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Information on EC 5.4.3.6 - tyrosine 2,3-aminomutase
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5.4.3.6 tyrosine 2,3-aminomutaseIUBMB Comments
Requires ATP.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
sgcc4, tyrosine aminomutase, l-tyrosine 2,3-aminomutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aminomutase, tyrosine 2,3-
-
-
-
-
TAM
Tyrosine alpha,beta-amino mutase
-
-
-
-
Tyrosine alpha,beta-mutase
-
-
-
-
tyrosine aminomutase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
-
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, amino group
-
isomerization
isomerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine 2,3-aminomutase
Requires ATP.
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CAS REGISTRY NUMBER
COMMENTARY
9073-38-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S)-amino-3-(4-hydroxyphenyl)propanoate
(3R)-amino-3-(4-hydroxyphenyl)propanoate
-
beta-tyrosine racemase activity
-
r
L-3,4-dihydroxyphenylalanine
3-amino-3-(3,4-dihydroxyphenyl)propanoate
-
-
-
?
L-3-chlorotyrosine
3-amino-3-(3-chloro-4-hydroxyphenyl)propanoate
-
-
-
?
L-phenylalanine
L-beta-phenylalanine
-
3% relative to the activity with L-tyrosine of wild-type enzyme
-
-
?
L-Tyr
?
-
formation of beta-Tyr which is the N-terminal amino acid of the antibiotic edeine
-
-
-
L-tyrosine
(4-hydroxyphenyl)prop-2-enoate + NH3
-
ammonia lyase activity of tyrosine aminomutase
-
?
[3-deutero]-(2S,3R)-alpha-tyrosine
[3-deutero]-(2S,3S)-4'-O,2-N-di((S)-2-methylbutanoic acid)-alpha-tyrosine methyl ester + [3-deutero]-(2S,3R)-4'-O,2-N-di((S)-2-methylbutanoic acid)-alpha-tyrosine methyl ester
-
-
-
-
?
[3-deutero]-(2S,3S)-alpha-tyrosine
[3-deutero]-(2S,3S)-4'-O,2-N-di((S)-2-methylbutanoic acid)-alpha-tyrosine methyl ester + ([3-deutero]-(2S,3R)-4'-O,2-N-di((S)-2-methylbutanoic acid)-alpha-tyrosine methyl ester
-
-
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
the enzyme isomerizes (S)-alpha-tyrosine to (R)-beta-tyrosine and is stereoselective for (R)-beta-tyrosine (85%), but also forms the (S)-beta-tyrosine enantiomer (15%) through inversion of configuration at both migration termini
-
-
r
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
Oryza sativa enzyme OsTAM makes 75% beta-tyrosine and 25% 4-coumarate from alpha-tyrosine
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
wild-type OsTAM from Oryza sativa preferentially isomerizes (2S)-alpha-tyrosine to (3R)-beta-tyrosine with an enantioselectivity (94% ee)
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
additional information
?
-
-
substrate specificity of recombinant wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
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. Autocatalysis of the 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) cofactor through cyclization of (A/T/S)-Ser-Gly residues within the active site
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Tyr
?
-
formation of beta-Tyr which is the N-terminal amino acid of the antibiotic edeine
-
-
-
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
Oryza sativa enzyme OsTAM makes 75% beta-tyrosine and 25% 4-coumarate from alpha-tyrosine
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methylideneimidazole-5-one
-
Mio cofactor, formed by the self-condensation of Ala152, Ser153, and Gly154
3,5-dihydro-5-methylidene-4H-imidazol-4-one
-
i.e. MIO, dependent on. The MIO group is formed by condensation and cyclization of backbone residues of an (A, T, or S)-Ser-Gly triad in the active site. The MIO 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
3,5-dihydro-5-methylidene-4H-imidazol-4-one
-
i.e. MIO, dependent on. The MIO group is formed by condensation and cyclization of backbone residues of an (A, T, or S)-Ser-Gly triad in the active site. The MIO 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. Autocatalysis of the 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) cofactor through cyclization of (A/T/S)-Ser-Gly residues within the active site, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
hemipteran and lepidopteran herbivores show no negative effects at physiologically relevant beta-tyrosine concentrations
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.49
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C/N446K
0.72
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant N446K
9
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant wild-type enzyme
0.028
L-tyrosine
-
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000035
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C
0.000052
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C/N446K
0.00008
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant N446K
0.00016
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant wild-type enzyme
0.0005
L-tyrosine
wild-type enzme, product para-hydroxycinnamic acid
0.0013
L-tyrosine
mutant CmdF_MIYMLV, product para-hydroxycinnamic acid
10000
L-tyrosine
-
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000018
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant wild-type enzyme
0.000035
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C
0.00011
L-phenylalanine
-
alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant N446K; alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C/N446K
36000
L-tyrosine
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10.5
-
approx. 50% of maximal activity at pH 7.5 and pH 10.0, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
(R)-beta-tyrosine occurs in the seeds, leaves, roots, and root exudates of the Nipponbare cultivar. Dry rice seeds from plants that have not been elicited with jasmonic acid also contain significant amounts of beta-tyrosine. When rice seedlings are grown hydroponically, beta-tyrosine is secreted into the medium
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
MIO-dependent aminomutases belong to a class I lyase-like family, in which the MIO group is formed by condensation and cyclization of backbone residues of an (A, T, or S)-Ser-Gly triad in the active site. The active sites of rice tyrosine aminomutase and Taxus canadensis phenylalanine aminomutase share a high degree of sequence identity, which may in part explain why OsTAM also converts phenylalanine to beta-phenylalanine
malfunction
-
rice cultivars that do not produce beta-tyrosine have a chromosome 12 deletion that encompasses TAM1
metabolism
(R)-beta-tyrosine is incorporated into the chondramides produced by Chondromyces crocatus
physiological function
additional information
physiological function
-
MIO (3,5-dihydro-5-methylidene-4H-imidazol-4-one)-dependent aminomutases (AMs) are involved in the the biosynthetic pathways of biologically active, medicinal compounds in plants and microorganisms
physiological function
-
tyrosine aminomutase TAM1 is required for beta-tyrosine biosynthesis in Oryza sativa, the tyrosine aminomutase converts the common protein amino acid tyrosine (alpha-tyrosine) into beta-tyrosine. beta-Tyrosine is most prevalent in temperate japonica cultivars. beta-Tyrosine is exuded into hydroponic medium at higher concentrations and may contribute to the allelopathic potential of rice. Pseudomonas syringae growth is inhibited by beta-tyrosine, and seedlings of dicot species are much more sensitive to exogenous beta-tyrosine than rice and other tested monocots
additional information
-
cryptic stereochemistry of the enzyme mechanism, structure-function relationship, detailed overview
additional information
-
residues Y125 and N446 not only play a central role in substrate selectivity but, in part, also set the intrinsic reactivity of OsTAM
additional information
-
homology modeling of wild-type enzyme OsTAM and OsTAM mutant enzymes using the phenylalanine aminomutase structure from Taxus canadensis with PDB ID 3NZ4 as template. The active site of enzyme TAM has a flexible inner loop region
additional information
-
hemipteran and lepidopteran herbivores show no negative effects at physiologically relevant beta-tyrosine concentrations
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
TALY_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
533
0
56163
Swiss-Prot
A0A1V6IPR8_9DELT
517
0
56088
TrEMBL
A0A0S4S597_CAMFE
223
0
23687
TrEMBL
A0A1V5TXV8_9BACT
279
0
31548
TrEMBL
A0A1V6J5E7_9BACT
509
0
56481
TrEMBL
A0A1V6BZF2_9SPIR
529
0
58541
TrEMBL
A0A1R3TAE5_9BACT
514
0
57450
TrEMBL
A0A1V5D6K1_9DELT
560
0
61027
TrEMBL
A0A1V5VTD6_9BACT
512
0
57165
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
mutant enzyme E71A using 100 mM trimethylamine N-oxide, 4.6 M sodium formate, at 4°C, and mutant enzyme Y63F using 95 mM trimethylamine N-oxide, 4.6 M sodium formate with 2 mM L-tyrosine, at 20°C
-
refined to 2.5 A resolution. Enzyme has a closed active site well suited to retain ammonia and minimize the formation of lyase elimination products
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K113N/E114Q/F115L
-
site-directed mutagenesis, substrate specificity compared to wild-type
M92E/N93D/T95A/T97I
-
site-directed mutagenesis, substrate specificity compared to wild-type
N446K
N93D/T95A/T97I/G106A/A107C/A108S/H109S
-
site-directed mutagenesis, substrate specificity compared to wild-type
T95A/T97I/H109S
-
site-directed mutagenesis, substrate specificity compared to wild-type
Y125C
Y125C/N446K
Y125C/N446K/T95A/T97I/H109S
-
site-directed mutagenesis, substrate specificity compared to wild-type
Y125C/N446K/T95A/T97I/H109S/F115L
-
site-directed mutagenesis, almost inactive mutant
H93F
additional information
N446K
-
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
N446K
-
site-directed mutagenesis, the mutant shows increased activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
Y125C
-
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
-
site-directed mutagenesis, the mutant shows altered activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
Y125C/N446K
-
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
-
site-directed mutagenesis, the mutant shows altered activity with phenylalanine and halogenated phenylalanine substrates compared to the wild-type enzyme
H93F
-
the mutant has no activity with L-phenylalanine and L-tyrosine
additional information
-
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
-
a point mutation in TAM1 eliminates beta-tyrosine production in cultivar Nipponbare, TILLING enzyme knockout mutant
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
-
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
-
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene cctam, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene TAM1, gene mapping to chromosome 12, transient expression in Nicotiana benthamiana
-
into a pGEX-derived plasmid for expression in Escherichia coli BL21DE3 cells
into the pCR2.1Topo and pJET1/blunt vector and subsequently into pGEX-6P-1 for expression in Escherichia coli BL21DE3 cells
into the pJET1/blunt vector and subsequently into pGEX-6P-1 for expression in Escherichia coli BL21DE3 cells
sequence comparisons, recombinant expression of His-tagged wild-type and mutant enzymes
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
beta-tyrosine accumulation is induced by the plant defense signaling molecule jasmonic acid, jasmonic acid treatment of the seedlings increases beta-tyrosine content in the leaves, roots, and imbibed seed material.
-
hemipteran and lepidopteran herbivores show no negative effects at physiologically relevant beta-tyrosine concentrations
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurylo-Borowska, Z.; Abramsky, T.
Biosynthesis of beta-tyrosine
Biochim. Biophys. Acta
264
1-10
1972
Brevibacillus brevis
brenda
Parry, R.J.; Kurylo-Borowska, Z.
Biosynthesis of amino acids. Investigation of the mechanism of beta-tyrosine formation
J. Am. Chem. Soc.
102
836-837
1980
Brevibacillus brevis
-
brenda
Christenson, S.D.; Wu, W.; Spies, M.A.; Shen, B.; Toney, M.D.
Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis
Biochemistry
42
12708-12718
2003
Streptomyces globisporus
brenda
Christianson, C.V.; Montavon, T.J.; Van Lanen, S.G.; Shen, B.; Bruner, S.D.
The structure of L-tyrosine 2,3-aminomutase from the C-1027 enediyne antitumor antibiotic biosynthetic pathway
Biochemistry
46
7205-7214
2007
Streptomyces globisporus
brenda
Montavon, T.J.; Christianson, C.V.; Festin, G.M.; Shen, B.; Bruner, S.D.
Design and characterization of mechanism-based inhibitors for the tyrosine aminomutase SgTAM
Bioorg. Med. Chem. Lett.
18
3099-3102
2008
Streptomyces globisporus
brenda
Krug, D.; Mueller, R.
Discovery of additional members of the tyrosine aminomutase enzyme family and the mutational analysis of CmdF
ChemBioChem
10
741-750
2009
Chondromyces crocatus, Chondromyces crocatus (Q0VZ68), Myxococcus fulvus Mx f65 (B8ZV93), Myxococcus sp. Mx-B0 (B8ZV94)
brenda
Cooke, H.A.; Bruner, S.D.
Probing the active site of MIO-dependent aminomutases, key catalysts in the biosynthesis of beta-amino acids incorporated in secondary metabolites
Biopolymers
93
802-810
2010
Streptomyces globisporus
brenda
Wu, B.; Szymanski, W.; Wijma, H.J.; Crismaru, C.G.; de Wildeman, S.; Poelarends, G.J.; Feringa, B.L.; Janssen, D.B.
Engineering of an enantioselective tyrosine aminomutase by mutation of a single active site residue in phenylalanine aminomutase
Chem. Commun. (Camb. )
46
8157-8159
2010
Chondromyces crocatus, Cupriavidus crocatus, Streptomyces globisporus
brenda
Wanninayake, U.; Walker, K.D.
A bacterial tyrosine aminomutase proceeds through retention or inversion of stereochemistry to catalyze its isomerization reaction
J. Am. Chem. Soc.
135
11193-11204
2013
Chondromyces crocatus
brenda
Walter, T.; Wijewardena, D.; Walker, K.
Mutation of aryl binding pocket residues results in an unexpected activity switch in an Oryza sativa tyrosine aminomutase
Biochemistry
55
3497-3503
2016
Oryza sativa
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Attanayake, G.; Walter, T.; Walker, K.D.
Understanding which residues of the active site and loop structure of a tyrosine aminomutase define its mutase and lyase activities
Biochemistry
57
3503-3514
2018
Oryza sativa
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Yan, J.; Aboshi, T.; Teraishi, M.; Strickler, S.R.; Spindel, J.E.; Tung, C.W.; Takata, R.; Matsumoto, F.; Maesaka, Y.; McCouch, S.R.; Okumoto, Y.; Mori, N.; Jander, G.
The tyrosine aminomutase TAM1 is required for beta-tyrosine biosynthesis in rice
Plant Cell
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1265-1278
2015
Oryza sativa Japonica Group
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