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
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enediyne
- ammonia
- chromophore
- crocatus
- sativa
- lyases
-
chondromyces
-
stereochemistry
-
myxobacterium
-
enantioselectivity
-
isomerizes
- globisporus
-
peptidyl
-
prosthetic
-
chromoprotein
- taxus
-
enantiomeric
-
fluorinated
-
protein-tethered
-
fad-dependent
- depsipeptides
- acrylate
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pathway-specific
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toney
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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
5.4.3.6 tyrosine 2,3-aminomutaseAdvanced search results
results (
results (Engineering
Engineering on EC 5.4.3.6 - tyrosine 2,3-aminomutase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K113N/E114Q/F115L
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site-directed mutagenesis, substrate specificity compared to wild-type
M92E/N93D/T95A/T97I
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site-directed mutagenesis, substrate specificity compared to wild-type
N446K
N93D/T95A/T97I/G106A/A107C/A108S/H109S
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site-directed mutagenesis, substrate specificity compared to wild-type
T95A/T97I/H109S
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site-directed mutagenesis, substrate specificity compared to wild-type
Y125C
Y125C/N446K
Y125C/N446K/T95A/T97I/H109S
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site-directed mutagenesis, substrate specificity compared to wild-type
Y125C/N446K/T95A/T97I/H109S/F115L
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site-directed mutagenesis, almost inactive mutant
H93F
additional information
N446K
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site-directed mutagenesis, the mutant shows increased activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
N446K
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site-directed mutagenesis, the mutant shows increased activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme, the mutant activity is reduced at converting alpha-tyrosine to its beta-isomer and 4-coumarate (ratio 22:78) compared to the wild-type, the mutant binds alpha-phenylalanine about 9fold better than wild-type OsTAM, total turnover rate of the mutant for converting alpha-phenylalanine to both beta-phenylalanine and cinnamate is about 4fold greater than the wild-type OsTAM rate for making beta-phenylalanine and cinnamate. Mutation of Asn446 of OsTAM to a Lys residue creates an active site bearing the characteristic triad sequence ([aromatic amino acid]-Leu-Lys) conserved in all PALs and thus explains in part why N446K-OsTAM has increased PAL activity compared to wild-type OsTAM
Y125C
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site-directed mutagenesis, the mutant shows altered activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
Y125C
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site-directed mutagenesis, the mutant shows altered activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme, mutant activity is reduced at converting alpha-tyrosine to its beta-isomer and 4-coumarate (ratio 2:98) compared to the wild-type, the mutant binds alpha-phenylalanine about 9fold better than wild-type OsTAM, total turnover rate of the mutant for converting alpha-phenylalanine to both beta-phenylalanine and cinnamate is about 4fold greater than the wild-type OsTAM rate for making beta-phenylalanine and cinnamate
Y125C/N446K
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site-directed mutagenesis, inactive mutant with L-tyrosine, the mutant binds alpha-phenylalanine about 9fold better than wild-type OsTAM, the mutant converts alpha-phenylalanine to both beta-phenylalanine and cinnamate
Y125C/N446K
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site-directed mutagenesis, the mutant shows altered activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
H93F
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the mutant has no activity with L-phenylalanine and L-tyrosine
additional information
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homology modeling of wild-type enzyme OsTAM and OsTAM mutant enzymes using the phenylalanine aminomutase (PAM) structure from Taxus canadensis with PDB ID 3NZ4 as template. Exchanging the active residues of OsTAM, Y125C and N446K for those in a phenylalanine aminomutase Taxus canadensis PAM alters its substrate specificity from tyrosine to phenylalanine
additional information
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a point mutation in TAM1 eliminates beta-tyrosine production in cultivar Nipponbare, TILLING enzyme knockout mutant
