Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas

Fields, Jeremy H. A.; Eng, Alvin K.; Ramsden, W.; Hochachka, Peter W.; Weinstein, Boris

doi:10.1016/0003-9861(80)90493-2

Cited by 65 publications

(18 citation statements)

References 10 publications

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“…Opine formation is a cytosolic fermentation pathway in which pyruvate is condensed with an amino acid by a specific dehydrogenase that reduces the Schiff base with glycolytic NADH, resulting in an iminoacid derivative, an opine (176), as the end product of energy metabolism. The condensation of pyruvate and arginine by octopine dehydrogenase results in the formation of octopine as the reduced end product, whereas condensation with alanine or glycine results in the formation of alanopine and strombine, respectively (143,169).…”

Section: Animalsmentioning

confidence: 99%

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Müller

Mentel

Hellemond

et al. 2012

Microbiol Mol Biol Rev

695

904

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SUMMARY Major insights into the phylogenetic distribution, biochemistry, and evolutionary significance of organelles involved in ATP synthesis (energy metabolism) in eukaryotes that thrive in anaerobic environments for all or part of their life cycles have accrued in recent years. All known eukaryotic groups possess an organelle of mitochondrial origin, mapping the origin of mitochondria to the eukaryotic common ancestor, and genome sequence data are rapidly accumulating for eukaryotes that possess anaerobic mitochondria, hydrogenosomes, or mitosomes. Here we review the available biochemical data on the enzymes and pathways that eukaryotes use in anaerobic energy metabolism and summarize the metabolic end products that they generate in their anaerobic habitats, focusing on the biochemical roles that their mitochondria play in anaerobic ATP synthesis. We present metabolic maps of compartmentalized energy metabolism for 16 well-studied species. There are currently no enzymes of core anaerobic energy metabolism that are specific to any of the six eukaryotic supergroup lineages; genes present in one supergroup are also found in at least one other supergroup. The gene distribution across lineages thus reflects the presence of anaerobic energy metabolism in the eukaryote common ancestor and differential loss during the specialization of some lineages to oxic niches, just as oxphos capabilities have been differentially lost in specialization to anoxic niches and the parasitic life-style. Some facultative anaerobes have retained both aerobic and anaerobic pathways. Diversified eukaryotic lineages have retained the same enzymes of anaerobic ATP synthesis, in line with geochemical data indicating low environmental oxygen levels while eukaryotes arose and diversified.

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Section: Animalsmentioning

confidence: 99%

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Müller

Mentel

Hellemond

et al. 2012

Microbiol Mol Biol Rev

695

904

View full text Add to dashboard Cite

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“…Determination of the stoichiometry of the enzymecatalyzed reaction was carried out using an approach similar to that of Fields et al [28]. Due to the relatively low affinity of tauropine dehydrogenase for taurine, the stoichiometry between NADH, pyruvate and taurine was investigated under the following conditions.…”

Section: Stoichiometry Of the Reactionmentioning

confidence: 99%

Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa

GÄde

1986

European Journal of Biochemistry

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Tauropine dehydrogenase (tauropine : NAD oxidoreductase) was purified from the shell adductor muscle of the ormer, Haliotis lamellosa. The enzyme was found to utilize stoichiometrically NADH as co-enzyme and pyruvate and taurine as substrates producing tauropine [rhodoic acid; N-(D-1-carboxyethy1)-taurine]. The enzyme was purified to a specific activity of 463 units/mg protein using a combination of ammonium sulphate fractionation, ion-exchange and affinity chromatography. The relative molecular mass was 38000 f 1000 when assessed by gel filtration on Ultrogel AcA 54 and 42000 f 150 by electrophoresis on 5 -10% polyacrylamide gels in the presence of 1 YO sodium dodecyl sulphate; the data suggest a monomeric structure. Tauropine and pyruvate were found to be the preferred substrates. Among the amino acids tested for activity with the enzyme, only alanine is used as an alternative substrate, but with a rate less than 6% of the enzyme activity with taurine. Of the 0x0 acids tested, 2-oxobutyrate and 2-oxovalerate were also found to be substrates. Apparent K , values for the substrates NADH, pyruvate and taurine are 0.022 f 0.003 mM, 0.64 5 0.07 mM and 64.7 f 5.4 mM, respectively, at pH 7.0 and for the products, NAD' and tauropine, are 0.29 L-0.01 mM and 9.04 f 1.27 mM, respectively, at pH 8.3. Apparent K , values for both pyruvate and taurine decrease with increasing co-substrate (taurine or pyruvate) concentration. NAD+ and tauropine were found to be product inhibitors of the forward reaction. NAD' was a competitive inhibitor of NADH, whereas tauropine gave a mixed type of inhibition with respect to pyruvate and taurine. Succinate was found to inhibit non-competitively with respect to taurine and pyruvate with an apparent Ki value in the physiological range of this anaerobic end product. The inhibition by L-lactate, not an end product in the ormer, was competitive with respect to pyruvate. The physiological role or tauropine dehydrogenase during anaerobiosis is discussed.Exposure during low tide or reduced oxygen tension at the bottom of muddy, shallow, eutrophic waters force many marine and fresh water invertebrates such as bivalves, gastropods and various annelids to survive hypoxic or even anoxic conditions in the environment [l -31. These species can withstand prolonged periods of environmental anaerobiosis and, similarly, exposure to nitrogen in the laboratory [4 -61. Investigations on the main pathways of intermediary metabolism in these species have shown that the simultaneous breakdown of aspartate and carbohydrates lead to the production of multiple end products such as alanine, acetate, succinate and propionate in varying species-specific concentrations [l -3, 7 -91. Degradation of carbohydrates via the Embden-Meyerhof-Parnas pathway to lactate, i. e. anaerobic glycolysis, appeared to be of minor importance, since accumulation of lactate has been rarely demonstrated under hypoxic conditions [8, 11, 121. Several enzymes, however, have been discovered in molluscs and annelids, other than lactate dehydrog...

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“…One group can be categorized as N-substituted D-alanine and includes lysopine, octopine, octopinic acid, and histopine (4,14), and the other can be categorized as N-substituted D-glutamic acid and includes nopaline and nopalinic acid (16). Octopine is found in molluscan organisms, together with structurally related alanopine and strombine (10). Octopine dehydrogenase (EC 1.5.1.11) (9,13,15,37), lysopine dehydrogenase (EC 1.5.1.16) (30), alanopine dehydrogenase (EC 1.5.1.17) (11), and nopaline dehydrogenase (synthase) (EC 1.5.1.19) (20), involved in the metabolism of these compounds, have been characterized from crown gall tumor tissues and molluscs.…”

mentioning

confidence: 99%

A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C

1989

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A new NAD+-dependent opine dehydrogenase was purified to homogeneity from Arthrobacter sp. strain 1C isolated from soil by an enrichment culture technique. The enzyme has a molecular weight of about 70,000 and consists of two identical subunits with molecular weights of about 36,000. The enzyme catalyzed a reversible oxidation-reduction reaction of opine-type secondary amine dicarboxylic acids. In the oxidative deamination reaction, the enzyme was active toward unusual opines, such as N-[l-R-(carboxyl)ethyl]-S-methionine and N-[l-R-(carboxyl)ethylJ-S-phenylalanine. In the reductive secondary amine-forming reaction with NADH as a cofactor, the enzyme utilized L-amino acids such as L-methionine, L-isoleucine, L-valine, L-phenylalanine, L-leucine, L-alanine, and L-threonine as amino donors and a-keto acids such as pyruvate, oxaloacetate, glyoxylate, and x-ketobutyrate as amino acceptors. The product enzymatically synthesized from L-phenylalanine and pyruvate in the presence of NADH was identified as N-[l-R-(carboxyl)ethyl]-S-phenylalanine.

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Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas

Cited by 65 publications

References 10 publications

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Biochemistry and Evolution of Anaerobic Energy Metabolism in Eukaryotes

Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa

A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C

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