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Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
Gly + pyruvate + NADH
?
-
at 6.7% of the activity with taurine
-
-
?
Homotaurine + pyruvate + NADH
?
Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
Taurine + 2-oxobutanoate + NADH
?
Taurine + 2-oxohexanoate + NADH
?
-
at 4.8% of the activity with pyruvate
-
-
?
Taurine + 2-oxopentanoate + NADH
?
Taurine + 3-hydroxypyruvate + NADH
?
Taurine + glyoxylate + NADH
?
taurine + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
taurine is involved in osmoregulation in marine animals
-
-
?
taurine + oxaloacetate + NADH
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
tauropine + NAD+ + H2O
taurine + pyruvate + NADH
-
-
-
r
tauropine + NAD+ + H2O
taurine + pyruvate + NADH + H+
Val + pyruvate + NADH
?
Rhodoglossum japonicum
-
at 17% of the activity with taurine
-
-
?
additional information
?
-
Ala + pyruvate + NADH
?
-
about 2% of the activity with taurine
-
-
?
Ala + pyruvate + NADH
?
-
at 6% of the activity with taurine
-
-
?
Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
-
at 1.8% of the activity with taurine
-
-
?
Aminomethane sulfonic acid + pyruvate + NADH
N2-(1-Carboxyethyl)aminomethanesulfonic acid + NAD+ + H2O
-
at 10.9% of the activity with taurine
-
-
?
Homotaurine + pyruvate + NADH
?
-
at 2.4% of the activity with taurine
-
-
?
Homotaurine + pyruvate + NADH
?
-
at 8.1% of the activity with taurine
-
-
?
Homotaurine + pyruvate + NADH
?
-
at 32.1% of the activity with taurine
-
-
?
Homotaurine + pyruvate + NADH
?
Rhodoglossum japonicum
-
at 12% of the activity with taurine
-
-
?
Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
-
at 40% of the activity with taurine
-
-
?
Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
-
at 35.2% of the activity with taurine
-
-
?
Hypotaurine + pyruvate + NADH
N2-(1-Carboxyethyl)aminoethanesulfinic acid + NAD+ + H2O
-
at 21.2% of the activity with taurine
-
-
?
Taurine + 2-oxobutanoate + NADH
?
-
-
-
-
?
Taurine + 2-oxobutanoate + NADH
?
-
,at 7.9% of the activity with pyruvate
-
-
?
Taurine + 2-oxobutanoate + NADH
?
-
-
-
-
?
Taurine + 2-oxobutanoate + NADH
?
-
at 4.4% of the activity with pyruvate
-
-
?
Taurine + 2-oxopentanoate + NADH
?
-
at 7.8% of the activity with pyruvate
-
-
?
Taurine + 2-oxopentanoate + NADH
?
-
at 4.8% of the activity with pyruvate
-
-
?
Taurine + 2-oxopentanoate + NADH
?
-
-
-
-
?
Taurine + 2-oxopentanoate + NADH
?
-
-
-
-
?
Taurine + 3-hydroxypyruvate + NADH
?
-
at 21.2% of the activity with pyruvate
-
-
?
Taurine + 3-hydroxypyruvate + NADH
?
-
at 4.1% of the activity with pyruvate
-
-
?
Taurine + glyoxylate + NADH
?
-
at 10.9% of the activity with pyruvate
-
-
?
Taurine + glyoxylate + NADH
?
-
at 12.8% of the activity with pyruvate
-
-
?
Taurine + glyoxylate + NADH
?
-
at 6.8% of the activity with pyruvate
-
-
?
taurine + oxaloacetate + NADH
?
-
-
-
-
?
taurine + oxaloacetate + NADH
?
-
at 85.8% of the activity with pyruvate
-
-
?
taurine + oxaloacetate + NADH
?
-
at 78.1% of the activity with pyruvate
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
Balanus cariosus
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
r
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
r
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
no activity with NADPH
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
r
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
Rhodoglossum japonicum
-
r
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
Taurine + pyruvate + NADH
Tauropine + NAD+ + H2O
-
-
-
?
tauropine + NAD+ + H2O
taurine + pyruvate + NADH + H+
-
-
-
-
?
tauropine + NAD+ + H2O
taurine + pyruvate + NADH + H+
-
-
-
-
?
additional information
?
-
-
the enzyme is a dominant pyruvate reductase in this organism
-
-
?
additional information
?
-
-
the enzyme plays an important physiological role in energy production during shell fixation activity in the columnella muscle
-
-
?
additional information
?
-
involvement of the sponge TaDH in the final step of the glycolytic pathway in the regeneration of NAD+ under anaerobic conditions
-
-
?
additional information
?
-
opine production, opines are condensation products of an amino acid and a ketonic acid or a sugar
-
-
?
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brenda
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brenda
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brenda
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Balanus cariosus
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brenda
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brenda
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brenda
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brenda
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brenda
-
-
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brenda
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brenda
-
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brenda
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brenda
Japanese population (JJ), Taiwanese population (TT), and Vietnamese population (VV)
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
no activity in Amphitrite sp.
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-
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brenda
no activity in Aplysia juliana
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brenda
no activity in Aplysia kurodai
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-
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brenda
no activity in Aurelia aurita
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-
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brenda
no activity in Bugula neritina
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-
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brenda
no activity in Cerebratulus sp.
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brenda
no activity in Chaetopleura apiculata
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brenda
no activity in Chaetopterus variopedatus
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brenda
no activity in Clymenella torquata
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brenda
no activity in Crassostrea virginica
-
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brenda
no activity in Crepidula fornicata
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brenda
no activity in Dentalium pilsbryi
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-
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brenda
no activity in Glycera sp.
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brenda
no activity in Halocynthia roretzi
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-
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brenda
no activity in Hemigrapsus sanguineus
-
-
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brenda
no activity in Hexagrammos otakii
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brenda
no activity in Hydroides sp.
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-
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brenda
no activity in Lepidonotus sp.
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-
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brenda
no activity in Lineus sp.
-
-
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brenda
no activity in Littorina littorea
-
-
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brenda
no activity in Loligo bleekeri
-
-
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brenda
no activity in Lyonsia hyalina
-
-
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brenda
no activity in Membranipora tenuis
-
-
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brenda
no activity in Mopalia muscosa
-
-
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brenda
no activity in Mya arenaria
-
-
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brenda
no activity in Mytilus edulis
-
-
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brenda
no activity in Nereis sp.
-
-
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brenda
no activity in Nucella lapillus
-
-
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brenda
no activity in Nucula proxima
-
-
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brenda
no activity in Octopus membranaceus
-
-
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brenda
no activity in Oncorhynchus keta
-
-
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brenda
no activity in Phascolopsis sp.
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-
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brenda
no activity in Phascolosoma sp.
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brenda
no activity in Phoronis architecta
-
-
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brenda
no activity in Phoronis vancouverensis
-
-
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brenda
no activity in Priapulus sp.
-
-
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brenda
no activity in Pseudocardium sachalinensis
-
-
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brenda
no activity in Pugettia quadridens
-
-
-
brenda
no activity in Schizoporella floridana
-
-
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brenda
no activity in Solemya velum
-
-
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brenda
no activity in Spisula solidissima
-
-
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brenda
no activity in Stichopus japonicus
-
-
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brenda
no activity in Strongylocentrotus nudus
-
-
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brenda
no activity in Themiste sp.
-
-
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brenda
no activity in Urechis sp.
-
-
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brenda
no activity in Urosalpinx cinerea
-
-
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brenda
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brenda
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brenda
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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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brenda
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brenda
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brenda
Rhodoglossum japonicum
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brenda
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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
brenda
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brenda
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SwissProt
brenda
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brenda
from Japan population (RR), Taiwan population (TT), and the F1 hybrid (TR)
-
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brenda
-
UniProt
brenda
demosponge
UniProt
brenda
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metabolism
-
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
-
the enzyme is involved in energy production
physiological function
-
the enzyme pertains to muscle contraction and muscle protein regulation, it is involved in energy production
physiological function
-
the major anaerobic enzymes produced by abalone are lactate dehydrogenase (LDH) and tauropine dehydrogenase (TDH), which catalyse the reaction of pyruvate to D-lactate and tauropine, respectively. Abalone produce energy via opine and lactate pathways not only during functional tissue hypoxia that results from exercise but also during environmental hypoxia and thermal stress. Abalone are experimentally acclimated to control (16°C) and typical summer temperatures (23°C), each with oxygen treatments of 100% air saturation (O2sat) or 70% O2sat. During the first phase (chronic exposure), movement and oxygen consumption rates (MO2) of abalone are measured during a 2 day observation period at stable acclimation conditions. Additionaly, lactate dehydrogenase (LDH) and tauropine dehydrogenase (TDH) activities are measured. During phase two (acute exposure), O2sat is raised to 100% for abalone acclimated to 70% O2sat followed by an acute decrease in oxygen to anoxia for all acclimation groups during which movement and MO2 are determined again. During the chronic exposure, hybrids and Haliotis laevigata move shorter distances than Haliotis rubra. Resting MO2, LDH and TDH activities, however, are similar between abalone types but are increased at 23°C compared to 16°C. During the acute exposure, the initial increase to 100% O2sat for individuals acclimated to 70% O2sat result in increased movement compared to individuals acclimated to 100% O2sat for hybrids and Haliotis rubra when compared within type of abalone. Similarly, MO2 during spontaneous activity of all three types of abalone previously subjected to 70% O2sat increase above those at 100% O2sat. When oxygen levels have dropped below the critical oxygen level (Pcrit), movement in hybrids and Haliotis laevigata increase up to 6.5fold compared to movement above Pcrit. Differences in movement and energy use between hybrids and pure species are not marked enough to support the hypothesis that the purportedly higher growth in hybrids is due to an energetic advantage over pure species. Lactate dehydrogenase activity is twice as high in abalone_23°C in comparison to abalone_16°C, as is TDH activity. Further, TDH activity tends to be influenced by acclimation oxygen level and type of abalone. While movement tends to decrease with increasing temperatures, resting MO2 as well as LDH and TDH activities are increased at the higher temperature in all three types of abalone during the chronic exposure
physiological function
-
the major anaerobic enzymes produced by abalone are lactate dehydrogenase (LDH) and tauropine dehydrogenase (TDH), which catalyse the reaction of pyruvate to D-lactate and tauropine, respectively. Abalone produce energy via opine and lactate pathways not only during functional tissue hypoxia that results from exercise but also during environmental hypoxia and thermal stress. Abalone are experimentally acclimated to control (16°C) and typical summer temperatures (23°C), each with oxygen treatments of 100% air saturation (O2sat) or 70% O2sat. During the first phase (chronic exposure), movement and oxygen consumption rates (MO2) of abalone are measured during a 2 day observation period at stable acclimation conditions. Additionaly, lactate dehydrogenase (LDH) and tauropine dehydrogenase (TDH) activities are measured. During phase two (acute exposure), O2sat is raised to 100% for abalone acclimated to 70% O2sat followed by an acute decrease in oxygen to anoxia for all acclimation groups during which movement and MO2 are determined again. During the chronic exposure, hybrids and Haliotis laevigata move shorter distances than Haliotis rubra. Resting MO2, LDH and TDH activities, however, are similar between abalone types but are increased at 23°C compared to 16°C. During the acute exposure, the initial increase to 100% O2sat for individuals acclimated to 70% O2sat result in increased movement compared to individuals acclimated to 100% O2sat for hybrids and Haliotis rubra when compared within type of abalone. Similarly, MO2 during spontaneous activity of all three types of abalone previously subjected to 70% O2sat increase above those at 100% O2sat. When oxygen levels have dropped below the critical oxygen level (Pcrit), movement in hybrids and Haliotis laevigata increase up to 6.5fold compared to movement above Pcrit. Differences in movement and energy use between hybrids and pure species are not marked enough to support the hypothesis that the purportedly higher growth in hybrids is due to an energetic advantage over pure species. Lactate dehydrogenase activity is twice as high in abalone_23°C in comparison to abalone_16°C, as is TDH activity. Further, TDH activity tends to be influenced by acclimation oxygen level and type of abalone. While movement tends to decrease with increasing temperatures, resting MO2 as well as LDH and TDH activities are increased at the higher temperature in all three types of abalone during the chronic exposure
additional information
-
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
-
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
-
proteomic analysis, the enzyme shows an expression pattern of Japan > Taiwan/Japan hybrid > Taiwan in the different populations, overview
additional information
-
the differences in movement, anaerobic enzyme activities, and MO2 between hybrids and pure species in this study are not marked enough to support the original hypothesis that hybrids have an energetic advantage over pure species
additional information
-
the differences in movement, anaerobic enzyme activities, and MO2 between hybrids and pure species in this study are not marked enough to support the original hypothesis that hybrids have an energetic advantage over pure species
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Hammen, C.S.; Fileding, C.
Opine oxidoreductases in marine worms of five phyla
Comp. Biochem. Physiol. B
106
989-992
1993
no activity in Amphitrite sp., no activity in Cerebratulus sp., no activity in Chaetopterus variopedatus, no activity in Clymenella torquata, no activity in Glycera sp., no activity in Hydroides sp., no activity in Lepidonotus sp., no activity in Lineus sp., no activity in Nereis sp., no activity in Phascolopsis sp., no activity in Phascolosoma sp., no activity in Priapulus sp., no activity in Themiste sp., no activity in Urechis sp.
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brenda
Sato, M.; Takeuchi, M.; Kanno, N.; Nagahisa, E.; Sato, Y.
Distribution of opine dehydrogenases and lactate dehydrogenase activities in marine animals
Comp. Biochem. Physiol. B
106
955-960
1993
Anthopleura japonica, Anthopleura nigrescens, Asterias amurensis, Patiria pectinifera, Balanus cariosus, Buccinum isaotakii, Cellana grata, Azumapecten farreri nipponensis, Chlorostoma lischkei, Crassostrea gigas, Fusitriton oregonensis, Halichondria japonica, Haliotis discus hannai, Liolophura japonica, Littorina brevicula, Meretrix lusoria, Neptunea arthritica, no activity in Aplysia kurodai, no activity in Aplysia juliana, no activity in Aurelia aurita, no activity in Halocynthia roretzi, no activity in Hemigrapsus sanguineus, no activity in Hexagrammos otakii, no activity in Loligo bleekeri, no activity in Mytilus edulis, no activity in Octopus membranaceus, no activity in Oncorhynchus keta, no activity in Pugettia quadridens, no activity in Pseudocardium sachalinensis, no activity in Stichopus japonicus, no activity in Strongylocentrotus nudus, Octopus vulgaris, Pagurus samuelis, Mizuhopecten yessoensis, Perinereis nuntia, Capitulum mitella, Pseudopotamilla occelata, Reishia clavigera, Ruditapes philippinarum, Anadara broughtonii, Solaster paxillatus, Todarodes pacificus, Scelidotoma gigas
-
brenda
Hammen, C.S.; Bullock, R.C.
Opine oxidoreductases in brachiopods, bryozoans, phoronids and molluscs
Biochem. Syst. Ecol.
19
263-269
1991
Lunarca ovalis, Diodora cayenensis, Glottidia pyramidata, Haliotis rufescens, Laqueus californianus, no activity in Bugula neritina, no activity in Chaetopleura apiculata, no activity in Crassostrea virginica, no activity in Crepidula fornicata, no activity in Dentalium pilsbryi, no activity in Littorina littorea, no activity in Lyonsia hyalina, no activity in Membranipora tenuis, no activity in Mopalia muscosa, no activity in Mya arenaria, no activity in Nucella lapillus, no activity in Nucula proxima, no activity in Phoronis architecta, no activity in Phoronis vancouverensis, no activity in Schizoporella floridana, no activity in Solemya velum, no activity in Spisula solidissima, no activity in Urosalpinx cinerea, Testudinalia testudinalis, Tegula funebralis, Terebratalia transversa, Turbo castanea
-
brenda
Gde, G.
A specific enzymatic method for determination of taurine
Biol. Chem. Hoppe-Seyler
368
1519-1523
1987
Haliotis tuberculata lamellosa
brenda
Gde, G.
Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa
Eur. J. Biochem.
160
311-318
1986
Haliotis tuberculata lamellosa
brenda
Sato, M.; Takeuchi, M.; Kanno, N.; Nagahisa, E.; Sato, Y.
Characterization and physiological role of tauropine dehydrogenase and lactate dehydrogenase from muscle of abalone, Haliotis discus hannai
Tohoku J. Agric. Res.
41
83-95
1991
Haliotis discus hannai
-
brenda
Kanno, N.; Sato, M.; Nagahisa, E.; Sato, Y.
Purification and characterization of tauropine dehydrogenase from the marine sponge Halichondria japonica Kadota (demospongia)
Fish. Sci.
63
414-420
1997
Halichondria japonica
-
brenda
Sato, M.; Takeuchi, M.; Kanno, N.; Nagahisa, E.; Sato, Y.
Purification and properties of tauropine dehydrogenase from a red alga Rhodoglossum japonicum
Hydrobiologia
260/261
673-678
1993
Rhodoglossum japonicum
-
brenda
Kan-no, N.; Sato, M.; Yokoyama, T.; Nagahisa, E.; Sato, Y.
Tauropine dehydrogenase from the starfish Asterina pectinifera (echinodermata: asteroidea): presence of opine production pathway in a deuterostome invertebrate
Comp. Biochem. Physiol. B
121
323-332
1998
Patiria pectinifera
brenda
Kanno, N.; Sato, M.; Nagahisa, E.; Sato, Y.
Tauropine dehydrogenase from the sandworm Arabella iricolor (polychaeta: errantia): purification and characterization
Comp. Biochem. Physiol. B
114
409-416
1996
Arabella iricolor
brenda
Kan-no, N.; Endo, N.; Moriyama, S.; Nagahisa, E.; Sato, M.
The amino acid sequence of tauropine dehydrogenase from the polychaete Arabella iricolor
Comp. Biochem. Physiol. B
140
475-485
2005
Arabella iricolor (Q8T882), Arabella iricolor
brenda
Kan-no, N.; Matsu-ura, H.; Jikihara, S.; Yamamoto, T.; Endo, N.; Moriyama, S.; Nagahisa, E.; Sato, M.
Tauropine dehydrogenase from the marine sponge Halichondria japonica is a homolog of ornithine cyclodeaminase/m-crystallin
Comp. Biochem. Physiol. B
141B
331-339
2005
Halichondria japonica (Q60FC7)
-
brenda
Plese, B.; Grebenjuk, V.A.; Schroeder, H.C.; Breter, H.J.; Mueller, I.M.; Mueller, W.E.
Cloning and expression of a tauropine dehydrogenase from the marine sponge Suberites domuncula
Mar. Biol.
153
1219-1232
2008
Suberites domuncula (B1GT63)
-
brenda
Lagana, G.; Barreca, D.; Giacobbe, S.; Bellocco, E.
Anaerobiosis and metabolic plasticity of Pinna nobilis biochemical and ecological features
Biochem. Syst. Ecol.
56
138-143
2014
Pinna nobilis
-
brenda
Di, G.; Miao, X.; Ke, C.; Kong, X.; Li, H.; You, W.
Protein changes in abalone foot muscle from three geographical populations of Haliotis diversicolor based on proteomic approach
Ecol. Evol.
6
3645-3657
2016
Haliotis diversicolor
brenda
Di, G.; You, W.; Yu, J.; Wang, D.; Ke, C.
Genetic changes in muscle protein following hybridization between Haliotis diversicolor reeve Japan and Taiwan populations revealed using a proteomic approach
Proteomics
13
845-859
2013
Haliotis discus hannai
brenda
Alter, K.; Morash, A.; Andrewartha, S.; Andrew, S.; Clark, T.; Elliott, N.; Frappell, P.
Aerobic and anaerobic movement energetics of hybrid and pure parental abalone
J. Comp. Physiol. B
191
1111-1124
2021
Haliotis rubra, Haliotis laevigata
brenda