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T Sueoka

Publications and source records attributed to T Sueoka.

At least 19 recordsLinked to original sources
PubMed1996

Yellow marking and pteridine contents in the integument of albino Armadillidium vulgare.

The albino mutant strain in the woodlice, Armadillidium vulgare, was investigated with respect to the yellow patterns on the dorsal integument. Pigment cells were observed with electron microscope in order to determine the cell types of yellow markings. Quantitative analyses of pteridines in the albino were carried out by HPLC. The result indicated that the albino integument contain sepiapterin, biopterin, pterin, isoxanthopterin as in the wild type and the red mutant strain. The total amount of the four pteridines in the albino was about half as much as that in the red phenotype for both males and females, respectively. Males and females showed almost the same totals and ratios of the four pteridines in the albino and red phenotypes. Therefore, pteridine contents in both phenotypes of A. vulgare may not be related to the activity of androgenic gland hormone. Yellow chromatophores of the albino and red phenotypes were morphologically identical, emitting a yellow fluorescence. These cells contained numerous electron-lucent pigment organelles which were similar to pteridine granules of the wild type.

Animals↗
PubMed1994

Phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein kinase C of sepiapterin reductase, the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin.

Sepiapterin reductase, the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin, was stoichiometrically phosphorylated by Ca2+/calmodulin-dependent protein kinase II and protein kinase C (Ca2+/phospholipid-dependent protein kinase) in vitro. Maximal incorporation of phosphate into the enzyme subunit by these was 3.05 +/- 0.05 (n = 4) and 0.74 +/- 0.03 (n = 5) 32P mol per mol enzyme subunit, respectively. The enzyme was not phosphorylated by cyclic nucleotide-dependent protein kinase of either the cAMP-dependent or cGMP-dependent type in this study. Dihydropteridine reductase, another enzyme working in direct supply of tetrahydrobiopterin, was also a good substrate for Ca2+/calmodulin-dependent protein kinase II. Phosphorylation of sepiapterin reductase by these protein kinases modified the kinetic properties of the enzyme. It is likely that these multifunctional Ca(2+)-activated protein kinases may play a role in the regulation of the physiological function of the BH4-generating enzymes in vivo, as was previously found in the case of BH4-requiring enzymes.

Alcohol Oxidoreductases↗
PubMed1992

Role of enzymes in tetrahydrobiopterin biosynthesis: computer analysis of the sequential reaction of the last step.

Computer simulation analysis of the experimental data showed that Cl'-keto PH4 and C2'-keto PH4 were sequential intermediates of the reduction of PPH4 to BH4 by SPR and that the reaction in the last step of the BH4 biosynthesis proceeds as follows: PPH4-->Cl'-keto PH4-->C2'-keto PH4-->BH4 Cl'-keto PH4 is not detectable in the reduction of PPH4 by the purified SPR at neutral pH since isomerization (-->) [8] may occur far more rapidly than the first reduction (-->).

Alcohol Oxidoreductases↗
PubMed1991

Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis.

A full-length cDNA clone for sepiapterin reductase, an enzyme involved in tetrahydrobiopterin biosynthesis, was isolated from a human liver cDNA library by plaque hybridization. The nucleotide sequence of hSPR 8-25, which contained an entire coding region of the enzyme, was determined. The clone encoded a protein of 261 amino acids with a calculated molecular mass of 28,047 daltons. The predicted amino acid sequence of human sepiapterin reductase showed a 74% identity with the rat enzyme. We further found a striking homology between human SPR and carbonyl reductase, estradiol 17 beta-dehydrogenase, and 3 beta-hydroxy-5-ene steroid dehydrogenase, especially in their N-terminal region.

Alcohol Oxidoreductases↗
PubMed1991

Computer studies on the stereostructure and quantum chemical properties of 6-pyruvoyl tetrahydropterin, the key intermediate of tetrahydrobiopterin biosynthesis.

The optimized geometry of the conformation of atoms constituting the 6-pyruvoyl tetrahydropterin molecule, the labile key intermediate of tetrahydrobiopterin biosynthesis, was obtained by molecular orbital calculations within the MINDO/3 framework. The stereostructure of the molecule showing the preferred mode for binding to sepiapterin reductase or pyruvoyl tetrahydropterin reductase was drawn in perspective. The resulting structure with the equatorial staggered configuration of the 6-1',2'-dioxopropyl (pyruvoyl) side chain indicated that O(1') and H(6) were located in the trans position around the C(6)-C(1') bond and that the two vicinal carbonyls in the side chain were fixed in the incomplete trans form. The calculation of atomic charges and LUMO coefficients of these carbonyls suggests that the C2'-carbonyl may be more reactive toward NADPH than the C1'-carbonyl in the enzymatic reaction.

Alcohol Oxidoreductases↗
PubMed1990

The complete amino acid sequence of the mature form of rat sepiapterin reductase.

The partial amino acid sequence of rat sepiapterin reductase was determined using peptides generated by cleavage of the S-carboxyamidomethylated protein with Achromobacter protease I, cyanogen bromide, chymotrypsin or BNPS-skatole. The protein began with N-acetyl methionyl residue at the N-terminus and ended with isoleucyl residue at the C-terminus. The present results essentially coincided with the amino acid sequence predicted from the nucleotide sequence of the cDNA recently reported by Citron et al. (Proc. Natl. Acad. Sci. USA 87, 6436-6440 (1990)), clarified the processing event during the biosynthesis and provided the complete amino acid sequence of the mature form of the enzyme.

Alcohol Oxidoreductases↗
PubMed1989

Biopterin and neopterin in human saliva.

Presence of biopterin and neopterin in human saliva was investigated by HPLC after iodine oxidation in acidic medium. Concentrations of biopterin and neopterin (M +/- SEM) were 1.271 +/- 0.254 and 0.358 +/- 0.075 ng per ml, respectively, in saliva of apparently healthy young male adults, ages 20 to 22 years (n = 9). Nearly identical value of the neopterin/biopterin ratio (0.29 +/- 0.07) was obtained for each of these specimens. Monapterin, the L-threo-isomer of neopterin (0.084 +/- 0.022 ng per ml saliva), and other unconjugated pterins such as xanthopterin, 6-hydroxymethylpterin and pterin were also found in the saliva. These pterins were all detectable in saliva of young female adults with similar levels to those of male saliva. Another fluorescent compound which was identical with 7-iso biopterin in retention time on HPLC was observed in all specimens of normal saliva examined.

Adult↗
PubMed1988

Coenzyme stimulation of isomerase activity of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin.

The 6-lactoyl tetrahydropterin (C1'-keto PH4) isomerase activity of sepiapterin reductase, which was found in our recent work (Katoh and Sueoka (1987) J. Biochem. 101, 275-278) as a novel activity of the enzyme, i.e., the conversion of C1'-keto PH4 to 6-1'-hydroxy-2'-oxopropyl tetrahydropterin (C2'-keto PH4) without coenzymes, could be enhanced by a small amount of NADPH or NADP+. The concentration of NADP+ required for the maximal stimulation was approximately the same as the concentration of the enzyme subunit. When NADP+ was added with the enzyme and C1'-keto PH4 at pH 8.6, the reaction sequence of C1'-keto PH4----C2'-keto PH4----tetrahydrobiopterin (BH4) was observed in the presence of dithioerythritol. These observations suggest that the coenzyme stimulating the isomerase function of sepiapterin reductase may be involved in the two sequential reductions, from pyruvoyl tetrahydropterin to BH4, by causing internal rearrangement of the keto group of the first intermediate, C1'-keto PH4, to form the second one, C2'-keto PH4.

Alcohol Oxidoreductases↗
PubMed1987

Isomerization of 6-lactoyl tetrahydropterin by sepiapterin reductase.

Isomerization of 6-1'-oxo-2'-hydroxypropyl tetrahydropterin (6-lactoyl tetrahydropterin) to 6-1'-hydroxy-2'-oxopropyl tetrahydropterin has been attributed to sepiapterin reductase. The activity is N-acetylserotonin-insensitive and has a well defined pH optimum of 8.6. The product of the reaction was detected on a HPLC chromatogram by means of electrochemical oxidation at 200 mV according to Smith and Nichol (J. Biol. Chem. 261, 2725-2737 (1986]. The C2'-keto structure of the product was confirmed by 1H-NMR spectroscopy.

Alcohol Oxidoreductases↗
PubMed1986

Development of tetrahydrobiopterin and GTP cyclohydrolase in salivary glands of rats.

A significant amount of 5,6,7,8-tetrahydrobiopterin (BH4), an essential cofactor of tyrosine hydroxylase, and the activity of GTP cyclohydrolase (GTP cycl), the first and rate-limiting enzyme in BH4 biosynthesis, were found in rat salivary glands, in which adrenergic transmitters are localized, from day 4 through 56 after birth. About 90 ng of BH4 per g wet weight were determined in the glands (submandibular and sublingual) of adult rats. The levels of them which were maintained from 2 weeks after birth up to the adult stage correlated with a previous finding in the maintenance of catecholamine concentration during the same stage in rat salivary glands.

Aging↗
PubMed1985

Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes.

A homogeneous preparation of sepiapterin reductase, an enzyme involved in the biosynthesis of tetrahydrobiopterin, from rat erythrocytes was found to be responsible for the reduction with NADPH of various carbonyl compounds of non-pteridine derivatives including some vicinal dicarbonyl compounds which were reported in the previous paper (Katoh, S. and Sueoka, T. (1984) Biochem, Biophys. Res. Commun. 118, 859-866) in addition to the general substrate, sepiapterin (2-amino-4-hydroxy-6-lactoyl-7,8-dihydropteridine). The compounds sensitive as substrates of the enzyme were quinones, e.g., p-quinone and menadione; other vicinal dicarbonyls, e.g., methylglyoxal and phenylglyoxal; monoaldehydes, e.g., p-nitrobenzaldehyde; and monoketones, e.g., acetophenone, acetoin, propiophenone and benzylacetone. Rutin, dicoumarol, indomethacin, and ethacrynic acid inhibited the enzyme activity toward either a carbonyl compound of a non-pteridine derivative or sepiapterin as substrate. Sepiapterin reductase is quite similar to general aldo-keto reductases, especially to carbonyl reductase.

Alcohol Oxidoreductases↗
PubMed1985

Dyspropterin, an intermediate formed from dihydroneopterin triphosphate in the biosynthetic pathway of tetrahydrobiopterin.

The structure of dyspropterin, a new name given to an intermediate which is formed from dihydroneopterin triphosphate in the biosynthetic pathway of tetrahydrobiopterin, has been studied. Sepiapterin reductase (EC 1.1.1.153) was found to reduce dyspropterin to tetrahydrobiopterin in the presence of NADPH. Several lines of evidence showing the formation of tetrahydrobiopterin have been presented. Stoichiometric analysis revealed that there is a 1:2 relationship between the production of biopterin and the oxidation of NADPH during the reductase-catalyzed reduction of dyspropterin. The tetrahydrobiopterin production from dyspropterin was enhanced by dihydropteridine reductase (EC 1.6.99.7). Dyspropterin could also serve as a cofactor in phenylalanine hydroxylase (EC 1.14.16.1) system. These results are consistent with the view that dyspropterin is 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin. Based on our findings, the biosynthetic pathway of tetrahydrobiopterin from dihydroneopterin triphosphate has been discussed.

Alcohol Oxidoreductases↗