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(2S,3S)-3-methylaspartate
L-glutamate
-
-
-
-
r
(S)-2-hydroxyglutarate
(2S,3S)-3-methylmalate
-
-
analysis of the energy profile for the various intermediate steps of reaction
-
?
L-2-hydroxyglutarate
L-threo-3-methylmalate
-
rate-limiting step is most likely the rearrangement of the 2-hydroxyglutaryl radical to the 3-methylmalyl radical
-
?
L-Glu
L-threo-3-methylaspartate
L-Glu
threo-3-Methylaspartate
L-glutamate
L-threo-3-methylaspartate
L-glutamate
threo-3-methyl-L-aspartate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
additional information
?
-
-
the catalytic mechanism proceeds via a fragmentation/recombination sequence with intermediates stabilized by partial protonation/deprotonation
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
the enzyme is involved in the dissimilation of Glu to acetyl-CoA and pyruvate through the following pathway
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
first step in Glu fermentation pathway
-
-
?
Glu
?
Clostridium saccharobutyricum
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
initial reaction in anaerobic degradation of Glu
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
Glu
?
-
the enzyme is involved in the dissimilation of Glu to acetyl-CoA and pyruvate through the following pathway
-
-
?
Glu
?
-
energy-yielding fermentation of Glu
-
-
?
L-Glu
L-threo-3-methylaspartate
-
-
-
r
L-Glu
L-threo-3-methylaspartate
-
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
r
-
?
L-Glu
threo-3-Methylaspartate
-
equilibrium favours glutamate formation
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
(2S,3S)-3-methylaspartate
?
L-Glu
threo-3-Methylaspartate
-
high-level quantum chemistry calculations on catalytic reaction. Overall reaction is exothermic by 5.2 kJ per mol, while the equilibrium for the reaction in aqueous solution lies in the opposite direction
-
-
?
L-Glu
threo-3-Methylaspartate
Clostridium saccharobutyricum
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
(2S,3S)-3-methylaspartate
?
L-Glu
threo-3-Methylaspartate
-
r
-
?
L-Glu
threo-3-Methylaspartate
-
equilibrium favours glutamate formation
-
?
L-Glu
threo-3-Methylaspartate
-
in the reverse reaction: erythro-3-methylaspartate does not serve as substrate
-
?
L-Glu
threo-3-Methylaspartate
-
L-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
-
-
?
L-Glu
threo-3-Methylaspartate
-
r
-
?
L-Glu
threo-3-Methylaspartate
-
equilibrium favours glutamate formation
-
?
L-glutamate
L-threo-3-methylaspartate
-
-
-
?
L-glutamate
L-threo-3-methylaspartate
-
-
-
?
L-glutamate
L-threo-3-methylaspartate
-
-
-
?
L-glutamate
L-threo-3-methylaspartate
-
kinetic competence of acrylate and glycyl radical as intermediates in the rearrangement of glutamate to methylaspartate
-
?
L-glutamate
L-threo-3-methylaspartate
-
-
-
-
?
L-glutamate
L-threo-3-methylaspartate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
-
-
-
-
r
L-threo-3-methylaspartate
L-glutamate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
-
-
-
r
L-threo-3-methylaspartate
L-glutamate
-
-
-
r
L-threo-3-methylaspartate
L-glutamate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
-
equilibrium constants favouring glutamate over 3-methylaspartate, formation of L-threo-(2S,3S)- and L-erythro-(2S,3R)-3-methylaspartate in the reverse reaction direction
no activity with D-glutamate
-
?
L-threo-3-methylaspartate
L-glutamate
-
-
-
-
?
L-threo-3-methylaspartate
L-glutamate
-
equilibrium constants favouring glutamate over 3-methylaspartate, formation of L-threo-(2S,3S)- and L-erythro-(2S,3R)-3-methylaspartate in the reverse reaction direction
no activity with D-glutamate
-
?
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E171A
-
turnover number for glutamate is reduced 27.6fold, KM-value is increased 1.1fold, Km-value for adenosylcobalamin is reduced 1.23fold
E171D
-
turnover number for glutamate is reduced 1.8fold, KM-value is reduced 1.54fold, Km-value for adenosylcobalamin is reduced 2.7fold
E171N
-
turnover number for glutamate is reduced 232fold, KM-value is increased by 1.8fold, Km-value for adenosylcobalamin is reduced 1.4fold
E171Q
-
turnover number for glutamate is reduced 53fold, KM-value is reduced 2.4fold, Km-value for adenosylcobalamin is reduced 2fold, mutant enzyme is independent of pH
R100M
-
no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 276fold compared to wild-type enzyme, KM-value for glutamate is increased 13fold compared to wild-type enzyme
R100Y
-
no cob(II)alamin detected in UV-visible spectrum. Km-value for glutamate is reduced 322fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme
C15A
-
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
C15N
-
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
C15S
-
Cys15Ser and Cys15Ala of enzyme component S are active, but exhibit decreased maximal velocity and increased apparent Km-value for adenosylcobalamin. Mutants Cys15Asp and Cys15Asn of component S of the methylaspartate are inactive
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, glutamate binding is significantly weakened. 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. Km-value for glutamate is reduced 121fold compared to wild-type enzyme, KM-value for glutamate is increased 17fold compared to wild-type enzyme
R100K
-
mutation significantly impairs the ability of enzyme to catalyze the rearrangement of substrate radical to product radical
additional information
-
the S subunit is genetically fused to the C-terminus of the E subunit through an 11 amino acid 5-Gly linker segment. The affinity of adenosylcobalamine is unchanged, but the turnover-number and the Km-value for Glu in the conversion of L-Glu to (2S,3S)-3-methylaspartate are decreased by about a third
additional information
-
fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit
additional information
production of mesaconate in Escherichia coli by engineered glutamate mutase pathway, establishment of mesaconate pathway in Escherichia coli. First, glutamate is synthesized from glucose via glycolysis and TCA cycle.Then glutamate is converted into 3-methylaspartate by glutamate mutase. Finally, mesaconate is formed by elimination of ammonia from 3-methylaspartate via MAL. Since Escherichia coli does not contain glutamate mutase and 3-methylaspartate ammonia lyase, the two enzymes from Clostridium tetanomorphum are heterologously expressed. To increase the flux from glutamate to mesaconate, two effective strategies are employed to optimize the critical enzyme activity in the pathway: one is regenerating inactive mutase. The other is enhancing the availability of glutamate mutase (stability) and coenzyme B12 (regeneration). For the highest mesaconate production strain EM9, the consumed glutamate is 6.91 g/l (40.9 mM) and mesaconate titer is 7.81 g/l (60 mM). The GlmE from Clostridium cochlearium shows best performance in mesaconate titer because GlmE is more stable than MutE
additional information
-
production of mesaconate in Escherichia coli by engineered glutamate mutase pathway, establishment of mesaconate pathway in Escherichia coli. First, glutamate is synthesized from glucose via glycolysis and TCA cycle.Then glutamate is converted into 3-methylaspartate by glutamate mutase. Finally, mesaconate is formed by elimination of ammonia from 3-methylaspartate via MAL. Since Escherichia coli does not contain glutamate mutase and 3-methylaspartate ammonia lyase, the two enzymes from Clostridium tetanomorphum are heterologously expressed. To increase the flux from glutamate to mesaconate, two effective strategies are employed to optimize the critical enzyme activity in the pathway: one is regenerating inactive mutase. The other is enhancing the availability of glutamate mutase (stability) and coenzyme B12 (regeneration). For the highest mesaconate production strain EM9, the consumed glutamate is 6.91 g/l (40.9 mM) and mesaconate titer is 7.81 g/l (60 mM). The GlmE from Clostridium cochlearium shows best performance in mesaconate titer because GlmE is more stable than MutE
additional information
-
production of mesaconate in Escherichia coli by engineered glutamate mutase pathway, establishment of mesaconate pathway in Escherichia coli. First, glutamate is synthesized from glucose via glycolysis and TCA cycle.Then glutamate is converted into 3-methylaspartate by glutamate mutase. Finally, mesaconate is formed by elimination of ammonia from 3-methylaspartate via MAL. Since Escherichia coli does not contain glutamate mutase and 3-methylaspartate ammonia lyase, the two enzymes from Clostridium tetanomorphum are heterologously expressed. To increase the flux from glutamate to mesaconate, two effective strategies are employed to optimize the critical enzyme activity in the pathway: one is regenerating inactive mutase. The other is enhancing the availability of glutamate mutase (stability) and coenzyme B12 (regeneration). For the highest mesaconate production strain EM9, the consumed glutamate is 6.91 g/l (40.9 mM) and mesaconate titer is 7.81 g/l (60 mM). The GlmE from Clostridium cochlearium shows best performance in mesaconate titer because GlmE is more stable than MutE
-
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Bothe, H.; Darley, D.J.; Albracht, S.P.; Gerfen, G.J.; Golding, B.T.; Buckel, W.
Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium
Biochemistry
37
4105-4113
1998
Clostridium cochlearium
brenda
Ohmori, H.; Ishitani, H.; Sato, K.; Shimizu, S.; Fukui, S.
Vitamin B12 dependent glutamate mutase activity in photosynthetic bacteria
Biochem. Biophys. Res. Commun.
43
156-162
1971
Cereibacter sphaeroides, Rhodospirillum rubrum
brenda
Eagar, R.G.; Baltimore, B.G.; Herbst, M.M.; Barker, H.A.; Richards, J.H.
Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of beta-methylaspartate to glutamate
Biochemistry
11
253-264
1972
Clostridium tetanomorphum
brenda
Ohmori, H.; Ishitani, H.; Sato, K.; Shimizu, S.; Fukui, S.
Metabolism of glutamate in purple nonsulfur bacteria. Participation of vitamin B12
Agric. Biol. Chem.
38
359-365
1974
Cereibacter sphaeroides, Rhodospirillum rubrum
-
brenda
Barker, H.A.
Glutamate mutase
Methods Enzymol.
13
319-330
1969
Clostridium tetanomorphum
-
brenda
Switzer, R.L.
Glutamate mutase
B12 (Dolphin, D. ed. ) Wiley, New York
2
289-305
1982
Acetoanaerobium sticklandii, Cereibacter sphaeroides, Clostridium cochlearium, Clostridium saccharobutyricum, Clostridium sp., Clostridium sp. SB4, Clostridium tetani, Clostridium tetanomorphum, no activity in Acidaminococcus fermentans, no activity in Clostridium microsporum, no activity in Fusobacterium fusiforme, no activity in Fusobacterium nucleatum, no activity in Micrococcus aerogenes, Rhodospirillum rubrum
-
brenda
Barker, H.A.
beta-Methylaspartate-glutamate mutase from Clostridium tetanomorphum
Methods Enzymol.
113
121-133
1985
Clostridium tetanomorphum
brenda
Barker, H.A.
Coenzyme B12-dependent mutases causing carbon chain rearrangements
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
509-537
1972
Clostridium cochlearium, Clostridium tetanomorphum, Cereibacter sphaeroides, Rhodospirillum rubrum
-
brenda
Marsh, E.N.G.
Tritium isotope effects in adenosylcobalamin-dependent glutamate mutase: implications for the mechanism
Biochemistry
34
7542-7547
1995
Clostridium tetanomorphum
brenda
Chen, H.P.; Marsh, E.N.G.
Adenosylcobalamin-dependent glutamate mutase: examination of substrate and coenzyme binding in an engineered fusion protein possessing simplified subunit structure and kinetic properties
Biochemistry
36
14939-14945
1997
Clostridium cochlearium
brenda
Hartzoulakis, B.; Gani, D.
The mechanism of glutamate mutase: an unusually substrate-specific enzyme
Proc. Indian Acad. Sci. Chem. Sci.
106
1165-1176
1994
Clostridium tetanomorphum
-
brenda
Buckel, W.; Golding, B.T.
Glutamate and 2-methyleneglutarate mutase: from microbial curiosities to paradigms for coenzyme B12-dependent enzymes
Chem. Soc. Rev.
25
329-337
1996
Clostridium cochlearium, Clostridium tetanomorphum
-
brenda
Holloway, D.E.; Harding, S.E.; Marsh, E.N.G.
Adenosylcobalamin-dependent glutamate mutase: properties of a fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit
Biochem. J.
320
825-830
1996
Clostridium tetanomorphum
brenda
Holloway, D.E.; Chen, H.P.; Marsh, E.N.G.
Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase
J. Biol. Chem.
271
29121-29125
1996
Clostridium tetanomorphum
brenda
Holloway, D.E.; Marsh, E.N.G.
Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme
J. Biol. Chem.
269
20425-20430
1994
Clostridium tetanomorphum
brenda
Leutbecher, U.; Bcher, R.; Linder, D.; Buckel, W.
Glutamate mutase from Clostridium cochlearium
Eur. J. Biochem.
205
759-765
1992
Clostridium cochlearium
brenda
Reitzer, R.; Krasser, M.; Jogl, G.; Buckel, W.; Bothe, H.; Kratky, C.
Crystallization and preliminary X-ray analysis of recombinant glutamate mutase and of the isolated component S from Clostridium cochlearium
Acta Crystallogr. Sect. D
54
1039-1042
1998
Clostridium cochlearium
brenda
Zelder, O.; Beatrix, B.; Leutbecher, U.; Buckel, W.
Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli
Eur. J. Biochem.
226
577-585
1994
Clostridium cochlearium
brenda
Tollinger, M.; Konrat, R.; Hilbert, B.H.; Marsh, E.N.; Krautler, B.
How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum
Structure
15
1021-1033
1998
Clostridium tetanomorphum
brenda
Roymoulik, I.; Moon, N.; Dunham, W.R.; Ballou, D.P.; Marsh, E.N.
Rearrangement of L-2-hydroxyglutarate to L-threo-3-methylmalate catalyzed by adenosylcobalamin-dependent glutamate mutase
Biochemistry
39
10340-10346
2000
Clostridium cochlearium
brenda
Huhta, M.S.; Ciceri, D.; Golding, B.T.; Marsh, E.N.
A novel reaction between adenosylcobalamin and 2-methyleneglutarate catalyzed by glutamate mutase
Biochemistry
41
3200-3206
2002
Clostridium cochlearium
brenda
Xia, L.; Ballou, D.P.; Marsh, E.N.
Role of arg100 in the active site of adenosylcobalamin-dependent glutamate mutase
Biochemistry
43
3238-3245
2004
Clostridium cochlearium
brenda
Madhavapeddi, P.; Marsh, E.N.
The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase
Chem. Biol.
8
1143-1149
2001
Clostridium cochlearium
brenda
Hoffmann, B.; Tollinger, M.; Konrat, R.; Huhta, M.; Marsh, E.N.G.; Krautler, B.
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
ChemBioChem
2
643-655
2001
Clostridium tetanomorphum
brenda
Gruber, K.; Kratky, C.
Coenzyme B(12) dependent glutamate mutase
Curr. Opin. Chem. Biol.
6
598-603
2002
Clostridium cochlearium
brenda
Hoffmann, B.; Konrat, R.; Bothe, H.; Buckel, W.; Krautler, B.
Structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium cochlearium
Eur. J. Biochem.
263
178-188
1999
Clostridium cochlearium
brenda
Chih, H.W.; Marsh, E.N.G.
Mechanism of glutamate mutase: identification and kinetic competence of acrylate and glycyl radical as intermediates in the rearrangement of glutamate to methylaspartate
J. Am. Chem. Soc.
122
10732-10733
2000
Clostridium cochlearium
-
brenda
Roymoulik, I.; Chen, H.P.; Marsh, E.N.
The reaction of the substrate analog 2-ketoglutarate with adenosylcobalamin-dependent glutamate mutase
J. Biol. Chem.
274
11619-11622
1999
Clostridium cochlearium
brenda
Tollinger, M.; Eichmuller, C.; Konrat, R.; Huhta, M.S.; Marsh, E.N.; Krautler, B.
The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12)
J. Mol. Biol.
309
777-791
2001
Clostridium tetanomorphum
brenda
Reitzer, R.; Gruber, K.; Jogl, G.; Wagner, U.G.; Bothe, H.; Buckel, W.; Kratky, C.
Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights
Structure
7
891-902
1999
Clostridium cochlearium
brenda
Cheng, M.C.; Marsh, E.N.
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
Biochemistry
43
2155-2158
2004
Clostridium cochlearium
brenda
Brooks, A.J.; Fox, C.C.; Marsh, E.N.; Vlasie, M.; Banerjee, R.; Brunold, T.C.
Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase
Biochemistry
44
15167-15181
2005
Clostridium cochlearium
brenda
Cheng, M.C.; Marsh, E.N.
Isotope effects for deuterium transfer between substrate and coenzyme in adenosylcobalamin-dependent glutamate mutase
Biochemistry
44
2686-2691
2005
Clostridium cochlearium
brenda
Sension, R.J.; Cole, A.G.; Harris, A.D.; Fox, C.C.; Woodbury, N.W.; Lin, S.; Marsh, E.N.G.
Photolysis and recombination of adenosylcobalamin bound to glutamate mutase
J. Am. Chem. Soc.
126
1598-1599
2004
Clostridium cochlearium
brenda
Sension, R.J.; Harris, D.A.; Stickrath, A.; Cole, A.G.; Fox, C.C.; Marsh, E.N.G.
Time-resolved measurements of the photolysis and recombination of adenosylcobalamin bound to glutamate mutase
J. Phys. Chem. B
109
18146-18152
2005
Clostridium cochlearium
brenda
Li, Y.; Ling, H.; Li, W.; Tan, H.
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
Metab. Eng.
7
165-173
2005
Streptomyces ansochromogenes
brenda
Patwardhan, A.; Marsh, E.N.
Changes in the free energy profile of glutamate mutase imparted by the mutation of an active site arginine residue to lysine
Arch. Biochem. Biophys.
461
194-199
2007
Clostridium cochlearium
brenda
Yoon, M.; Patwardhan, A.; Qiao, C.; Mansoorabadi, S.O.; Menefee, A.L.; Reed, G.H.; Marsh, E.N.
Reaction of adenosylcobalamin-dependent glutamate mutase with 2-thiolglutarate
Biochemistry
45
11650-11657
2006
Clostridium cochlearium
brenda
Cheng, M.C.; Marsh, E.N.
Evidence for coupled motion and hydrogen tunneling of the reaction catalyzed by glutamate mutase
Biochemistry
46
883-889
2007
Clostridium cochlearium
brenda
Weng, Y.; Hsu, F.; Yang, W.; Chen, H.
Optimization of the overexpression of glutamate mutase S component under the control of T7 system by using lactose and IPTG as the inducers
Enzyme Microb. Technol.
38
465-469
2006
Clostridium tetanomorphum
-
brenda
Sandala, G.M.; Smith, D.M.; Marsh, E.N.; Radom, L.
Toward an improved understanding of the glutamate mutase system
J. Am. Chem. Soc.
129
1623-1633
2007
Clostridium cochlearium
brenda
Chen, H.P.; Hsu, H.J.; Hsu, F.C.; Lai, C.C.; Hsu, C.H.
Interactions between coenzyme B analogs and adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum
FEBS J.
275
5960-5968
2008
Clostridium tetanomorphum
brenda
Yoon, M.; Song, H.; Hakansson, K.; Marsh, E.N.
Hydrogen tunneling in adenosylcobalamin-dependent glutamate mutase: evidence from intrinsic kinetic isotope effects measured by intramolecular competition
Biochemistry
49
3168-3173
2010
Homo sapiens
brenda
Ramezani, M.; Resmer, K.L.; White, R.L.
Glutamate racemization and catabolism in Fusobacterium varium
FEBS J.
278
2540-2551
2011
Fusobacterium varium
brenda
Kozlowski, P.M.; Kamachi, T.; Kumar, M.; Nakayama, T.; Yoshizawa, K.
Theoretical analysis of the diradical nature of adenosylcobalamin cofactor-tyrosine complex in B12-dependent mutases: inspiring PCET-driven enzymatic catalysis
J. Phys. Chem. B
114
5928-5939
2010
Clostridium cochlearium (P80077), Clostridium cochlearium (P80078)
brenda
Biedendieck, R.; Malten, M.; Barg, H.; Bunk, B.; Martens, J.H.; Deery, E.; Leech, H.; Warren, M.J.; Jahn, D.
Metabolic engineering of cobalamin (vitamin B12) production in Bacillus megaterium
Microb. Biotechnol.
3
24-37
2010
Priestia megaterium
brenda
Rommel, J.B.; Kaestner, J.
The fragmentation-recombination mechanism of the enzyme glutamate mutase studied by QM/MM simulations
J. Am. Chem. Soc.
133
10195-10203
2011
Clostridium cochlearium
brenda
Rommel, J.B.; Liu, Y.; Werner, H.J.; Kaestner, J.
Role of tunneling in the enzyme glutamate mutase
J. Phys. Chem. B
116
13682-13689
2012
Clostridium cochlearium
brenda
Wang, J.; Zhang, K.
Production of mesaconate in Escherichia coli by engineered glutamate mutase pathway
Metab. Eng.
30
190-196
2015
no activity in Escherichia coli, Clostridium tetanomorphum (Q05488 AND Q05509), Clostridium tetanomorphum, Clostridium tetanomorphum ATCC 15920 (Q05488 AND Q05509)
brenda