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L-threo-3-methylaspartate = L-glutamate
L-threo-3-methylaspartate = L-glutamate
the reaction is initiated through hydrogen atom abstraction from C-4 of Glu by 5'-deoxyadenosyl radical which is derived by homolysis of the Co-C sigma-bond of coenzyme B12
-
L-threo-3-methylaspartate = L-glutamate
requires Co(II) for coordiation of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product
-
L-threo-3-methylaspartate = L-glutamate
the 4-glutamyl radical is an intermediate in the carbon skeleton rearrangement catalyzed the enzyme
-
L-threo-3-methylaspartate = L-glutamate
the catalytic mechanism proceeds via a fragmentation/recombination sequence with intermediates stabilized by partial protonation/deprotonation
-
L-threo-3-methylaspartate = L-glutamate
kinetic study of deuterium effects, an isotopically insensitive step is partially rate-determining
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L-threo-3-methylaspartate = L-glutamate
kinetic study of tritium effects, reaction has a late transition state
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L-threo-3-methylaspartate = L-glutamate
no significant activation of coenzyme adenosylcobalamin in absence of substrate
-
L-threo-3-methylaspartate = L-glutamate
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals
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L-threo-3-methylaspartate = L-glutamate
motions of the 5-hydrogen atoms are coupled in the transition state to the motion of the hydrogen undergoing transfer, in a reaction that involves a large degree of quantum tunneling
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L-threo-3-methylaspartate = L-glutamate
conversion of glutamate to methylaspartate catalyzed by glutamate mutase is investigated by quantum mechanical/molecular mechanical simulations based on coupled cluster and density functional calculations, overview. Binding of the Glu substrate induces a homolytic cleavage of the cobalt-carbon bond of the cofactor, which yields a 5'-deoxyadenosyl radical and cob(II)alamin, atom tunneling mechanism
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L-threo-3-methylaspartate = L-glutamate
radical mechanism of the conversion of glutamate to methylaspartate catalyzed by glutamate mutase by quantum mechanical/molecular mechanical simulations based on density functional theory, crystal structure analysis
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5'-deoxyadenosylcobalamin
-
dependent on
adenosylcobalamin
-
adenosylcobalamin
-
enzyme is dependent on, KM for wild-type enzyme is 0.0055 mM
adenosylcobalamin
-
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
adenosylcobalamin
-
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
adenosylcobalamin
-
kinetics of homolysis and recombination, ultrafast spectroscopic experiments, no significant activation of coenzyme in absence of substrate
adenosylcobalamin
-
study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals
adenosylcobalamin
-
study of tritium isotope effects on homolysis of adenosylcobalamin
adenosylcobalamin
-
dependent on, binding structure, modeling, overview
Cobalamin
-
-
Cobalamin
-
requires Co(II) for coordination of the acrylate, in order to enable the addition of the radical fragment to the alpha-carbon of this intermediate, leading to the branched product
Cobalamin
-
the weakly associated subunits E and S combine to form the coenzyme binding site. Interactions between the protein and the adenosyl moiety do not serve to weaken the cobalt-carbon bond in the ground state, variation of the apparent Km-value for adenosylcobalamine with protein concentration. Km: 0.0055 mM in the reaction with L-Glu, Km: 0.0031 mM in the reaction with (2S,3S)-3-methylaspartate, genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment
Cobalamin
-
component S binds coenzyme B12
coenzyme B12
-
-
coenzyme B12
-
each of the two independent coenzyme B12 molecules is associated with a substrate-binding site
coenzyme B12
-
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
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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
Switzer, R.L.
Glutamate mutase
B12 (Dolphin, D. ed. ) Wiley, New York
2
289-305
1982
Clostridium cochlearium, Clostridium saccharobutyricum, Clostridium sp., Acetoanaerobium sticklandii, 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, Cereibacter sphaeroides, Rhodospirillum rubrum, Clostridium sp. SB4
-
brenda
Barker, H.A.
Coenzyme B12-dependent mutases causing carbon chain rearrangements
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
509-537
1972
Cereibacter sphaeroides, Clostridium cochlearium, Clostridium tetanomorphum, Rhodospirillum rubrum
-
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
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
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
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
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
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
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
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
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
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