Information on EC 5.4.3.6 - tyrosine 2,3-aminomutase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
5.4.3.6
-
RECOMMENDED NAME
GeneOntology No.
tyrosine 2,3-aminomutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
-
-
-
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, amino group
-
isomerization
-
-
-
-
isomerization
Q0VZ68
-
isomerization
B8ZV93
-
isomerization
B8ZV94
-
PATHWAY
KEGG Link
MetaCyc Link
Tyrosine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine 2,3-aminomutase
Requires ATP.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Aminomutase, tyrosine 2,3-
-
-
-
-
MxTAM
B8ZV94
-
TAM
Cupriavidus crocatus
-
-
Tyrosine alpha,beta-amino mutase
-
-
-
-
Tyrosine alpha,beta-mutase
-
-
-
-
tyrosine aminomutase
-
-
tyrosine aminomutase
Q0VZ68
-
tyrosine aminomutase
Cupriavidus crocatus
-
-
tyrosine aminomutase
B8ZV93
-
tyrosine aminomutase
B8ZV94
-
tyrosine aminomutase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9073-38-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Cupriavidus crocatus
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Q0VZ68
(R)-beta-tyrosine is incorporated into the chondramides produced by Chondromyces crocatus
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S)-amino-3-(4-hydroxyphenyl)propanoate
(3R)-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
beta-tyrosine racemase activity
-
r
L-3,4-dihydroxyphenylalanine
3-amino-3-(3,4-dihydroxyphenyl)propanoate
show the reaction diagram
-
-
-
?
L-3-chlorotyrosine
3-amino-3-(3-chloro-4-hydroxyphenyl)propanoate
show the reaction diagram
-
-
-
?
L-Tyr
3-Amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
-
i.e. beta-Tyr
-
L-Tyr
?
show the reaction diagram
-
formation of beta-Tyr which is the N-terminal amino acid of the antibiotic edeine
-
-
-
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
-
-
-
?
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
-
-
r
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
L-tyrosine
(4-hydroxyphenyl)prop-2-enoate + NH3
show the reaction diagram
-
ammonia lyase activity of tyrosine aminomutase
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
Q0VZ68
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
B8ZV93
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
B8ZV94
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
Chondromyces crocatus, Cupriavidus crocatus
-
-
preferred product
-
r
L-tyrosine
4-hydroxycinnamic acid
show the reaction diagram
Q0VZ68
-
-
-
?
L-tyrosine
(S)-beta-tyrosine
show the reaction diagram
-
-
-
-
r
L-tyrosine
(S)-beta-tyrosine
show the reaction diagram
-
-
preferred product
-
r
additional information
?
-
-
L-phenylalanine is no substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Tyr
?
show the reaction diagram
-
formation of beta-Tyr which is the N-terminal amino acid of the antibiotic edeine
-
-
-
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
Q0VZ68
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
B8ZV93
-
-
-
?
L-tyrosine
(R)-beta-tyrosine
show the reaction diagram
B8ZV94
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
methylideneimidazole-5-one
-
Mio cofactor, formed by the self-condensation of Ala152, Ser153, and Gly154
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
-
-
2-oxoglutarate
-
-
Cd2+
-
weak inhibition
Cu2+
-
strong inhibition
p-hydroxycinnamate
-
-
p-hydroxyphenylpyruvate
-
-
phenylhydrazine
-
-
phenylpyruvate
-
-
Semicarbazide
-
-
Zn2+
-
weak inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.54
-
L-3,4-dihydroxyphenylalanine
-
-
6.1
-
L-3-chlorotyrosine
-
-
0.0023
-
L-tyrosine
-
lyase activity
0.028
-
L-tyrosine
-
-
0.028
-
L-tyrosine
-
pH and temperature not specified in the publication
0.178
-
L-tyrosine
Q0VZ68
mutant CmdF_MIYMLV
0.377
-
L-tyrosine
Q0VZ68
wild-type enzme
0.377
-
L-tyrosine
Chondromyces crocatus, Cupriavidus crocatus
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0067
-
L-3,4-dihydroxyphenylalanine
-
-
0.0048
-
L-3-chlorotyrosine
-
-
0.0004
-
L-tyrosine
Q0VZ68
mutant CmdF_MIYMLV, product (R)-beta-tyrosine
0.0005
-
L-tyrosine
Q0VZ68
wild-type enzme, product para-hydroxycinnamic acid
0.0012
-
L-tyrosine
-
lyase activity
0.0013
-
L-tyrosine
Q0VZ68
mutant CmdF_MIYMLV, product para-hydroxycinnamic acid
0.0072
-
L-tyrosine
Q0VZ68
wild-type enzme, product (R)-beta-tyrosine
0.01
-
L-tyrosine
-
-
7000
-
L-tyrosine
Chondromyces crocatus, Cupriavidus crocatus
-
pH and temperature not specified in the publication
10000
-
L-tyrosine
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1900
-
L-tyrosine
Chondromyces crocatus, Cupriavidus crocatus
-
pH and temperature not specified in the publication
12450
36000
-
L-tyrosine
-
pH and temperature not specified in the publication
12450
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
11.6
-
(2S,3R)-3-(4-fluorophenyl)oxirane-2-carboxylate
-
-
3
-
(2S,3R)-3-(4-methoxyphenyl)oxirane-2-carboxylate
-
-
5.8
-
(2S,3R)-3-phenyloxirane-2-carboxylate
-
-
4.8
-
(3R)-3-ammonio-2,2-difluoro-3-(4-hydroxyphenyl)propanoate
-
-
5.3
-
(3R)-3-ammonio-2,2-difluoro-3-(4-methoxyphenyl)propanoate
-
-
7.3
-
(3R)-3-ammonio-2,2-difluoro-3-phenylpropanoate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00188
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.8
-
Q0VZ68
activity assay
8.8
-
B8ZV93
activity assay
8.8
-
B8ZV94
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
10.5
-
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q0VZ68
activity assay
30
-
B8ZV93
activity assay
30
-
B8ZV94
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32
39
-
active in this range
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 58100, SDS-PAGE
tetramer
-
crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
75% loss of activity after 24 h at room temperature
60
-
-
5 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable to freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, stable for at least 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
Q0VZ68
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
B8ZV93
purification is carried out by affinity chromatography with GST-Sepharose, the GST-tag is cleaved by using the PreScission protease
B8ZV94
Ni-NTA resin column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
-
recombinant tyrosine aminomutase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into a pGEX-derived plasmid for expression in Escherichia coli BL21DE3 cells
Q0VZ68
into the pCR2.1Topo and pJET1/blunt vector and subsequently into pGEX-6P-1 for expression in Escherichia coli BL21DE3 cells
B8ZV93
into the pJET1/blunt vector and subsequently into pGEX-6P-1 for expression in Escherichia coli BL21DE3 cells
B8ZV94
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli with His-tag
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C107F
-
inactive
C396S
Q0VZ68
single amino acid alteration
CmdF_DEL
Q0VZ68
position 275-288 deleted
CmdF_MIAQVTSA
Q0VZ68
position 399-406: EGGQYLAT substituted
CmdF_MIYMLV
Q0VZ68
position 62-67: LVPVMI substituted
CmdF_SAGREDH
Q0VZ68
position 427-433: NGSNQDV, substituted
CmdF_SANQEDH
Q0VZ68
position 427-433: NGSNQDV, substituted
CmdF_TFLSA
Q0VZ68
position 81-85: RSHAA, substituted
CmdF_YHLAT
Q0VZ68
position 81-85: RSHAA, substituted
F59Y
Q0VZ68
single amino acid alteration
G184R
Q0VZ68
single amino acid alteration
H93F
-
the mutation abolishes all enzymatic activity
K242R
Q0VZ68
single amino acid alteration
P377R
Q0VZ68
single amino acid alteration
C107F
Cupriavidus crocatus
-
inactive
H93F
Cupriavidus crocatus
-
the mutation abolishes all enzymatic activity
C107F
-
inactive
E71A
-
the mutant has a significant decrease in activity
H93F
-
the mutant has no activity with L-phenylalanine and L-tyrosine
H93F
-
the mutation abolishes all enzymatic 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