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
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homolysis
-
b12-dependent
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cobiialamin
- tetanomorphum
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cobalt-carbon
- cochlearium
-
s-glutamate
-
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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General Information
General Information on EC 5.4.99.1 - methylaspartate mutase
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metabolism
physiological function
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overexpression of glmS leads to a 4.9fold enhancement of intracellular vitamin B12 concentration
additional information
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glutamate mutase and methylaspartase are the first two enzymes in the methylaspartate pathway, overview
metabolism
Fusobacterium varium NCTC 10560 / ATCC 8501
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glutamate mutase and methylaspartase are the first two enzymes in the methylaspartate pathway, overview
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residue Glu117 and the arginine claw have a strong influence, and also residues Glu 214, Lys 322, Gln 147, Glu 330, Lys 326, and Met 294 play a catalytic role. The arginine claw keeps the intermediates in place and is probably responsible for the enantioselectivity. Glu 171 temporarily accepts a proton from the glutamyl radical intermediate and donates it back at the end of the reaction
additional information
identification of the reactivating factor of glutamate mutase, MutL. MutL regenerates glutamate mutase and releases inactive coenzyme from the inactive glutamate mutase-adenosylcobalamine complex. Reactivation of the spontaneous inactive mutase (mutase-X-Cbl) and inactive form B12 binding with mutase (mutase-CNCbl) in presence of ATP and coenzyme B12 by MutL
additional information
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identification of the reactivating factor of glutamate mutase, MutL. MutL regenerates glutamate mutase and releases inactive coenzyme from the inactive glutamate mutase-adenosylcobalamine complex. Reactivation of the spontaneous inactive mutase (mutase-X-Cbl) and inactive form B12 binding with mutase (mutase-CNCbl) in presence of ATP and coenzyme B12 by MutL
additional information
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identification of the reactivating factor of glutamate mutase, MutL. MutL regenerates glutamate mutase and releases inactive coenzyme from the inactive glutamate mutase-adenosylcobalamine complex. Reactivation of the spontaneous inactive mutase (mutase-X-Cbl) and inactive form B12 binding with mutase (mutase-CNCbl) in presence of ATP and coenzyme B12 by MutL
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