5.4.99.1: methylaspartate mutase
This is an abbreviated version!
For detailed information about methylaspartate mutase, go to the full flat file.
Word Map on EC 5.4.99.1
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5.4.99.1
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adenosylcobalamin
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adenosylcobalamin-dependent
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homolysis
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b12-dependent
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cobiialamin
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tetanomorphum
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cobalt-carbon
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cochlearium
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s-glutamate
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b12-binding
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2s,3s-3-methylaspartate
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5'-deoxyadenosine
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corrin
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adenosyl
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cobalamin-binding
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cobalamin-dependent
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methylmalonyl
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isomerizations
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mutases
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5\'-deoxyadenosyl
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2-methyleneglutarate
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mesaconate
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dimethylbenzimidazole
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synthesis
- 5.4.99.1
- adenosylcobalamin
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adenosylcobalamin-dependent
-
homolysis
-
b12-dependent
-
cobiialamin
- tetanomorphum
-
cobalt-carbon
- cochlearium
-
s-glutamate
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b12-binding
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2s,3s-3-methylaspartate
- 5'-deoxyadenosine
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corrin
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adenosyl
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cobalamin-binding
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cobalamin-dependent
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methylmalonyl
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isomerizations
- mutases
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5\'-deoxyadenosyl
- 2-methyleneglutarate
- mesaconate
- dimethylbenzimidazole
- synthesis
Reaction
Synonyms
AdoCbl-dependent glutamate mutase, Glm, GlmS, Glutamate isomerase, Glutamate mutase, Glutamic acid isomerase, Glutamic acid mutase, Glutamic isomerase, Glutamic mutase, Methylaspartic acid mutase, Mutase, methylaspartate, mutE, mutS, SanU, SanV
ECTree
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Reaction
Reaction on EC 5.4.99.1 - methylaspartate mutase
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L-threo-3-methylaspartate = L-glutamate
hydrogen transfer occurs directly between coenzyme and product and provides no evidence for the formation of a protein radical
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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
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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
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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
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L-threo-3-methylaspartate = L-glutamate
the 4-glutamyl radical is an intermediate in the carbon skeleton rearrangement catalyzed the enzyme
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L-threo-3-methylaspartate = L-glutamate
the catalytic mechanism proceeds via a fragmentation/recombination sequence with intermediates stabilized by partial protonation/deprotonation
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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
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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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