Occurrence of Two Different Enzymes in the Silkworm, Bombyx mori, to reduce Folate and Sepiapterin

Matsubara, Masako; Tsusué, Motoo; Akino, Miki

doi:10.1038/199908a0

Cited by 31 publications

(10 citation statements)

References 6 publications

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“…Previous studies have shown that a large amount of yellow pteridines, SP, and sepialumazine accumu-lated in the integument of the lem larvae (13,14). In addition, SPR activity was absent in the lem mutant silkworms (9). Lack of SPR activity accelerates the accumulation of SP and sepialumazine (Fig.…”

Section: Tetrahydrobiopterin (Bh4)mentioning

confidence: 99%

“…SPR has been previously purified from the silkworm Bombyx mori, and its activity in the fat body of normal larvae has been characterized (9,10). However, the SPR gene (BmSpr) has not been identified yet in B. mori.…”

Section: Tetrahydrobiopterin (Bh4)mentioning

confidence: 99%

“…Strains-Previous studies showed that SPR deficiency is involved in abnormal body coloration of the lem (lem l ) mutant (9,13,14). To examine whether the B. mori SPR gene (BmSpr) corresponds to lem (lem l ), we first determined a full-length cDNA sequence of BmSpr using expressed sequence tag data bases (16).…”

Section: Characterization Of Bmspr Gene In Normal and Mutantmentioning

confidence: 99%

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The Silkworm Mutant lemon (lemon lethal) Is a Potential Insect Model for Human Sepiapterin Reductase Deficiency

Meng

Katsuma

Daimon

et al. 2009

Journal of Biological Chemistry

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Tetrahydrobiopterin (BH4) is an essential cofactor for aromatic acid hydroxylases, which control the levels of monoamine neurotransmitters. BH4 deficiency has been associated with many neuropsychological disorders. An inherited defect in BH4 biosynthesis is caused by the deficiency of sepiapterin reductase (SPR), which catalyzes the biosynthesis of BH4 from guanosine triphosphate at the terminal step. The human SPR gene has been mapped at the PARK3 locus, which is related to the onset of Parkinson disease. In this study, we report that mutant strains, lemon (lem) and its lethal allele lemon lethal (lem 1 ) with yellow body coloration, of the silkworm Bombyx mori could be used as the first insect model for human SPR deficiency diseases. We demonstrated that mutations in the SPR gene (BmSpr) were responsible for the irregular body coloration of lem and lem l . Moreover, biochemical analysis revealed that SPR activity in lem l larvae was almost completely diminished, resulting in a lethal phenotype that the larvae cannot feed and that die immediately after the first ecdysis. Oral administration of BH4 and dopamine to lem l larvae effectively increased their survival rates and feeding abilities. Our data demonstrate that BmSPR plays a crucial role in the generation of BH4, and monoamine neurotransmitters in silkworms and the lem (lem l ) mutant strains will be an invaluable resource to address many questions regarding SPR and BH4 deficiencies.

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Section: Tetrahydrobiopterin (Bh4)mentioning

confidence: 99%

Section: Tetrahydrobiopterin (Bh4)mentioning

confidence: 99%

Section: Characterization Of Bmspr Gene In Normal and Mutantmentioning

confidence: 99%

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The Silkworm Mutant lemon (lemon lethal) Is a Potential Insect Model for Human Sepiapterin Reductase Deficiency

Meng

Katsuma

Daimon

et al. 2009

Journal of Biological Chemistry

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“…Later, sepiapterin was shown to be present only in the lemon mutant and a yellow pteridine, present in all the other strains and mutants, was identified as sepialumazine (1). Sepiapterin deaminase which catalyzes the hydrolitic deamination of sepiapterin to form sepialumazine was first found (5) in the integument of lemon silkworm because the mutant lacked sepiapterin reductase (6). The enzyme was purified 3300 fold and details of the properties of the enzyme have been reported.…”

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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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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“…Tsujita (1961) explained the properties of the multiple allele by stating that the lemon lethal mutant was completely deficient in sepiapterin reductase and the lemon mutant had a decreased level of the enzyme. Subsequent studies of the lemon mutant, however, have failed to detect any sepiapterin reductase activity (Matsubara et al 1963;Mazda et al 1980). Tsusue and Akino (1965) isolated a major yellow pigment from the integument of lemon silkworms and identified it as 7,8-dihydro-2-amino-4-hydroxy-6-lactylpteridine (sepiapterin).…”

Section: Introductionmentioning

confidence: 99%

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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Occurrence of Two Different Enzymes in the Silkworm, Bombyx mori, to reduce Folate and Sepiapterin

Cited by 31 publications

References 6 publications

The Silkworm Mutant lemon (lemon lethal) Is a Potential Insect Model for Human Sepiapterin Reductase Deficiency

The Silkworm Mutant lemon (lemon lethal) Is a Potential Insect Model for Human Sepiapterin Reductase Deficiency

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.

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