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Literature summary extracted from

  • Lagana, G.; Barreca, D.; Giacobbe, S.; Bellocco, E.
    Anaerobiosis and metabolic plasticity of Pinna nobilis biochemical and ecological features (2014), Biochem. Syst. Ecol., 56, 138-143 .
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.5.1.11 additional information the enzyme activity in adductor muscle increases following the marine-brackish gradient Pinna nobilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.17 additional information the enzyme activity in adductor muscle decreases following the marine-brackish gradient Pinna nobilis
1.5.1.22 additional information the enzyme activity in adductor muscle decreases following the marine-brackish gradient Pinna nobilis
1.5.1.23 additional information the enzyme activity in adductor muscle decreases following the marine-brackish gradient Pinna nobilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.11 L-arginine + pyruvate + NADH + H+ Pinna nobilis
-
 N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
 ?
1.5.1.17 beta-alanine + pyruvate + NADH + H+ Pinna nobilis
-
 beta-alanopine + NAD+ + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.11 Pinna nobilis
-
 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
-
1.5.1.17 Pinna nobilis
-
 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
-
1.5.1.22 Pinna nobilis
-
 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
-
1.5.1.23 Pinna nobilis
-
 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
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.11 adductor muscle ODH is the major opine dehydrogenase in the adductor muscle Pinna nobilis
-
1.5.1.11 gill
-
 Pinna nobilis
-
1.5.1.11 hepatopancreas very low enzyme content Pinna nobilis
-
1.5.1.11 mantle
-
 Pinna nobilis
-
1.5.1.11 additional information enzyme tissue distribution and expression analysis Pinna nobilis
-
1.5.1.17 adductor muscle the adductor muscle also shows a conspicuous amount of strombine dehydrogenase Pinna nobilis
-
1.5.1.17 gill
-
 Pinna nobilis
-
1.5.1.17 hepatopancreas
-
 Pinna nobilis
-
1.5.1.17 mantle
-
 Pinna nobilis
-
1.5.1.17 additional information enzyme tissue distribution and expression analysis Pinna nobilis
-
1.5.1.22 adductor muscle the adductor muscle also shows a conspicuous amount of strombine dehydrogenase Pinna nobilis
-
1.5.1.22 gill
-
 Pinna nobilis
-
1.5.1.22 hepatopancreas very low enzyme content Pinna nobilis
-
1.5.1.22 mantle
-
 Pinna nobilis
-
1.5.1.22 additional information enzyme tissue distribution and expression analysis Pinna nobilis
-
1.5.1.23 adductor muscle the adductor muscle also shows a conspicuous amount of strombine dehydrogenase Pinna nobilis
-
1.5.1.23 gill
-
 Pinna nobilis
-
1.5.1.23 hepatopancreas
-
 Pinna nobilis
-
1.5.1.23 mantle
-
 Pinna nobilis
-
1.5.1.23 additional information enzyme tissue distribution and expression analysis Pinna nobilis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.11 L-arginine + pyruvate + NADH + H+
-
 Pinna nobilis N2-(D-1-carboxyethyl)-L-arginine + NAD+ + H2O
-
 ?
1.5.1.17 beta-alanine + pyruvate + NADH + H+
-
 Pinna nobilis beta-alanopine + NAD+ + H2O
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.5.1.11 ODH
-
 Pinna nobilis
1.5.1.17 ADH
-
 Pinna nobilis
1.5.1.22 SDH
-
 Pinna nobilis
1.5.1.23 TDH
-
 Pinna nobilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.11 25
-
 assay at Pinna nobilis
1.5.1.17 25
-
 assay at Pinna nobilis
1.5.1.22 25
-
 assay at Pinna nobilis
1.5.1.23 25
-
 assay at Pinna nobilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.11 7
-
 assay at Pinna nobilis
1.5.1.17 7
-
 assay at Pinna nobilis
1.5.1.22 7
-
 assay at Pinna nobilis
1.5.1.23 7
-
 assay at Pinna nobilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.11 NAD+
-
 Pinna nobilis
1.5.1.11 NADH
-
 Pinna nobilis
1.5.1.17 NAD+
-
 Pinna nobilis
1.5.1.17 NADH
-
 Pinna nobilis
1.5.1.22 NAD+
-
 Pinna nobilis
1.5.1.22 NADH
-
 Pinna nobilis
1.5.1.23 NAD+
-
 Pinna nobilis
1.5.1.23 NADH
-
 Pinna nobilis

General Information

EC Number General Information Comment Organism
1.5.1.11 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). The ODH pathway is probably able to realize a higher rate of energy production than either the SDH or ADH pathways Pinna nobilis
1.5.1.11 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 Pinna nobilis
1.5.1.17 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) Pinna nobilis
1.5.1.17 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 Pinna nobilis
1.5.1.22 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) Pinna nobilis
1.5.1.22 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 Pinna nobilis
1.5.1.23 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) Pinna nobilis
1.5.1.23 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 Pinna nobilis