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Information on EC 5.4.3.6 - tyrosine 2,3-aminomutase for references in articles please use BRENDA:EC5.4.3.6Word Map on EC 5.4.3.6
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The enzyme appears in viruses and cellular organisms
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L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
mechanism
-
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
-
-
-
-
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group transfer
-
-
intramolecular, amino group
-
isomerization
-
-
-
-
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Biosynthesis of enediyne antibiotics
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-
Biosynthesis of antibiotics
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-
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L-tyrosine 2,3-aminomutase
Requires ATP.
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Aminomutase, tyrosine 2,3-
-
-
-
-
Tyrosine alpha,beta-amino mutase
-
-
-
-
Tyrosine alpha,beta-mutase
-
-
-
-
TAM
-
-
TAM
Cupriavidus crocatus
-
-
tyrosine aminomutase
-
-
tyrosine aminomutase
Cupriavidus crocatus
-
-
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-
-
-
brenda
Cupriavidus crocatus
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
-
-
-
brenda
-
UniProt
brenda
-
-
-
brenda
gene cctam
-
-
brenda
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metabolism
(R)-beta-tyrosine is incorporated into the chondramides produced by Chondromyces crocatus
additional information
-
cryptic stereochemistry of the enzyme mechanism, structure-function relationship, detailed overview
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(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-Tyr
3-Amino-3-(4-hydroxyphenyl)propanoate
-
-
i.e. beta-Tyr
-
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
-
?
L-tyrosine
(R)-beta-tyrosine
L-tyrosine
(S)-beta-tyrosine
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
L-tyrosine
4-hydroxycinnamic acid
-
-
-
?
[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
-
-
-
-
?
additional information
?
-
L-tyrosine
(R)-beta-tyrosine
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
-
-
preferred product
-
r
L-tyrosine
(R)-beta-tyrosine
Cupriavidus crocatus
-
-
preferred product
-
r
L-tyrosine
(R)-beta-tyrosine
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
-
-
-
?
L-tyrosine
(S)-beta-tyrosine
-
-
-
-
r
L-tyrosine
(S)-beta-tyrosine
-
-
preferred product
-
r
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
-
-
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
-
-
r
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
additional information
?
-
-
L-phenylalanine is no substrate
-
-
-
additional information
?
-
Cupriavidus crocatus
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L-phenylalanine is no substrate
-
-
-
additional information
?
-
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L-phenylalanine is no substrate
-
-
-
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L-Tyr
?
-
formation of beta-Tyr which is the N-terminal amino acid of the antibiotic edeine
-
-
-
L-tyrosine
(R)-beta-tyrosine
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
L-tyrosine
(R)-beta-tyrosine
Q0VZ68
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
B8ZV93
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
B8ZV94
-
-
-
?
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methylideneimidazole-5-one
-
Mio cofactor, formed by the self-condensation of Ala152, Ser153, and Gly154
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(2S,3R)-3-(4-fluorophenyl)oxirane-2-carboxylate
-
-
(2S,3R)-3-(4-methoxyphenyl)oxirane-2-carboxylate
-
-
(2S,3R)-3-phenyloxirane-2-carboxylate
-
-
(3R)-3-ammonio-2,2-difluoro-3-(4-hydroxyphenyl)propanoate
-
-
(3R)-3-ammonio-2,2-difluoro-3-(4-methoxyphenyl)propanoate
-
-
(3R)-3-ammonio-2,2-difluoro-3-phenylpropanoate
-
-
p-hydroxyphenylpyruvate
-
-
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1.54
L-3,4-dihydroxyphenylalanine
-
-
6.1
L-3-chlorotyrosine
-
-
0.0023 - 0.377
L-tyrosine
0.0023
L-tyrosine
-
lyase activity
0.028
L-tyrosine
-
pH and temperature not specified in the publication
0.178
L-tyrosine
mutant CmdF_MIYMLV
0.377
L-tyrosine
wild-type enzme
0.377
L-tyrosine
-
pH and temperature not specified in the publication
0.377
L-tyrosine
Cupriavidus crocatus
-
pH and temperature not specified in the publication
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0.0067
L-3,4-dihydroxyphenylalanine
-
-
0.0048
L-3-chlorotyrosine
-
-
0.0004 - 10000
L-tyrosine
0.0004
L-tyrosine
mutant CmdF_MIYMLV, product (R)-beta-tyrosine
0.0005
L-tyrosine
wild-type enzme, product para-hydroxycinnamic acid
0.0012
L-tyrosine
-
lyase activity
0.0013
L-tyrosine
mutant CmdF_MIYMLV, product para-hydroxycinnamic acid
0.0072
L-tyrosine
wild-type enzme, product (R)-beta-tyrosine
7000
L-tyrosine
-
pH and temperature not specified in the publication
7000
L-tyrosine
Cupriavidus crocatus
-
pH and temperature not specified in the publication
10000
L-tyrosine
-
pH and temperature not specified in the publication
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1900
L-tyrosine
-
pH and temperature not specified in the publication
1900
L-tyrosine
Cupriavidus crocatus
-
pH and temperature not specified in the publication
36000
L-tyrosine
-
pH and temperature not specified in the publication
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11.6
(2S,3R)-3-(4-fluorophenyl)oxirane-2-carboxylate
Streptomyces globisporus
-
-
3
(2S,3R)-3-(4-methoxyphenyl)oxirane-2-carboxylate
Streptomyces globisporus
-
-
5.8
(2S,3R)-3-phenyloxirane-2-carboxylate
Streptomyces globisporus
-
-
4.8
(3R)-3-ammonio-2,2-difluoro-3-(4-hydroxyphenyl)propanoate
Streptomyces globisporus
-
-
5.3
(3R)-3-ammonio-2,2-difluoro-3-(4-methoxyphenyl)propanoate
Streptomyces globisporus
-
-
7.3
(3R)-3-ammonio-2,2-difluoro-3-phenylpropanoate
Streptomyces globisporus
-
-
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8.5
-
-
8.8
activity assay
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6.5 - 10.5
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approx. 50% of maximal activity at pH 7.5 and pH 10.0, respectively
8 - 9
-
about 10% of maximal activity at pH 8 and 9
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30
activity assay
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32 - 39
-
active in this range
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58100
-
x * 58100, SDS-PAGE
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tetramer
-
crystallization data
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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
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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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22
-
75% loss of activity after 24 h at room temperature
60
-
5 min, complete inactivation
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stable to freezing and thawing
-
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-20°C, stable for at least 3 months
-
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Ni-NTA resin column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
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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 tyrosine aminomutase
-
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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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
-
expression in Escherichia coli with His-tag
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gene cctam, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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
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C396S
single amino acid alteration
CmdF_DEL
position 275-288 deleted
CmdF_MIAQVTSA
position 399-406: EGGQYLAT substituted
CmdF_MIYMLV
position 62-67: LVPVMI substituted
CmdF_SAGREDH
position 427-433: NGSNQDV, substituted
CmdF_SANQEDH
position 427-433: NGSNQDV, substituted
CmdF_TFLSA
position 81-85: RSHAA, substituted
CmdF_YHLAT
position 81-85: RSHAA, substituted
F59Y
single amino acid alteration
G184R
single amino acid alteration
H93F
-
the mutation abolishes all enzymatic activity
K242R
single amino acid alteration
P377R
single amino acid alteration
C107F
Cupriavidus crocatus
-
inactive
H93F
Cupriavidus crocatus
-
the mutation abolishes all enzymatic activity
E71A
-
the mutant has a significant decrease in activity
S153A
-
1.5% of wild-type activity
S153C
-
5% of wild-type activity
Y415F/H93
-
the mutant has no activity with L-phenylalanine
Y63F
-
completely inactive
H93F
-
the mutant has no activity with L-phenylalanine and L-tyrosine
H93F
-
the mutation abolishes all enzymatic activity
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TALY_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
533
56163
Swiss-Prot
TAM_MYXFU
526
56959
Swiss-Prot
TAM_MYXSM
Myxococcus sp. (strain Mx-B0)
526
56946
Swiss-Prot
TAM_CHOCO
531
56901
Swiss-Prot
TAM_STRGL
539
58139
Swiss-Prot
A0A2X2SKF7_CAPOC
502
56804
TrEMBL
A0A2X2RIK4_CAPOC
502
56855
TrEMBL
A0A1Y5S8G3_9PROT
482
50357
TrEMBL
A0A1D3UH35_TANFO
515
57871
TrEMBL
A0A0P9G876_9GAMM
514
56549
TrEMBL
A0A1V6IPR8_9DELT
517
56088
TrEMBL
A0A1A7KIK4_9FLAO
506
57070
TrEMBL
A0A0B7D3J3_PSEFL
514
56189
TrEMBL
A0A1V5VTD6_9BACT
512
57165
TrEMBL
A0A1V6BZF2_9SPIR
529
58541
TrEMBL
A0A1R3TAE5_9BACT
514
57450
TrEMBL
A0A173WBR7_9BACT
507
55706
TrEMBL
A0A143B7K2_9DELT
530
57613
TrEMBL
A0A1V6BGQ2_9BACT
515
57647
TrEMBL
U5Q5U8_9BACT
505
56583
TrEMBL
A0A125A050_9PSED
514
56080
TrEMBL
A0A1V6BV20_9BACT
509
56708
TrEMBL
A0A0X8X295_9SPHI
516
57990
TrEMBL
A0A2N9P793_9FLAO
505
56455
TrEMBL
A0A221UXT3_9FLAO
518
58322
TrEMBL
A0A2K9JY89_9GAMM
539
59590
TrEMBL
A0A0S4HTM4_9PSED
514
56288
TrEMBL
A0A221W599_9PSEU
534
57344
TrEMBL
A0A1V5TXV8_9BACT
279
31548
TrEMBL
A0A1V5D6K1_9DELT
560
61027
TrEMBL
A0A0S4S597_CAMFE
223
23687
TrEMBL
A0A136KLF5_9BACT
508
55401
TrEMBL
A0A174GDV1_BACVU
523
59094
TrEMBL
A0A2X3ZVL3_PAULE
515
56338
TrEMBL
A0A2N7RDU4_9PSED
514
56332
TrEMBL
A0A075UT61_9PSEU
543
58462
TrEMBL
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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
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