Studies on Sepiapterin Deaminase from the Silkworm, Bombyx mori

Tsusué, Motoo

doi:10.1093/oxfordjournals.jbchem.a129526

Cited by 28 publications

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“…The granule enzymer is competitively inhibited by 2-amino-4-hydroxypteridine and non-competitively by p-chloromercuribenzoate as shown in Figure 3. Based on the data, Ki values of 3.5 x 10 -5 and 8.0 x 10-4 M were calculated respectively and these coincide with previously described values (6,7) . All strains of silkworm tested had sepiapterin deaminase activity indicating that the enzyme may be essential for the insect.…”

Section: Comparison Of Properties Of Granule Attached Enzyme With Solsupporting

confidence: 83%

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Localization of Sepiapterin Deaminase and Pteridines In the Granules In Epidermal Cells of the Silkworm, Bombyx mori

1990

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SummaryA new method for assay of sepiapterin deaminase (3.5.4.24) activity by use of high performance liquid chromatography (HPLC) was developed. By this sensitive method the enzyme activity in the cell organelle was assayed. After cell fractionation, the enzyme was extracted with deoxycholate from pteridine granules of epidermal cells of the lemon mutant silkworm. On stepwise sucrose gradient centrifugation, most of the enzyme activity localized in the aggregated pteridine granules fraction, while the soluble fraction contained only one fourth of the total enzyme activity. The enzyme in the granule fraction had the same properties as the previously reported sepiapterin deaminase. These data show that the enzyme is localized in pteridine granules in the living cells. The attachment of the enzyme to the granule membrane is rather loose and previous papers studied the enzyme released from the granules.Cell fractionation and morphological observation showed that sepiapterin, sepialumazine and other pteridines were also localized in the granules together with uric acid.

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Section: Comparison Of Properties Of Granule Attached Enzyme With Solsupporting

confidence: 83%

“…The enzyme was purified 3300 fold and details of the properties of the enzyme have been reported. The enzyme is widely distributed in many tissues of the lemon silkworm (7). Later, the enzyme was found in normal strains of the silkworm (8).…”

Section: Introductionmentioning

confidence: 99%

Localization of Sepiapterin Deaminase and Pteridines In the Granules In Epidermal Cells of the Silkworm, Bombyx mori

1990

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“…Tsusue (1967) reported the occurrence of an enzyme in lemon larvae which catalyzed the deamination of sepiapterin to form sepialumazine. Detailed properties of the enzyme were revealed by subsequent work of Tsusue (1971). The occurrence of this same enzyme as well as its product in the normal type silkworm larvae was shown by Tsusue and Mazda (1977).…”

Section: Introductionmentioning

confidence: 82%

“…1963). Finally, although it is not known whether sepialumazine is further metabolized or not, a decrease of the pigment by further metabolism or excretion of the pigment through the malpighian tubules (Tsusue 1971) may also be a controlling force. Since many factors may be involved in the accumulation of the pigment, it is natural that the levels of larval integument sepialumazine are not simply proportional to the activity of sepiapterin deaminase.…”

Section: Discussionmentioning

confidence: 99%

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Studies on the genetical and biochemical properties of the Kiuki mutant of the silkworm, Bombyx mori.

Mazda

Tsusué

Sakate

et al. 1981

The Japanese journal of genetics

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Genetic studies of the Bombyx mori Kiuki mutant were made on the segregation of the F2 and BFl phenotypes. Assay of sepialumazine in these phenotypes revealed that the Kiuki mutant is an incomplete dominant. A symbol Sel is given to the mutant gene. Enzymatic studies on F2 progeny showed that the yellow larval integument colour characteristic of the mutant, which is due to accumulation of sepialumazine, is dependent on the activity of sepiapterin deaminase. Linkage test showed that the Sel is independent of the so far established 23 linkage groups but represents one of the still unknown group among remaining five chromosomes.

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Biochemie der Pteridine

Rembold

Gyure

1972

Angewandte Chemie

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Chemische Labilitat und eine zumeist ungewohnlich niedrige biologische Konzentration sind die Hauptgriinde, warum die Biochemie der offenbar ubiquitaren Pteridine erst im Verlauf der letzten funfzehn Jahre experimentell zuganglich wurde. Neben schonenden Isolierungsmethoden brachte vor allem die Isotopentechnik Erkenntnisse uber Biosynthese, Anabolismus und Katabolismus dieser Stoflklasse. Hydrierte Pterine sind Cofaktoren mehrerer mischfunktioneller Oxygenasen und sind am zellularen Elektronentransport beteiligt. Das physiologische Verhalten, das negative Redoxpotential und histoautoradiographische Daten sprechen fur eine Rcihe weiterer, bisher noch unbekannter katalytischer Funktionen der Pteridine im Zellstoffwechsel.

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Studies on Sepiapterin Deaminase from the Silkworm, Bombyx mori

Cited by 28 publications

References 0 publications

Localization of Sepiapterin Deaminase and Pteridines In the Granules In Epidermal Cells of the Silkworm, Bombyx mori

Localization of Sepiapterin Deaminase and Pteridines In the Granules In Epidermal Cells of the Silkworm, Bombyx mori

Studies on the genetical and biochemical properties of the Kiuki mutant of the silkworm, Bombyx mori.

Biochemie der Pteridine

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