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Enzyme Nomenclature
Information on EC 1.5.1.23 - Tauropine dehydrogenase
for references in articles please use BRENDA:EC1.5.1.23
Word Map on EC 1.5.1.23
- 1.5.1.23
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haliotis
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invertebrate
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polychaete
- abalone
- adductor
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intrachain
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halichondria
- l-alanine
- diversicolor
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triosephosphate
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.5.1.23
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RECOMMENDED NAME
GeneOntology No.
Tauropine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+
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tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+
Cys146 might be essential for the catalytic reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
N2-(D-1-carboxyethyl)taurine:NAD+ oxidoreductase (taurine-forming)
In the reverse reaction, alanine can act instead of taurine, but more slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of pyruvate.
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CAS REGISTRY NUMBER
COMMENTARY
104645-74-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Japanese population (JJ), Taiwanese population (TT), and Vietnamese population (VV)
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collected in the straits of Messina area (central Mediterranean) between May and June of 2011, from two nearby marine and brackish-water sites, two populations
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sandworm, polychaete, 2 isozymes differing at position 41 of the aminoa cid sequence: isozyme 1 has Thr41, isozyme 2 has Ile41
SwissProt
from Japan population (RR), Taiwan population (TT), and the F1 hybrid (TR)
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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bivalves have evolved diverse and highly specialised strategies for surviving in hypoxic episodes including pathways that are efficient both in terms of ATP production, and in minimising H+ and toxic end product accumulation. Under these circumstances, glycogen is metabolized to pyruvate and the cytosolic NADH/NAD+ redox ratio is balanced by the reduction of pyruvate to lactate. Alternatively, NAD+ can be recycled more efficiently by coupling an amino acid to pyruvate, with formation of opines such as alanopine, tauropine, octopine, and strombine. Specimens utilizing the octopine rather than the alanopine pathway will increase energy flow rapidly, developing a major ability to counteract environmental variations. The high ratio between malate dehydrogenase/lactate dehydrogenase is due to the ability of Pinna nobilis to turn on anaerobic metabolism as a consequence of environmental or anthropogenic stresses. Anaerobic pathways are not all equivalent in terms of energy production based upon maximum rates for ATP output (lactate > octopine > alanopine = strombine)
physiological function
additional information
physiological function
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the enzyme pertains to muscle contraction and muscle protein regulation, it is involved in energy production
additional information
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comparisons of opine dehydrogenases activities (octopine dehydrogenase, alanopine dehydrogenase, strombine dehydrogenase, and tauropine dehydrogenase) in the adductor muscle, overview. The ODH activity in adductor muscle increases following the marine-brackish gradient, while the one of ADH, SDH and TDH decreases following the same gradient
additional information
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proteomic analysis of foot muscle proteins from three geographical populations of Haliotis diversicolor, the enzyme shows an expression pattern in the populations of Japan > Vietnam > Taiwan, overview
additional information
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proteomic analysis, the nezyme shows an expression pattern of Japan > Taiwan/Japan hybrid > Taiwan in the different populations, overview
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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
Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
Taurine + 2-oxohexanoate + NADH
?
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at 4.8% of the activity with pyruvate
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taurine + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
taurine is involved in osmoregulation in marine animals
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?
Ala + pyruvate + NADH
?
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at 6% of the activity with taurine
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Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
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at 1.8% of the activity with taurine
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Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
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at 10.9% of the activity with taurine
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Homotaurine + pyruvate + NADH
?
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at 2.4% of the activity with taurine
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Homotaurine + pyruvate + NADH
?
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at 8.1% of the activity with taurine
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Homotaurine + pyruvate + NADH
?
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at 32.1% of the activity with taurine
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Homotaurine + pyruvate + NADH
?
Rhodoglossum japonicum
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at 12% of the activity with taurine
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Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
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at 40% of the activity with taurine
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Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
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at 35.2% of the activity with taurine
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Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
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at 21.2% of the activity with taurine
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Taurine + 2-oxobutanoate + NADH
?
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,at 7.9% of the activity with pyruvate
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Taurine + 2-oxobutanoate + NADH
?
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at 4.4% of the activity with pyruvate
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Taurine + 2-oxopentanoate + NADH
?
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at 7.8% of the activity with pyruvate
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Taurine + 2-oxopentanoate + NADH
?
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at 4.8% of the activity with pyruvate
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Taurine + 3-hydroxypyruvate + NADH
?
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at 21.2% of the activity with pyruvate
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Taurine + 3-hydroxypyruvate + NADH
?
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at 4.1% of the activity with pyruvate
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Taurine + glyoxylate + NADH
?
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at 10.9% of the activity with pyruvate
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Taurine + glyoxylate + NADH
?
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at 12.8% of the activity with pyruvate
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Taurine + glyoxylate + NADH
?
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at 6.8% of the activity with pyruvate
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taurine + oxaloacetate + NADH
?
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at 85.8% of the activity with pyruvate
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taurine + oxaloacetate + NADH
?
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at 78.1% of the activity with pyruvate
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Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
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Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
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no activity with NADPH
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additional information
?
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the enzyme is a dominant pyruvate reductase in this organism
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additional information
?
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the enzyme plays an important physiological role in energy production during shell fixation activity in the columnella muscle
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additional information
?
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involvement of the sponge TaDH in the final step of the glycolytic pathway in the regeneration of NAD+ under anaerobic conditions
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additional information
?
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opine production, opines are condensation products of an amino acid and a ketonic acid or a sugar
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
B1GT63
taurine is involved in osmoregulation in marine animals
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?
additional information
?
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the enzyme is a dominant pyruvate reductase in this organism
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additional information
?
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the enzyme plays an important physiological role in energy production during shell fixation activity in the columnella muscle
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additional information
?
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B1GT63
involvement of the sponge TaDH in the final step of the glycolytic pathway in the regeneration of NAD+ under anaerobic conditions
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additional information
?
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B1GT63
opine production, opines are condensation products of an amino acid and a ketonic acid or a sugar
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)+
TaDH displays the GxGxxG/A motif known to be conserved among NAD(P)-dependent dehydrogenases
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
succinate
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noncompetitive with respect to taurine and pyruvate
tauropine
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mixed type inhibition with respect to pyruvate and taurine
additional information
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the enzyme activity in adductor muscle decreases following the marine-brackish gradient
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additional information
level of expression of TaDH is controlled by oxygen: TaDH is expressed when the oxygen level is low, during anaerobic glycolysis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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effect of cosubstrate concentration on the Km-value of tauropine and pyruvate
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additional information
additional information
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effect of cosubstrate concentration on the Km-value of tauropine and pyruvate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 7.2
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50% of maximal activity at pH 5.1 and at pH 7.2, tauropine formation
5.5 - 7.9
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50% of maximal activity at pH 5.5 and at pH 7.9, tauropine formation, enzyme form TaDH-1
5.5 - 7.4
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50% of maximal activity at pH 5.5 and at pH 7.4, tauropine formation
6.8 - 8.5
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50% of maximal activity at pH 6.8, optimum at pH 8.5, tauropine oxidation, enzyme form TaDH-1
8 - 9
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pH 8.0: 50% of maximal activity, pH 9.0: optimum, tauropine oxidation
8.7 - 9.2
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50% of maximal activity at pH 8.7 and at pH 9.2, tauropine oxidation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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the adductor muscle also shows a conspicuous amount of strombine dehydrogenase
additional information
additional information
sponges are collected in Croatia and whole bodys are used for enzyme characterization, high levels of this enzyme in most of cell types
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
36920
calculated from amino acid sequence; deduced from cDNA and determined by SDS polyacrylamide gele electrophoresis and Western blot analysis
42000
43086
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
43098
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
43500
43500
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 43086, isozyme 1, amino acid sequence calculation, x * 43098, isozyme 2, amino acid sequence calculation, x * 43500, both isozymes, SDS-PAGE
additional information
amino acid sequence determination and analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
enzyme contains 2 possible N-glycoslyation sites but no carbohydrates
additional information
protein sequence contains a N-acetylated N-terminal serine and no intrachain disulfide bond
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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
4°C, 2 mM KH2PO4-NaOH, pH 7.2, 1 mM EDTA, 10 mM 2-mercaptoethanol, stable for at least 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA-column chromatography; purification by metal-chelate affinity chromatography on a Ni-NTA-column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of the cDNA by PCR. DNA encoding TaDH is amplified by PCR from Suberites domuncula cDNA library, using the primers that are designed to amplify the complete open reading frame. Expression in Escherichia coli as His-tag fusion protein. Two allelic variants are identified, which are present in the different specimens either in a homozygotic or in a heterozygotic way (length polymorphism (453 bp and 468 bp long) is detected in the second intron and the beginning of third exon).
DNA and amino acid sequence determination and analysis, sequence comparisons
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.23)
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