Information on EC 1.5.1.23 - Tauropine dehydrogenase

Ruditapes philippinarum

13292

Scapharca broughtonii

; demosponge

UniProt

Terebratalia transversa

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metabolism

Pinna nobilis

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)

741868

physiological function

additional information

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Ala + pyruvate + NADH

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

47 entries

tauropine + NAD+ + H2O

taurine + pyruvate + NADH

Val + pyruvate + NADH

Rhodoglossum japonicum

at 17% of the activity with taurine

additional information

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taurine + NADH + H+ + pyruvate

tauropine + NAD+ + H2O

B1GT63

taurine is involved in osmoregulation in marine animals

tauropine + NAD+ + H2O

taurine + pyruvate + NADH

Q8T882

additional information

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NAD(P)+

TaDH displays the GxGxxG/A motif known to be conserved among NAD(P)-dependent dehydrogenases

NAD+

NADH

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2-oxobutanoate

slight substrate inhibition

5,5'-dithiobis(2-nitrobenzoate)

sulfhydryl reagents restore activity

Cu2+

Fe2+

Fluorescein mercuric acetate

sulfhydryl reagents restore activity

Hg2+

L-lactate

competitive with respect to pyruvate

NAD+

oxaloacetate

slight substrate inhibition

pyruvate

succinate

noncompetitive with respect to taurine and pyruvate

tauropine

Zn2+

additional information

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3.3 - 21.1

2-oxobutanoate

3.6

2-oxovalerate

235

Ala

0.051 - 0.29

NAD+

0.022 - 0.071

NADH

6 entries

4.9

oxaloacetate

0.068 - 0.8

pyruvate

15 - 44.4

taurine

0.39 - 30

tauropine

additional information

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Rhodoglossum japonicum

463

551.8

780

878.3

additional information

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tauropine formation

6.6 - 7.3

tauropine formation, enzyme form TaDH-1

6.8

tauropine formation

assay at

7.2

8.5

tauropine oxidation

8.7 - 9.2

tauropone oxidation

tauropine oxidation

9.7

Rhodoglossum japonicum

tauropine oxidation

tauropine oxidation

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5.1 - 7.2

50% of maximal activity at pH 5.1 and at pH 7.2, 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

5.5 - 7.4

50% of maximal activity at pH 5.5 and at pH 7.4, tauropine formation

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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assay at

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5.34

sequence calculation

743766

5.4

theoretical value

5.44

calculated from amino acid sequence

isozyme 2

7.5

isozyme 1

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the adductor muscle also shows a conspicuous amount of strombine dehydrogenase

additional information

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36500

36920

calculated from amino acid sequence; deduced from cDNA and determined by SDS polyacrylamide gele electrophoresis and Western blot analysis

37000

1 * 37000, SDS-PAGE

38000

gel filtration

39000

Rhodoglossum japonicum

gel filtration

41300

1 * 41300, SDS-PAGE

42000

42400

gel filtration

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

43700

gel filtration

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monomer

7 entries

additional information

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no glycoprotein

enzyme contains 2 possible N-glycoslyation sites but no carbohydrates

additional information

Q60FC7;

protein sequence contains a N-acetylated N-terminal serine and no intrachain disulfide bond

673151

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Rhodoglossum japonicum

unstable above

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unstable to freezing and thawing

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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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2 enzyme forms: TaDH-1 and TaDH-2

Ni-NTA-column chromatography; purification by metal-chelate affinity chromatography on a Ni-NTA-column

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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