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Information on EC 2.6.1.77 - taurine-pyruvate aminotransferase
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EC Tree
2.6.1.77 taurine-pyruvate aminotransferaseIUBMB Comments
The enzyme from the bacterium Bilophila wadsworthia requires pyridoxal 5'-phosphate as a cofactor, and catalyses a reversible reaction that starts an anaerobic taurine degradation pathway. beta-Alanine is also a significant amino group donor. The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyses to sulfite and acetaldehyde. Unlike, EC 2.6.1.55, taurine---2-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.
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Word Map
- 2.6.1.77
- sulfoacetaldehyde
-
2-aminoethanesulfonate
- sulfur
- sulfonate
-
bilophila
- wadsworthia
-
transamination
- sulfite
- cysteate
- sulfoacetate
-
paracoccus
-
desulfonation
-
deamination
-
rhodobacter
- isethionate
- acetaldehyde
-
organosulfonate
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
taurine:pyruvate aminotransferase, taurine-pyruvate aminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, taurine-pyruvate
-
-
-
-
HPA
hypotaurine-inducible hypotaurine:pyruvate aminotransferase
Pden_4273
taurine transaminase
taurine:pyruvate aminotransferase
tPA
hypotaurine-inducible hypotaurine:pyruvate aminotransferase
-
hypotaurine-inducible hypotaurine:pyruvate aminotransferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
-
-
-
-
taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
first step
-
-
-
taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde
The enzyme from Bilophila wadsworthia requires pryidoxal 5'-phosphate as a cofactor, is reversible, and catalyses the first step of anaerobic taurine degradation. Hypotaurine (i.e. 2-aminoethanesulfinate) and beta-alanine are also significant donors of an amino group. Unlike, EC 2.6.1.55, taurine-2-oxoglutarate transaminase, 2-oxoglutarate is not an acceptor of amino groups
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transamination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
taurine:pyruvate aminotransferase
The enzyme from the bacterium Bilophila wadsworthia requires pyridoxal 5'-phosphate as a cofactor, and catalyses a reversible reaction that starts an anaerobic taurine degradation pathway. beta-Alanine is also a significant amino group donor. The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyses to sulfite and acetaldehyde. Unlike, EC 2.6.1.55, taurine---2-oxoglutarate transaminase, 2-oxoglutarate cannot serve as an acceptor for the amino group.
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CAS REGISTRY NUMBER
COMMENTARY
51901-18-9
-
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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
taurine + 2-oxobutyrate
2-sulfoacetaldehyde + 2-aminobutyrate
-
-
?
taurine + glycolaldehyde
2-sulfoacetaldehyde + ?
-
-
-
?
taurine + glyoxylate
2-sulfoacetaldehyde + glycine
-
-
-
?
taurine + hexanal
2-sulfoacetaldehyde + hexyl-1-amine
-
-
-
?
taurine + methanal
2-sulfoacetaldehyde + methylamine
-
-
-
?
taurine + pentanal
2-sulfoacetaldehyde + pentylamine
-
-
-
?
taurine + propanal
2-sulfoacetaldehyde + propyl-1-amine
-
-
-
?
(S)-1-methylbenzylamine + pyruvate
acetophenone + L-alanine
no substrate: (R)-enantiomer
-
-
?
(S)-1-methylbenzylamine + pyruvate
acetophenone + L-alanine
no substrate: (R)-enantiomer
-
-
?
1,4-diaminobutane + pyruvate
? + L-alanine
-
3.1% of activity with taurine
-
-
?
1,4-diaminobutane + pyruvate
? + L-alanine
-
3.1% of activity with taurine
-
-
?
1,6-diaminohexane + pyruvate
? + L-alanine
-
2.6% of activity with taurine
-
-
?
1,6-diaminohexane + pyruvate
? + L-alanine
-
2.6% of activity with taurine
-
-
?
1,7-diaminoheptane + pyruvate
? + L-alanine
-
2.1% of activity with taurine
-
-
?
1-amylamine + pyruvate
pentanaldehyde + L-alanine
-
low activity
-
-
?
1-amylamine + pyruvate
pentanaldehyde + L-alanine
-
8.1% of activity with taurine
-
-
?
1-butylamine + pyruvate
4-aminobutyraldehyde + L-alanine
-
low activity
-
-
?
1-butylamine + pyruvate
4-aminobutyraldehyde + L-alanine
-
12% of activity with taurine
-
-
?
beta-alanine + pyruvate
3-oxopropanoate + L-alanine
-
best substrate
-
-
?
beta-alanine + pyruvate
3-oxopropanoate + L-alanine
-
best substrate
-
-
?
hypotaurine + pyruvate
2-aminoethanesulfinic acid + L-alanine
-
product 2-aminoethanesulfinic acid desulfinates spontaneously to acetaldehyde and sulfite
-
?
hypotaurine + pyruvate
2-aminoethanesulfinic acid + L-alanine
-
product 2-aminoethanesulfinic acid desulfinates spontaneously to acetaldehyde and sulfite
-
?
hypotaurine + pyruvate
?
i.e. 2-aminoethanesulfinate
-
-
?
spermidine + pyruvate
? + L-alanine
-
4.7% of activity with taurine
-
-
?
spermine + pyruvate
? + L-alanine
-
4.2% of activity with taurine
-
-
?
taurine + 2-oxobutanoate
2-sulfoacetaldehyde + 2-aminobutanoate
about 50% of the activity with taurine
product 2-sulfoacetaldehyde desulfinates spontaneously to acetaldehyde and sulfite
-
?
taurine + 2-oxobutanoate
2-sulfoacetaldehyde + 2-aminobutanoate
about 50% of the activity with taurine
product 2-sulfoacetaldehyde desulfinates spontaneously to acetaldehyde and sulfite
-
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
-
less active compared to pyruvate
-
-
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
-
56% of activity with pyruvate
-
-
?
taurine + butanal
2-sulfoacetaldehyde + butyl-1-amine
-
-
-
?
taurine + butanal
2-sulfoacetaldehyde + butyl-1-amine
-
-
-
?
taurine + ethanal
2-sulfoacetaldehyde + ethylamine
-
-
-
?
taurine + ethanal
2-sulfoacetaldehyde + ethylamine
-
-
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
best substrates
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
i.e. 2-aminoethanesulfonate
-
r
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
i.e. 2-aminoethanesulfonate
-
r
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
-
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
specific for taurine
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
i.e. 2-aminoethanesulfonate
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
specific for taurine
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
i.e. 2-aminoethanesulfonate
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
-
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
-
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
-
-
-
?
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
involved in taurine catabolism
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
essential for growth on taurine
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
essential for growth on taurine
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
best substrate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
best substrate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
i.e. 2-aminoethanesulfonate
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in the desulfonation pathway dissimilating taurine
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
i.e. 2-aminoethanesulfonate
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
enzyme is involved in the desulfonation pathway dissimilating taurine, overview, homeostatic mechanism
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
i.e. 2-aminoethanesulfonate
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
enzyme is involved in the desulfonation pathway dissimilating taurine, overview, homeostatic mechanism
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
best substrate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
best substrate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
sulfoacetaldehyde + L-alanine
-
inducible enzyme
-
-
?
additional information
?
-
no activity with 2-oxoglutarate and phenylpyruvate as amino group acceptor
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate and phenylpyruvate as amino group acceptor
-
-
?
additional information
?
-
cysteate, glutamate and 2-aminoethanephosphonate are poor amino group donor substrates
-
-
?
additional information
?
-
-
cysteate, glutamate and 2-aminoethanephosphonate are poor amino group donor substrates
-
-
?
additional information
?
-
no activity with 2-oxoglutarate and phenylpyruvate as amino group acceptor
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate and phenylpyruvate as amino group acceptor
-
-
?
additional information
?
-
cysteate, glutamate and 2-aminoethanephosphonate are poor amino group donor substrates
-
-
?
additional information
?
-
-
cysteate, glutamate and 2-aminoethanephosphonate are poor amino group donor substrates
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
-
-
?
additional information
?
-
the enzyme displays broad donor and acceptor ranges for unnatural substrates, with relatively good activity toward ketoses. Enzyme shows a unique mechanism of sulfonate/alpha-carboxylate recognition contributed by Arg163 and Gln160
-
-
?
additional information
?
-
the enzyme displays broad donor and acceptor ranges for unnatural substrates, with relatively good activity toward ketoses. Enzyme shows a unique mechanism of sulfonate/alpha-carboxylate recognition contributed by Arg163 and Gln160
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
-
-
?
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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
taurine + pyruvate
2-sulfoacetaldehyde + L-alanine
involved in taurine catabolism
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
essential for growth on taurine
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
essential for growth on taurine
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
one of several mechanisms for desulfonation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
initial step in anaerobic taurine degradation
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in the desulfonation pathway dissimilating taurine
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
enzyme is involved in the desulfonation pathway dissimilating taurine, overview, homeostatic mechanism
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
enzyme is involved in the desulfonation pathway dissimilating taurine, overview, homeostatic mechanism
-
-
r
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
L-alanine + 2-sulfoacetaldehyde
-
enzyme is involved in desulfonation in the cells, the pathway produces bisulfite and acetyl phosphate, in vivo independently of pyruvate
-
-
?
taurine + pyruvate
sulfoacetaldehyde + L-alanine
-
inducible enzyme
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
-
-
?
additional information
?
-
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxyl 5'-phosphate is not essentially required
pyridoxal 5'-phosphate
pyridoxyl 5'-phosphate is not essentially required
additional information
-
pyridoxal 5'-phosphate is not necessary for activity
-
additional information
-
pyridoxal 5'-phosphate is not necessary for activity
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-alanine
-
feed-back inhibition, no growth of the organism in presence of L-alanine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme is inducible by taurine, and beta-alanine + sulfate
-
additional information
incubation th at 50°C for 8 h or at 60°C for 30 min increases activity by up to 2.5fold
-
additional information
-
enzyme is induced under nitrogen- and carbon-limited conditions
-
additional information
enzyme is induced under nitrogen- and carbon-limited conditions
-
additional information
-
enzyme is induced under nitrogen- and carbon-limited conditions
-
additional information
-
enzyme is inducible by taurine, and beta-alanine + sulfate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
taurine
pH 9.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.26
substrate (S)-1-methylbenzylamine, pH 9.0, 37°C
0.52
substrate methanal, pH 9.0, 37°C
0.67
substrate propanal, pH 9.0, 37°C
0.68
0.71
substrate glyoxylate, pH 9.0, 37°C
0.75
substrate glycolaldehyde, pH 9.0, 37°C
0.78
substrate hexanal, pH 9.0, 37°C
0.8
substrate pentanal, pH 9.0, 37°C
10.2
substrate taurine, pH 9.0, 37°C
additional information
0.68
substrate butanal, pH 9.0, 37°C
0.68
substrate ethanal, pH 9.0, 37°C
additional information
activity depends strongly on growth substrate
additional information
-
activity depends strongly on growth substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10
more than 20% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
17% of maximum activity
70
less than 30% of maximum activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
of the tauR-ald-tpa gene cluster; inducible enzyme
SwissProt
brenda
of the tauR-ald-tpa gene cluster; inducible enzyme
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
brenda
additional information
additional information
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
brenda
additional information
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source, and partial carbon source, in presence of CO2 during photoheterotrophic growth
-
brenda
additional information
-
cells grow on taurine as sole carbon, sulfur, and nitrogen source, enzyme is induced under nitrogen- and carbon-limited conditions
brenda
additional information
cells grow on taurine as sole carbon, sulfur, and nitrogen source, enzyme is induced under nitrogen- and carbon-limited conditions, activity overview
brenda
additional information
-
cells grow on taurine as sole carbon, sulfur, and nitrogen source, enzyme is induced under nitrogen- and carbon-limited conditions, activity overview
brenda
additional information
-
cells grow on taurine as sole carbon, sulfur, and nitrogen source, enzyme is induced under nitrogen- and carbon-limited conditions, activity overview
-
brenda
additional information
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
brenda
additional information
-
cells grow on taurine as sole electron donor, sulfur and nitrogen source during photoautotrophic growth
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
degradation pathway for hypotaurine in strain PD1222 can be depicted as follows: The aminotransferase converts hypotaurine to sulfinoacetaldehyde, which desulfinates spontaneously to acetaldehyde and sulfite. An inducible aldehyde dehydrogenase oxidizes acetaldehyde to yield acetate, which is metabolized, and sulfite, which is excreted
physiological function
-
degradation pathway for hypotaurine in strain PD1222 can be depicted as follows: The aminotransferase converts hypotaurine to sulfinoacetaldehyde, which desulfinates spontaneously to acetaldehyde and sulfite. An inducible aldehyde dehydrogenase oxidizes acetaldehyde to yield acetate, which is metabolized, and sulfite, which is excreted
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Show AA Sequence and Transmembrane Helices (789 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
x * 45000, SDS-PAGE
50000
51000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
formation of large aggregates depends on storage conditions, freezing at -20°C, or rapid freezing in liquid nitrogen with storage at -20°C increases the 350 kDa form, addition of glycerol decreases the aggregation, a dimer of 95 kDa is preferably formed during storage at 4°C
additional information
-
formation of large aggregates depends on storage conditions, freezing at -20°C, or rapid freezing in liquid nitrogen with storage at -20°C increases the 350 kDa form, addition of glycerol decreases the aggregation, a dimer of 95 kDa is preferably formed during storage at 4°C
additional information
-
formation of large aggregates depends on storage conditions, freezing at -20°C, or rapid freezing in liquid nitrogen with storage at -20°C increases the 350 kDa form, addition of glycerol decreases the aggregation, a dimer of 95 kDa is preferably formed during storage at 4°C
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additional information
-
tetramers are most common, but other aggregates are also present
additional information
-
tetramers are most common, but other aggregates are also present
-
additional information
-
tetramers are most common, but other aggregates are also present
additional information
-
tetramers are most common, but other aggregates are also present
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of activte site. The active site shows a special large pocket and substrate tunnel
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme is unstable in buffers with neutral or alkaline pH value, except for HEPES at pH 7.0
640197
additional information
-
enzyme is unstable in buffers with neutral or alkaline pH value, except for HEPES at pH 7.0
640197
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
8 h, 2.5fold increase in activity
60
30 min, 2.5fold increase in activity
70
15 min, almost complete loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate may stabilize the enzyme
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
Methanol
DMSO
increase in DMSO concentration up to 10% enhances activity by up to 135%
DMSO
-
increase in DMSO concentration up to 10% enhances activity by up to 135%
-
Methanol
5%, fast loss of activity
Methanol
-
5%, fast loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or 22°C, sulfonate buffers MES or MOPS, pH range 6.0-7.0, 22 h, stable
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially by ultracentrifugation and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene cluster tauR-ald-tpa, genetic organization, DNA and amino acid sequence determination and analysis
orf459, essential for activity, no enzyme activity in deletion mutants
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
identification of Bilophila wadsworthia by specific PCR which targets the taurine:pyruvate aminotransferase gene
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Laue, H.; Cook, A.M.
Biochemical and molecular characterization of taurine:pyruvate transaminase from the anaerobe Bilophila wadsworthia
Eur. J. Biochem.
267
6841-6848
2000
Bilophila wadsworthia (Q9APM5), Bilophila wadsworthia, Bilophila wadsworthia RZATAU (Q9APM5), Bilophila wadsworthia RZATAU
brenda
Cook, A.M.; Denger, K.
Dissimilation of the C2 sulfonates
Arch. Microbiol.
179
1-6
2002
Bilophila wadsworthia, Bilophila wadsworthia (Q9APM5), Castellaniella defragrans, Castellaniella defragrans NKNTAU, Pseudomonas aeruginosa, Pseudomonas aeruginosa TAU5
brenda
Masepohl, B.; Fuhrer, F.; Klipp, W.
Genetic analysis of a Rhodobacter capsulatus gene region involved in utilization of taurine as a sulfur source
FEMS Microbiol. Lett.
205
105-111
2001
Rhodobacter capsulatus
brenda
Chien, C.C.; Leadbetter, E.R.; Godchaux, W.III.
Taurine-sulfur assimilation and taurine-pyruvate aminotransferase activity in anaerobic bacteria
Appl. Environ. Microbiol.
63
3021-3024
1997
Clostridium pasteurianum, no activity in Clostridium pasteurianum, no activity in Clostridium sp., no activity in Klebsiella oxytoca, no activity in Klebsiella sp., no activity in Clostridium sp. MS-1, no activity in Klebsiella oxytoca M5a1, Clostridium pasteurianum C1
brenda
Denger, K.; Ruff, J.; Schleheck, D.; Cook, A.M.
Rhodococcus opacus expresses the xsc gene to utilize taurine as a carbon source or as a nitrogen source but not as a sulfur source
Microbiology
150
1859-1867
2004
Rhodococcus jostii RHA1, Rhodococcus opacus (Q6JE91), Rhodococcus opacus, Bilophila wadsworthia (Q9APM5), Rhodococcus opacus ISO-5 (Q6JE91), Rhodococcus opacus ISO-5
brenda
Novak, R.T.; Gritzer, R.F.; Leadbetter, E.R.; Godchaux, W.
Phototrophic utilization of taurine by the purple nonsulfur bacteria Rhodopseudomonas palustris and Rhodobacter sphaeroides
Microbiology
150
1881-1891
2004
Cereibacter sphaeroides, Rhodopseudomonas palustris, Cereibacter sphaeroides Tau3, Rhodopseudomonas palustris Tau1
brenda
Shimamoto, G.; Berk, R.S.
Catabolism of taurine in Pseudomonas aeruginosa
Biochim. Biophys. Acta
569
287-292
1979
Pseudomonas aeruginosa, Pseudomonas aeruginosa TAU-5
brenda
Styp von Rekowski, K.; Denger, K.; Cook, A.M.
Isethionate as a product from taurine during nitrogen-limited growth of Klebsiella oxytoca TauN1
Arch. Microbiol.
183
325-330
2005
Klebsiella oxytoca, Klebsiella oxytoca TauN1
brenda
Laue, H.; Smits, T.H.; Schumacher, U.K.; Claros, M.C.; Hartemink, R.; Cook, A.M.
Identification of Bilophila wadsworthia by specific PCR which targets the taurine:pyruvate aminotransferase gene
FEMS Microbiol. Lett.
261
74-79
2006
Bilophila wadsworthia
brenda
Gorzynska, A.K.; Denger, K.; Cook, A.M.; Smits, T.H.
Inducible transcription of genes involved in taurine uptake and dissimilation by Silicibacter pomeroyi DSS-3T
Arch. Microbiol.
185
402-406
2006
Ruegeria pomeroyi (Q5LVM7)
brenda
Chen, Y.; Yi, D.; Jiang, S.; Wei, D.
Identification of novel thermostable taurine-pyruvate transaminase from Geobacillus thermodenitrificans for chiral amine synthesis
Appl. Microbiol. Biotechnol.
100
3101-3111
2016
Geobacillus thermodenitrificans subsp. thermodenitrificans (A0A0S2VC96), Geobacillus thermodenitrificans subsp. thermodenitrificans DSM 465 (A0A0S2VC96)
brenda
Felux, A.K.; Denger, K.; Weiss, M.; Cook, A.M.; Schleheck, D.
Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination followed by spontaneous desulfination to yield acetaldehyde and, finally, acetate for growth
J. Bacteriol.
195
2921-2930
2013
Paracoccus denitrificans (A1B9Z3), Paracoccus denitrificans Pd 1222 (A1B9Z3)
brenda
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