-dependent glycerol dehydratase and diol deydratase
Eur. J. Biochem.
245
398-401
1997
Klebsiella pneumoniae
brenda
Toraya, T.; Abeles, R.H.
Inactivation of dioldehydrase in the presence of a coenzyme-B12 analog
Arch. Biochem. Biophys.
203
174-180
1980
Klebsiella pneumoniae
brenda
McGee, D.E.; Richards, J.H.
Purification and subunit characterization of propanediol dehydratase, a membrane-associated enzyme
Biochemistry
20
4293-4298
1981
Klebsiella pneumoniae
brenda
Toraya, T.; Fukui, S.
Diol dehydrase
B12 (Dolphin, D. ed. ) Wiley, New York
2
233-262
1982
Citrobacter freundii, Klebsiella pneumoniae, Propionibacterium freudenreichii
-
brenda
Forage, R.G.; Foster, M.A.
Glycerol fermentation in Klebsiella pneumoniae: functions of the coenzyme B12-dependent glycerol and diol dehydratases
J. Bacteriol.
149
413-419
1982
Klebsiella pneumoniae
brenda
McGee, D.E.; Carroll, S.S.; Bond, M.W.
Diol dehydratase: N-terminal amino acid sequences and subunit stoichiometry
Biochem. Biophys. Res. Commun.
108
547-551
1982
Klebsiella pneumoniae
brenda
Schuetz, H.; Radler, F.
Propanediol-1,2-dehydratase and metabolism of glycerol of Lactobacillus brevis
Arch. Microbiol.
139
366-370
1984
Levilactobacillus brevis, Lentilactobacillus buchneri
-
brenda
Ichikawa, Y.; Horike, Y.; Mori, N.; Hosoi, N.; Kitamoto, Y.
Purification and properties of propanediol dehydratase from Propionibacterium freudenreichii
J. Ferment. Technol.
63
135-141
1985
Propionibacterium freudenreichii
-
brenda
Hartmanis, M.G.N.; Stadtman, T.C.
Diol metabolism and diol dehydratase in Clostridium glycoliticum
Arch. Biochem. Biophys.
245
144-152
1986
Terrisporobacter glycolicus
brenda
Tanizawa, K.; Nakijama, N.; Toraya, T.; Tanaka, H.; Soda, K.
Re-investigation of the protein structure of coenzyme-B12-dependent diol dehydrase
Z. Naturforsch. C
42
353-359
1986
Klebsiella pneumoniae
brenda
Masuda, J.; Yamaguchi, T.; Tobimatsu, T.; Toraya, T.; Suto, K.; Shibata, N.; Morimoto, Y.; Higuchi, Y.; Yasuoka, N.
Crystallization and preliminary X-ray study of two crystal forms of Klebsiella oxytoca diol dehydratase-cyanocobalamin complex
Acta Crystallogr. Sect. D
55
907-909
1999
Klebsiella pneumoniae
brenda
Toraya, T.; Mori, K.
A reactivating factor for coenzyme B12-dependent diol dehydratase
J. Biol. Chem.
274
3372-3377
1999
Klebsiella pneumoniae
brenda
Yamanishi, M.; Yamada, S.; Ishida, A.; Yamauchi, J.; Toraya, T.
EPR spectroscopic evidence for the mechanism-based inactivation of adenosylcobalamin-dependent diol dehydratase by coenzyme analogs
J. Biochem.
124
598-601
1998
Klebsiella pneumoniae
brenda
Schramm, E.; Schink, B.
Ether-cleaving enzyme and diol dehydratase involved in anaerobic polyethylene glycol degradation by a new Acetobacterium sp
Biodegradation
2
71-79
1991
Acetobacterium sp.
brenda
Ishida, A.; Toraya, T.
Adenosylcobinamide methyl phosphate as a pseudocoenzyme for diol dehydrase
Biochemistry
32
1535-1540
1993
Klebsiella pneumoniae
brenda
Tobimatsu, T.; Sakai, T.; Hashida, Y.; Mizoguchi, N.; Miyoshi, S.; Toraya, T.
Heterologous expression, purification, and properties of diol dehydratase, an adenosylcobalamin-dependent enzyme of Klebsiella oxytoca
Arch. Biochem. Biophys.
247
132-140
1997
Klebsiella pneumoniae
brenda
Hartmanis, M.G.N.
Diol dehydrase from Clostridium glycolyticum: the non-B12-dependent enzyme
Met. Ions Biol. Syst.
30
201-215
1994
Terrisporobacter glycolicus
-
brenda
Tobimatsu, T.; Kajiura, H.; Toraya, T.
Specificities of reactivating factors for adenosylcobalamin-dependent diol dehydratase and glycerol dehydratase
Arch. Microbiol.
174
81-88
2000
Klebsiella oxytoca, Klebsiella pneumoniae
brenda
Mori, K.; Toraya, T.
Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor
Biochemistry
38
13170-13178
1999
Klebsiella oxytoca
brenda
Abend, A.; Bandarian, V.; Reed, G.H.; Frey, P.A.
Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase
Biochemistry
39
6250-6257
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Toraya, T.
Radical catalysis of B12 enzymes: structure, mechanism, inactivation, and reactivation of diol and glycerol dehydratases
Cell. Mol. Life Sci.
57
106-127
2000
Klebsiella oxytoca, Klebsiella pneumoniae
brenda
Sauvageot, N.; Pichereau, V.; Louarme, L.; Hartke, A.; Auffray, Y.; Laplace, J.M.
Purification, characterization and subunits identification of the diol dehydratase of Lactobacillus collinoides
Eur. J. Biochem.
269
5731-5737
2002
Secundilactobacillus collinoides
brenda
Fukuoka, M.; Yamada, S.; Miyoshi, S.; Yamashita, K.; Yamanishi, M.; Zou, X.; Brown, K.L.; Toraya, T.
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
J. Biochem.
132
935-943
2002
Klebsiella oxytoca
brenda
Shibata, N.; Nakanishi, Y.; Fukuoka, M.; Yamanishi, M.; Yasuoka, N.; Toraya, T.
Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase
J. Biol. Chem.
278
22717-22725
2003
Klebsiella oxytoca
brenda
Masuda, J.; Shibata, N.; Morimoto, Y.; Toraya, T.; Yasuoka, N.
How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex
Structure Fold. Des.
8
775-788
2000
Klebsiella oxytoca
brenda
Fukuoka, M.; Nakanishi, Y.; Hannak, R.B.; Krautler, B.; Toraya, T.
Homoadenosylcobalamins as probes for exploring the active sites of coenzyme B12-dependent diol dehydratase and ethanolamine ammonia-lyase
FEBS J.
272
4787-4796
2005
Klebsiella oxytoca
brenda
Tobimatsu, T.; Kawata, M.; Toraya, T.
The N-terminal regions of beta and gamma subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase
Biosci. Biotechnol. Biochem.
69
455-462
2005
Klebsiella oxytoca
brenda
Mansoorabadi, S.O.; Magnusson, O.T.; Poyner, R.R.; Frey, P.A.; Reed, G.H.
Analysis of the Cob(II)alamin-5-deoxy-3,4-anhydroadenosyl radical triplet spin system in the active site of diol dehydrase
Biochemistry
45
14362-14370
2006
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Schwartz, P.A.; Frey, P.A.
Dioldehydrase: an essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin
Biochemistry
46
7293-7301
2007
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kajiura, H.; Mori, K.; Shibata, N.; Toraya, T.
Molecular basis for specificities of reactivating factors for adenosylcobalamin-dependent diol and glycerol dehydratases
FEBS J.
274
5556-5566
2007
Klebsiella oxytoca, Klebsiella pneumoniae
brenda
Sakai, T.; Yamasaki, A.; Toyofuku, S.; Nishiki, T.; Yunoki, M.; Komoto, N.; Tobimatsu, T.; Toraya, T.
Construction and characterization of hybrid dehydratases between adenosylcobalamin-dependent diol and glycerol dehydratases
J. Nutr. Sci. Vitaminol.
53
102-108
2007
Klebsiella oxytoca, Klebsiella pneumoniae
brenda
Kawata, M.; Kinoshita, K.; Takahashi, S.; Ogura, K.; Komoto, N.; Yamanishi, M.; Tobimatsu, T.; Toraya, T.
Survey of Catalytic Residues and Essential Roles of Glutamate-aplpha170 and Aspartate-alpha335 in Coenzyme B12-dependent Diol Dehydratase
J. Biol. Chem.
281
18327-18334
2006
Klebsiella oxytoca
brenda
Schwartz, P.A.; Lobrutto, R.; Reed, G.H.; Frey, P.A.
Probing interactions from solvent-exchangeable protons and monovalent cations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase
Protein Sci.
16
1157-1164
2007
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Tobimatsu, T.; Nishiki, T.; Morimoto, M.; Miyata, R.; Toraya, T.
Low-solubility glycerol dehydratase, a chimeric enzyme of coenzyme B(12)-dependent glycerol and diol dehydratases
Arch. Microbiol.
191
199-206
2008
Salmonella enterica, Klebsiella oxytoca, Klebsiella pneumoniae
brenda
Kinoshita, K.; Kawata, M.; Ogura, K.; Yamasaki, A.; Watanabe, T.; Komoto, N.; Hieda, N.; Yamanishi, M.; Tobimatsu, T.; Toraya, T.
Histidine-alpha143 assists 1,2-hydroxyl group migration and protects radical intermediates in coenzyme B12-dependent diol dehydratase
Biochemistry
47
3162-3173
2008
Klebsiella oxytoca
brenda
Ogura, K.; Kunita, S.; Mori, K.; Tobimatsu, T.; Toraya, T.
Roles of adenine anchoring and ion pairing at the coenzyme B12-binding site in diol dehydratase catalysis
FEBS J.
275
6204-6216
2008
Klebsiella oxytoca
brenda
Sriramulu, D.D.; Liang, M.; Hernandez-Romero, D.; Raux-Deery, E.; Luensdorf, H.; Parsons, J.B.; Warren, M.J.; Prentice, M.B.
Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation
J. Bacteriol.
190
4559-4567
2008
Limosilactobacillus reuteri
brenda
Toraya, T.; Tamura, N.; Watanabe, T.; Yamanishi, M.; Hieda, N.; Mori, K.
Mechanism-based inactivation of coenzyme B12-dependent diol dehydratase by 3-unsaturated 1,2-diols and thioglycerol
J. Biochem.
144
437-446
2008
Klebsiella oxytoca
brenda
Parsons, J.B.; Dinesh, S.D.; Deery, E.; Leech, H.K.; Brindley, A.A.; Heldt, D.; Frank, S.; Smales, C.M.; Luensdorf, H.; Rambach, A.; Gass, M.H.; Bleloch, A.; McClean, K.J.; Munro, A.W.; Rigby, S.E.; Warren, M.J.; Prentice, M.B.
Biochemical and structural insights into bacterial organelle form and biogenesis
J. Biol. Chem.
283
14366-14375
2008
Citrobacter freundii (B1VB64), Citrobacter freundii (B1VB65), Citrobacter freundii (B1VB66)
brenda
Toraya, T.; Honda, S.; Mori, K.
Coenzyme B12-dependent diol dehydratase is a potassium ion-requiring calcium metalloenzyme: evidence that the substrate-coordinated metal ion is calcium
Biochemistry
49
7210-7217
2010
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724
brenda
Mori, K.; Hosokawa, Y.; Yoshinaga, T.; Toraya, T.
Diol dehydratase-reactivating factor is a reactivase - evidence for multiple turnovers and subunit swapping with diol dehydratase
FEBS J.
277
4931-4943
2010
Klebsiella oxytoca (Q59470), Klebsiella oxytoca (Q59471), Klebsiella oxytoca (Q59472)
brenda
Kamachi, T.; Doitomi, K.; Takahata, M.; Toraya, T.; Yoshizawa, K.
Catalytic roles of the metal ion in the substrate-binding site of coenzyme B12-dependent diol dehydratase
Inorg. Chem.
50
2944-2952
2011
Klebsiella oxytoca
brenda
Fan, C.; Bobik, T.A.
The N-terminal region of the medium subunit (PduD) packages adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu microcompartment
J. Bacteriol.
193
5623-5628
2011
Salmonella enterica
brenda
Wei, X.; Meng, X.; Chen, Y.; Wei, Y.; Du, L.; Huang, R.
Cloning, expression, and characterization of coenzyme-B12-dependent diol dehydratase from Lactobacillus diolivorans
Biotechnol. Lett.
36
159-165
2014
Lentilactobacillus diolivorans, Lentilactobacillus diolivorans DSM 14421
brenda
Yamanishi, M.; Kinoshita, K.; Fukuoka, M.; Saito, T.; Tanokuchi, A.; Ikeda, Y.; Obayashi, H.; Mori, K.; Shibata, N.; Tobimatsu, T.; Toraya, T.
Redesign of coenzyme B12 dependent diol dehydratase to be resistant to the mechanism-based inactivation by glycerol and act on longer chain 1,2-diols
FEBS J.
279
793-804
2012
Klebsiella oxytoca (Q59470), Klebsiella oxytoca ATCC 8724 (Q59470)
brenda
Shibata, N.; Sueyoshi, Y.; Higuchi, Y.; Toraya, T.
Direct participation of a peripheral side chain of a corrin ring in coenzyme B12 catalysis
Angew. Chem. Int. Ed. Engl.
57
7830-7835
2018
Klebsiella oxytoca (Q59470)
brenda
Toraya, T.; Tanokuchi, A.; Yamasaki, A.; Nakamura, T.; Ogura, K.; Tobimatsu, T.
Diol dehydratase-reactivase is essential for recycling of coenzyme B12 in diol dehydratase
Biochemistry
55
69-78
2016
Klebsiella oxytoca (Q59470 and Q59471 and Q59472), Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724 (Q59470 and Q59471 and Q59472)
brenda
Levin, B.J.; Balskus, E.P.
Characterization of 1,2-propanediol dehydratases reveals distinct mechanisms for B12-dependent and glycyl radical enzymes
Biochemistry
57
3222-3226
2018
Roseburia inulinivorans, Klebsiella oxytoca (Q59470 and Q59471 and Q59472), Roseburia inulinivorans A2-194, Klebsiella oxytoca ATCC 8724 (Q59470 and Q59471 and Q59472)
brenda
Doitomi, K.; Kamachi, T.; Toraya, T.; Yoshizawa, K.
Computational mutation study of the roles of catalytic residues in coenzyme B12-dependent diol dehydratase
Bull. Chem. Soc. JPN
89
955-964
2016
Klebsiella oxytoca (Q59470)
-
brenda
Ghiaci, P.; Norbeck, J.; Larsson, C.
2-Butanol and butanone production in Saccharomyces cerevisiae through combination of a B12 dependent dehydratase and a secondary alcohol dehydrogenase using a TEV-based expression system
PLoS ONE
9
e102774
2014
Saccharomyces cerevisiae
brenda