Information on EC 5.4.3.6 - tyrosine 2,3-aminomutase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
5.4.3.6
-
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RECOMMENDED NAME
GeneOntology No.
tyrosine 2,3-aminomutase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine = 3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular, amino group
-
isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Tyrosine metabolism
-
-
Biosynthesis of enediyne antibiotics
-
-
Biosynthesis of antibiotics
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine 2,3-aminomutase
Requires ATP.
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CAS REGISTRY NUMBER
COMMENTARY hide
9073-38-5
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cupriavidus crocatus
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
(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
L-tyrosine
(S)-beta-tyrosine
show the reaction diagram
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
L-tyrosine
4-hydroxycinnamic acid
show the reaction diagram
-
-
-
?
[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
show the reaction diagram
-
-
-
-
?
[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
show the reaction diagram
-
-
-
-
?
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
(R)-beta-tyrosine
show the reaction diagram
L-tyrosine
3-amino-3-(4-hydroxyphenyl)propanoate
show the reaction diagram
-
involved in the biosynthesis of the enediyne antitumor antibiotic C-1027
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
required
methylideneimidazole-5-one
-
Mio cofactor, formed by the self-condensation of Ala152, Ser153, and Gly154
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
pyruvate
-
-
Semicarbazide
-
-
Zn2+
-
weak inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.54
L-3,4-dihydroxyphenylalanine
-
-
6.1
L-3-chlorotyrosine
-
-
0.0023 - 0.377
L-tyrosine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067
L-3,4-dihydroxyphenylalanine
-
-
0.0048
L-3-chlorotyrosine
-
-
0.0004 - 10000
L-tyrosine
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1900 - 36000
L-tyrosine
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32 - 39
-
active in this range
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58100
-
x * 58100, SDS-PAGE
75000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 58100, SDS-PAGE
tetramer
-
crystallization data
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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
75% loss of activity after 24 h at room temperature
60
-
5 min, complete inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to freezing and thawing
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 3 months
-
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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 tyrosine aminomutase
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli with His-tag
-
gene cctam, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C107F
-
inactive
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
C107F
-
inactive
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
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.3.6)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)