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
-
adenosylcobalamin-dependent
-
homolysis
-
b12-dependent
-
cobiialamin
- tetanomorphum
-
cobalt-carbon
- cochlearium
-
s-glutamate
-
b12-binding
-
2s,3s-3-methylaspartate
- 5'-deoxyadenosine
-
corrin
-
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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Cofactor
Cofactor on EC 5.4.99.1 - methylaspartate mutase
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adenosylcobalamin
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enzyme is dependent on, KM for wild-type enzyme is 0.0055 mM
adenosylcobalamin
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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
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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
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kinetics of homolysis and recombination, ultrafast spectroscopic experiments, no significant activation of coenzyme in absence of substrate
adenosylcobalamin
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study of Co-C bond activation, cofactor/active site interactions give rise to a fairly uniform stabilization of the Co 3d orbitals
adenosylcobalamin
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study of tritium isotope effects on homolysis of adenosylcobalamin
adenosylcobalamin
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dependent on, binding structure, modeling, overview
Cobalamin
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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
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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
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coenzyme binding and catalysis is very sensitive to mutations at position 15
Cobalamin
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the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor
Cobalamin
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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
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and at least seven analogs containing bases other than dimethylbenzimidazolyl can serve as coenzymes
coenzyme B12
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each of the two independent coenzyme B12 molecules is associated with a substrate-binding site
coenzyme B12
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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
coenzyme B12
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the coenzyme B12-binding subunit traps the nucleotide moiety of coenzyme B12
coenzyme B12
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binds to subunit SanU with about 0.1 mol Co per mol SanU
coenzyme B12
adenosylcobalamin, the concentration of internal coenzyme B12 is crucial for the full activity of B12-dependent enzyme