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
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b12-dependent
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cobiialamin
- tetanomorphum
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cobalt-carbon
- cochlearium
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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
5.4.99.1 methylaspartate mutaseAdvanced search results
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results (Engineering
Engineering on EC 5.4.99.1 - methylaspartate mutase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E171A
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turnover number for glutamate is reduced 27.6fold, KM-value is increased 1.1fold, Km-value for adenosylcobalamin is reduced 1.23fold
E171D
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turnover number for glutamate is reduced 1.8fold, KM-value is reduced 1.54fold, Km-value for adenosylcobalamin is reduced 2.7fold
E171N
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turnover number for glutamate is reduced 232fold, KM-value is increased by 1.8fold, Km-value for adenosylcobalamin is reduced 1.4fold
E171Q
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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
R100K
R100M
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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
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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
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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
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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
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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
additional information
R100K
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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
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mutation significantly impairs the ability of enzyme to catalyze the rearrangement of substrate radical to product radical
additional information
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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
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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
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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
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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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