Properties of the flavoenzyme d-aspartate oxidase from Octopus vulgaris

Tedeschi, Gioacchino; Negri, Armando; Ceciliani, Fabrizio; Ronchi, Severino; Vetere, Amedeo; D’Aniello, Gemma; D’Aniello, Antimo

doi:10.1016/0167-4838(94)00071-9

Cited by 44 publications

(28 citation statements)

References 19 publications

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“…It was also a good substrate for DDO from fish 16 . A good performance for D-glutamate of DDO from flying squid liver is in agreement with those of octopus 23 , microorganism 27 , and carp kidney enzyme 16 , and in marked contrast with those of the mammalian 26 , and amphibian enzyme 28 , in which D-glutamate was a poor substrate. D-Glutamate was also reported to be a poor substrate in comparison with D-aspartate for DDO from the liver of carp, crucian carp, rainbow trout, yellowtail, and red sea bream 15 , but flying squid liver showed the opposite result.…”

Section: Animal Animal Animal Animal Animalsupporting

confidence: 65%

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Sarower¹,

Mizutani²,

Abe³

2004

ScienceAsia

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ABSTRACT:The distribution of D-amino acid oxidase (DAO, EC 1.4.3.3) and D-aspartate oxidase (DDO, EC 1.4.3.1) activities was examined on several tissues of various marine invertebrate species. Only DAO activity was detected in kidney and midgut gland from most of the mollusks with some exceptions. Hepatopancreas or liver from kuruma prawn, crayfish, squid, and octopus and antenal gland from crayfish showed significant amount of activity of both enzymes. Squid demonstrated a higher activity of DDO than that of DAO. DProline was the best substrate for DAO in common flying squid liver followed by D-alanine, D-histidine, Dtyrosine, and D-phenylalanine. On the contrary, meso-2,3-diaminosuccinate was the best substrate for DDO followed by N-acetyl-DL-aspartate, D-glutamate, D-amino adipate, and D-homocysteic acid. These enzymes, at least in kidney and midgut gland, are believed to metabolize exogenous and endogenous free D-alanine, that is abundant in aquatic invertebrates such as crustaceans and bivalve mollusks.

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Section: Animal Animal Animal Animal Animalsupporting

confidence: 65%

“…The properties of DDO of Octopus vulgaris have been studied extensively 23 . Both of these enzyme activities are commonly high in kidney and liver and low in intestine of fish, and are believed to eliminate D-amino acids from fish tissues 16 .…”

Section: Animal Animal Animal Animal Animalmentioning

confidence: 99%

Untitled

Sarower¹,

Mizutani²,

Abe³

2004

ScienceAsia

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“…As a standard, 10 µl of a solution of 1 mM -aspartate and 40 µl distilled water was used instead of a sample. Using this method, it is possible to determine only the sum of -Asp, -Glu and NMDA (Tedeschi et al 1994), because -aspartate oxidase oxidizes -Asp, -Glu and NMDA.…”

Section: Enzymatic Colorimetric Methods For the Determination Of -Aspmentioning

confidence: 99%

“…-Asp has been found in the nervous tissue of cephalopods, Octopus vulgaris, Loligo vulgaris and Sepia officinalis (D'Aniello & Giuditta 1977, 1978, D'Aniello et al 1995b, the opisthobranch mollusc, Aplysia fasciata (D'Aniello et al 1992a), and the tunicate, Ciona intestinalis (D'Aniello et al 1992b). Among vertebrates, free -Asp has been found in the nervous tissue of chickens (Neidle & Dunlop 1990), rodents (Dunlop et al 1986, D'Aniello et al 1993a, Hashimoto et al 1993b) and humans (Fisher et al 1991, 1994, Hashimoto et al 1993a. More recently, studies have shown that this enantiomer is also present in other body structures, including the endocrine glands and reproductive organs of the rat (Hashimoto et al 1993b, D'Aniello et al 1996 and in the sexual glands of Octopus vulgaris (D'Aniello et al 1995a).…”

Section: Introductionmentioning

confidence: 99%

D-aspartic acid is implicated in the control of testosterone production by the vertebrate gonad. Studies on the female green frog, Rana esculenta

Fiore¹,

Assisi²,

Botte³

et al. 1998

Journal of Endocrinology

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In the present study we report the occurrence of -aspartic acid (-Asp) in the ovary of the green frog Rana esculenta and its putative involvement in testosterone production by the gonad. In the ovary, -Asp concentrations undergo significant variations during the main phases of the sexual cycle. In spawning females (March), its concentration was low (2·5 1·1 nmol/g ovary) and during the postreproductive period ( June) it increased and reached its peak level (58·0 10·1 nmol/g) in October. In that month, vitellogenesis occurs in a new set of ovarian follicles and continues until the next spring. The concentrations of -Asp in the ovary and of testosterone in the ovary and in the plasma were inversely correlated during the reproductive cycle: when endogenous -Asp was low (March), testosterone was high (36·9 4·8 ng/g ovary; 23·1 2·76 ng/ml plasma) and, in contrast, when the -Asp concentration was high (October), the testosterone concentration was low (0·86 0·21 ng/g ovary and 5·0 1·3 ng/ml plasma). In vivo experiments, consisting of injection of -Asp (2·0 µmol/g body weight) into the dorsal lymphatic sac of adult female frogs, demonstrated that this amino acid accumulates significantly in the ovary. After 3 h, moreover, it caused a decrease in testosterone level in the plasma of about 80%. This inhibition was reversible: within 18 h after the amino acid injection, as the -Asp concentration in the ovary decreased, the testosterone titre was restored in both ovary and plasma.In vitro experiments, conducted in isolated ovarian follicles, confirmed this phenomenon and identified these gonadal components as the putative -Asp targets. Other amino acids (-Asp, -Glu, -Glu, -Ala and -Ala) used instead of -Asp were ineffective.These findings indicate that -Asp is involved in the control of androgen secretion by the ovary in this amphibian species, revealing a more complex system for control of this androgen synthesis than was previously believed to exist.

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“…The enzymes have been suggested to work as detoxifying agents that eliminate D-amino acids derived from both exogenous and endogenous sources. 36) In aquatic animals, D-aspartate oxidase has been known to exist in several fish liver 35) and several tissues of octopus, [36][37][38] and the latter also have D-amino acid oxidase. 36) Both enzyme activities are detected in kidney, liver (hepatopancreas), and intestine of fishes.…”

Section: Metabolic Utilization Of Exogenous D-alanine In Fishmentioning

confidence: 99%