The relation of d-alanine and alanine racemase activity in molluscs

Yamada, Ayumu; Matsushima, Osamu

doi:10.1016/0305-0491(92)90379-6

Cited by 10 publications

(6 citation statements)

References 12 publications

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“…D-AAs may be endogenously synthesized through enzymatic activity or obtained from exogenous sources. D-alanine (D-Ala) has been observed in microorganisms and mollusks [4,5], crustaceans [6,7] and mammals [8,9], including humans [10]. One reported source in animals is intestinal microorganisms [11,12], which incorporate D-Ala in into their cell walls [13,14].…”

Section: Introductionmentioning

confidence: 99%

d-Alanine in the islets of Langerhans of rat pancreas

Ota

Rubakhin

Sweedler

2014

Biochemical and Biophysical Research Communications

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Relatively high levels of D-alanine (D-Ala), an endogenous D-amino acid, have been found in the endocrine systems of several animals, especially in the anterior pituitary; however, its functional importance remains largely unknown. We observed D-Ala in islets of Langerhans isolated from rat pancreas in significantly higher levels than in the anterior/intermediate pituitary; specifically, 180 ± 60 fmol D-Ala per islet (300 ± 100 nmol/g islet), and 10 ± 2.5 nmol/g of wet tissue in pituitary. Additionally, 12 ± 5% of the free Ala in the islets was in the D-isomer, almost an order of magnitude higher than the percentage of D-Ala found in the pituitary. Surprisingly, glucose stimulation of the islets resulted in D-Ala release of 0.6 ± 0.5 fmol per islet. As D-Ala is stored in islets and released in response to changes in extracellular glucose, D-Ala may have a hormonal role.

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Section: Introductionmentioning

confidence: 99%

d-Alanine in the islets of Langerhans of rat pancreas

Ota

Rubakhin

Sweedler

2014

Biochemical and Biophysical Research Communications

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“…[1][2][3][4][5][6][7][8] Even the distribution of these D-amino acids, however, is still con troversial on various molluscan species. It is not clear whether the distribution of D-amino acids depends on the phylogenetic positions or ecological environments.…”

Section: Introductionmentioning

confidence: 99%

Distribution of Free D-Amino Acids in Bivalve Mollusks and the Effects of Physiological Conditions on the Levels of D- and L-Alanine in the Tissues of the Hard Clam, <i>Meretrix lusoria</i>

Okuma

Abe

1998

Fisheries science

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The distribution of D-amino acids was examined on the tissues of seven species of marine bivalve mollusks belonging to two different subclasses, Pterimorphia and Heterodonta. High concentration of D-alanine was found in all tissues of only Heterodonta and not in the tissues of Pterimorphia except in gills and midgut gland. Several other D-amino acids including D-arginine also occurred in the several tis sues of both groups of bivalves.Along with the salinity stress on the hard clamMeretrix lusoria in 150% seawater, only D and L alanine increased in adductor muscle, gills, and midgut gland. The incorporation of D-alanine from ex ternal seawater was found onlyin gills, hemolymph, and midgut gland of hard clam, and the levels of D and L-alanine inadductor and foot muscles decreased in the seawater containing 50 HIM D-alanine and returned to the control level after recovery innormal seawater.During the starvation of hard clam for 22 days,D and L-alanine as well as other free amino acids decreased considerably in most tissues. The anoxia of hard clam for a week duration gave no large effect on the levels of free amino acids but resulted in the slight increases of D and L-alanine levels after sevendays.

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“…In Section 4 , Section 5 and Section 6 , tabulated lists of the remaining articles according to types of molecules on which these isomerases can catalyze their reactions are discussed. Isomerases acting on carbohydrate molecules ( Table 2 ) [ 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 ] are listed in the first of three tables following with lipids ( Table 3 ) [ 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 ] and amino acids and peptides ( Table 4 ) [ 47 , 48 , 49 , 50 , 51 , 52 , ...…”

Section: Literature Searchmentioning

confidence: 99%

Application-Oriented Marine Isomerases in Biocatalysis

Trincone¹

2020

Marine Drugs

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The class EC 5.xx, a group of enzymes that interconvert optical, geometric, or positional isomers are interesting biocatalysts for the synthesis of pharmaceuticals and pharmaceutical intermediates. This class, named “isomerases,” can transform cheap biomolecules into expensive isomers with suitable stereochemistry useful in synthetic medicinal chemistry, and interesting cases of production of l-ribose, d-psicose, lactulose, and d-phenylalanine are known. However, in two published reports about potential biocatalysts of marine origin, isomerases are hardly mentioned. Therefore, it is of interest to deepen the knowledge of these biocatalysts from the marine environment with this specialized in-depth analysis conducted using a literature search without time limit constraints. In this review, the focus is dedicated mainly to example applications in biocatalysis that are not numerous confirming the general view previously reported. However, from this overall literature analysis, curiosity-driven scientific interest for marine isomerases seems to have been long-standing. However, the major fields in which application examples are framed are placed at the cutting edge of current biotechnological development. Since these enzymes can offer properties of industrial interest, this will act as a promoter for future studies of marine-originating isomerases in applied biocatalysis.

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The relation of d-alanine and alanine racemase activity in molluscs

Cited by 10 publications

References 12 publications

d-Alanine in the islets of Langerhans of rat pancreas

d-Alanine in the islets of Langerhans of rat pancreas

Distribution of Free D-Amino Acids in Bivalve Mollusks and the Effects of Physiological Conditions on the Levels of D- and L-Alanine in the Tissues of the Hard Clam, <i>Meretrix lusoria</i>

Application-Oriented Marine Isomerases in Biocatalysis

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