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Information on EC 1.5.1.23 - Tauropine dehydrogenase
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1.5.1.23 Tauropine dehydrogenaseIUBMB Comments
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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Word Map
- 1.5.1.23
-
haliotis
-
invertebrate
- abalone
-
polychaete
- adductor
-
triosephosphate
-
halichondria
- diversicolor
-
intrachain
The enzyme appears in viruses and cellular organisms
Synonyms
tauropine dehydrogenase, tadh, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TaDH
tauropine dehydrogenase
belongs to the family of opine dehydrogenases, phylogenetic analyses indicate that TaDH is only distantly related to the opine dehydrogenases from marine invertebrates, high sequence similarity to bacterial ornithine cyclodeaminases
tauropine [(carboxyethyl)-taurine/derived from sulfhydryl-amino acids] dehydrogenase
-
tauropine [(carboxyethyl)-taurine/derived from sulfhydrylamino acids] dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tauropine + NAD+ + H2O = taurine + pyruvate + NADH + H+
-
-
-
-
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
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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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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
?
-
at 4.8% of the activity with pyruvate
-
?
taurine + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
taurine is involved in osmoregulation in marine animals
-
?
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
?
-
,at 7.9% of the activity with pyruvate
-
?
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 + 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
?
-
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
-
no activity with NADPH
-
?
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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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 + NADH + H+ + pyruvate
tauropine + NAD+ + H2O
taurine is involved in osmoregulation in marine animals
-
-
?
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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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
succinate
-
noncompetitive with respect to taurine and pyruvate
tauropine
-
mixed type inhibition with respect to pyruvate and taurine
additional information
-
the enzyme activity in adductor muscle decreases following the marine-brackish gradient
-
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
-
effect of cosubstrate concentration on the Km-value of tauropine and pyruvate
-
additional information
additional information
-
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
-
50% of maximal activity at pH 5.1 and at pH 7.2, tauropine formation
5.5 - 7.4
-
50% of maximal activity at pH 5.5 and at pH 7.4, tauropine formation
5.5 - 7.9
-
50% of maximal activity at pH 5.5 and at pH 7.9, tauropine formation, enzyme form TaDH-1
6.8 - 8.5
-
50% of maximal activity at pH 6.8, optimum at pH 8.5, tauropine oxidation, enzyme form TaDH-1
8 - 9
-
pH 8.0: 50% of maximal activity, pH 9.0: optimum, tauropine oxidation
8.7 - 9.2
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Japanese population (JJ), Taiwanese population (TT), and Vietnamese population (VV)
-
-
brenda
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
-
-
brenda
sandworm, polychaete, 2 isozymes differing at position 41 of the aminoa cid sequence: isozyme 1 has Thr41, isozyme 2 has Ile41
SwissProt
brenda
from Japan population (RR), Taiwan population (TT), and the F1 hybrid (TR)
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the adductor muscle also shows a conspicuous amount of strombine dehydrogenase
brenda
additional information
additional information
-
enzyme tissue distribution and expression analysis
brenda
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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
physiological function
-
the enzyme pertains to muscle contraction and muscle protein regulation, it is involved in energy production
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 nezyme shows an expression pattern of Japan > Taiwan/Japan hybrid > Taiwan in the different populations, overview
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TADH_ARAIR
397
0
43229
Swiss-Prot
other Location (Reliability: 3)
B1GT63_SUBDO
337
0
36924
TrEMBL
other Location (Reliability: 2)
Q60FC7_HALJA
334
0
36519
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
36920
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
36920
deduced from cDNA and determined by SDS polyacrylamide gele electrophoresis and Western blot analysis
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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SUBUNIT
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
-
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, Scapharca broughtonii, Solaster paxillatus, Todarodes pacificus, Tugali 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, Chlorostoma funebralis, Terebratalia transversa, Turbo castanea
-
brenda
Gäde, G.
A specific enzymatic method for determination of taurine
Biol. Chem. Hoppe-Seyler
368
1519-1523
1987
Haliotis tuberculata lamellosa
brenda
Gäde, 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
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