5.4.3.6: tyrosine 2,3-aminomutase
This is an abbreviated version!
For detailed information about tyrosine 2,3-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.6
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5.4.3.6
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enediyne
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ammonia
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chromophore
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crocatus
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sativa
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lyases
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chondromyces
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stereochemistry
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myxobacterium
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enantioselectivity
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isomerizes
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globisporus
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peptidyl
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prosthetic
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chromoprotein
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taxus
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enantiomeric
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fluorinated
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protein-tethered
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fad-dependent
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depsipeptides
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acrylate
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pathway-specific
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toney
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lyase-like
- 5.4.3.6
-
enediyne
- ammonia
- chromophore
- crocatus
- sativa
- lyases
-
chondromyces
-
stereochemistry
-
myxobacterium
-
enantioselectivity
-
isomerizes
- globisporus
-
peptidyl
-
prosthetic
-
chromoprotein
- taxus
-
enantiomeric
-
fluorinated
-
protein-tethered
-
fad-dependent
- depsipeptides
- acrylate
-
pathway-specific
-
toney
-
lyase-like
Reaction
Synonyms
3,5-dihydro-5-methylidene-4H-imidazol-4-one-dependent aminomutase, 3,5-dihydro-5-methylidine-4H-imidazol-4-one-dependent tyrosine aminomutase, Aminomutase, tyrosine 2,3-, CmdF, MfTAM, MIO-dependent aminomutase, MIO-dependent tyrosine aminomutase, More, MxTAM, OsTAM, SgcC4, TAM, Tam1, Tyrosine alpha,beta-amino mutase, Tyrosine alpha,beta-mutase, tyrosine aminomutase
ECTree
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Reaction
Reaction on EC 5.4.3.6 - tyrosine 2,3-aminomutase
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L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
pH-dependent stereochemic mechanism, detailed overview. The enzyme uses a retention-of-configuration mechanism at the amino migration terminus
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L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
MIO (3,5-dihydro-5-methylidene-4H-imidazol-4-one)-dependent aminomutases begin their reactions by adding the amino group of the substrate to the methylidene carbon of the MIO prosthesis. The enzyme removes the NH2/H pair from the substrate, yielding an NH2-MIO adduct, a tightly bound acrylate intermediate, and protonated catalytic Tyr
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L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
the 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) group in the enzyme's active site N-alkylates the NH2 of the alpha-amino acid substrates and promotes the removal of an intermediary NH2-MIO adduct. Concomitant removal of a beta-proton from the substrate (NH2-MIO adduct) by a catalytic tyrosine yields an acrylate intermediate. The aminomutase reaction continues by vicinal reprotonation and reamination at the alpha- and beta-carbons, respectively, of the acrylate to produce the beta-amino acid. Mechanism of MIO-dependent aminomutase, overview
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